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(DY-681)-Gly-Arg-Gln-Ser-Arg-Ala-Ile-Lys (DY-681)-NH + H2O
?
-
synthetic substrate, peptide sequence is derived from one of the preferred matriptase cleavage sequences, P4(Arg/Lys)-P3(Xxx)-P2(Ser)-P1(Arg)-P10(Ala), where Xxx is a nonbasic amino acid
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ala-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Gly-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ser-Tyr(3-NO2)-NH2
-
-
-
?
acetyl-L-lysyl-L-threonyl-L-lysyl-L-glutaminyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-4-methyl-coumaryl-7-amide + H2O
acetyl-Lys-Thr-Lys-Gln-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-4-methylcoumarin-7-amide + H2O
?
-
substrate almost matches the P5 to P1 residues of matriptase zymogen: P5(Thr)-P4(Lys)-P3(Gln)-P2(Ala)-P1(Arg). The hydrolysis of the substrate is expected to mimic the situation of activation cleavage of matriptase zymogen
-
-
?
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-methyl-coumaryl-7-amide + H2O
acetyl-Lys-Thr-Lys-Gln-Leu-Arg + 7-amino-4-methylcoumarin
-
relative activity: 19% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 16% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
acid-sensing ion channel 1 + H2O
?
-
the matriptase recognition sites Arg-145, Lys-185, and Lys-384 are identified in the specific substrate acid-sensing ion channel 1
-
-
?
alphaEbeta7 integrin + H2O
?
-
-
-
-
?
alphaEbeta7integrin + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
Arg-Xaa-Ser-Arg-Ala + H2O
Arg-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
benzoyl-L-arginine-4-methylcoumaryl-7-amide + H2O
benzoyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gln-Ala-Arg-4-nitroanilide + H2O
Boc-Gln-Ala-Arg + 4-nitroaniline
-
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gln-Ala-Arg + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide + H2O
butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
CUB-domain-containing protein 1 + H2O
?
-
-
-
?
denatured collagen + H2O
?
-
-
-
-
?
dumpy + H2O
?
i.e. a zona pellucida-domain protein
-
-
?
EpCAM + H2O
?
-
i.e. epithelial cell adhesion molecule CD326
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
fetuin-A + H2O
?
a liver-derived alpha2-Heremans-Schmid glycoprotein from plasma, processing into a two-chain form, cleavage sites are Arg and Lys residues in the 40 amino acid sequence of the linker connceting the two peptides
-
-
?
Fibrinogen + H2O
?
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
Glu-Gly-Arg-p-nitroanilide + H2O
?
-
substrate activity assay
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
H-Glu-Gly-Arg-p-nitroanilide + H2O
H-Glu-Gly + Arg-p-nitroanilide
-
low activity
-
-
?
hemojuvelin (furin site) + H2O
?
-
-
-
?
hepatocyte growth factor + H2O
?
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
HGF/SF + H2O
?
-
i.e. hepatocyte growth factor/scatter factor, growth factor
-
-
?
Ile-Pro-Arg-p-nitroanilide + H2O
Ile-Pro + Arg-p-nitroanilide
-
-
-
?
influenza A H1 virus hemagglutinin + H2O
?
the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range
-
-
?
insulin growth factor binding protein-related protein-1 + H2O
?
-
cleaved by the soluble form of active matripase
-
-
?
insulin-like growth factor binding protein related protein-1
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
insulin-like growth factor binding-related protein-1 + H2O
?
Lys-Xaa-Ser-Arg-Ala + H2O
Lys-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
matriptase + H2O
?
-
-
-
-
?
matriptase-2 + H2O
?
autocatalysis
-
-
?
matrix metalloprotease-3 + H2O
?
methyl-sulfonyl-D-cyclo-hexyltyrosyl-glycyl-L-arginine-4-nitroanilide + H2O
?
-
-
-
?
methylsulfonyl-D-cyclohexyltyrosyl-glycyl-arginine-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexyltyrosyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine + p-nitroaniline
-
-
-
-
?
MSP-1 + H2O
?
-
i.e. macrophage-stimulating protein 1, a growth factor
-
-
?
N-Ala-Ala-Ala-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxy-carbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
N-tert-butoxy-carbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg 7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
N2-t-butyloxycarbonyl-QNR-7-amido-4-methylcoumarin + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
plasminogen + H2O
?
-
-
?
pro matrix metalloproteinase 1 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro matrix metalloproteinase 3 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
pro-form influenza hemagglutinin H2 + H2O
mature influenza hemagglutinin H2 + ?
subtype H2N2
-
-
?
pro-form influenza hemagglutinin H3 + H2O
mature influenza hemagglutinin H3 + ?
subtype H3N2
-
-
?
pro-form matriptase + H2O
mature matriptase + ?
autocatalytic activation
-
-
?
pro-hepatocyte growth factor + H2O
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF + H2O
?
-
matriptase is an efficient activator of hepatocyte growth factor
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
pro-urokinase plasminogen activator + H2O
?
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
pro-urokinase-type plasminogen activator + H2O
?
profilaggrin + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
proform acid-sensing ion channel 1 + H2O
mature acid-sensing ion channel 1 + ?
-
-
-
-
?
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform G-protein-coupled protease activated receptor-2 + H2O
mature G-protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform hepatocyte growth factor + H2O
mature hepatocyte growth factor + ?
-
-
-
-
?
proform matriptase + H2O
mature matriptase
matriptase is expressed as a zymogen and is autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence
-
-
?
proform matriptase-2 + H2O
mature matriptase
matriptase-2 is expressed as zymogen form and undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
-
-
?
proform platelet-derived growth factor-D + H2O
mature platelet-derived growth factor-D + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
proform urokinase-type plasminogen activator + H2O
mature urokinase-type plasminogen activator + ?
-
-
-
-
?
prostasin + H2O
activated prostasin + ?
protease activated receptor 2 + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
protease-activated receptor-2 + H2O
?
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
-
-
-
-
?
RAARVVGG + H2O
RAAR + VVGG
-
-
-
-
?
RLARVVGG + H2O
RLAR + VVGG
-
-
-
-
?
RQARAVGG + H2O
RQAR + AVGG
-
-
-
-
?
RQARQVGG + H2O
RQAR + QVGG
-
-
-
-
?
RQARVVGG + H2O
RQAR + VVGG
-
-
-
-
?
RQARYVGG + H2O
RQAR + YVGG
-
-
-
-
?
RQLRVVGG + H2O
RQLR + VVGG
-
-
-
-
?
RQRRVVGG + H2O
RQRR + VVGG
-
-
-
-
?
RQYRVVGG + H2O
RQYR + VVGG
-
-
-
-
?
RRARVVGG + H2O
RRAR + VVGG
-
-
-
-
?
RYARVVGG + H2O
RYAR + VVGG
-
-
-
-
?
serine protease uPA + H2O
?
single-chain urokinase-type plaminogen activator + H2O
?
-
is activated by matriptase
-
?
single-chain urokinase-type plasminogen activator + H2O
?
-
sc-uPA
-
-
?
stromelysin + H2O
?
-
MMP-3
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
Suc-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
Suc-Ala-Ala-Pro + Arg-p-nitroanilide
-
low activity
-
-
?
Suc-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Lys + p-nitroaniline
-
-
-
-
?
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin + H2O
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Asp-Pro-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
relative activity: 66% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 69% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
enzymatic activity assay
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
relative activity: 100%, using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase) or engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-Glu-Gly-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
relative activity: 29% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 31% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
activity assay
-
-
?
t-butyloxycarbonyl-L-glutamyl-L-alanyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Gly-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
relative activity: 28% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 28% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
relative activity: 12% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 13% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-L-prolyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-4-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
TMPRSS6 + H2O
?
autocleavage site: PSSR/IVGG
-
-
?
tracheal-prostasin zymogen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
VPEKQTRGL + H2O
?
influenza hemagglutinin H3 cleavage site peptide mimic
-
-
?
Xaa-Arg-Ser-Arg-Ala + H2O
Xaa-Arg-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
Xaa-Lys-Ser-Arg-Ala + H2O
Xaa-Lys-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
Z-Phe-Val-Arg-p-nitroanilide + H2O
Z-Phe-Val + Arg-p-nitroanilide
-
-
-
-
?
additional information
?
-
Boc-QAR-Amc + H2O
?
-
-
-
?
Boc-QAR-Amc + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
CDCP1 + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
-
fragments of 135 and 110 kDa, EGFR110 is constitutively active, while EGFR135 is inactive in terms of tyrosine phosphorylation
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
the epidermal growth factor receptor, EGFR is proteolytically cleaved in the N-terminal extracellular domain by the matriptase-prostasin serine protease cascade in cultured epithelial cells
fragments of 135 and 110 kDa, no longer responsive to EGF stimulation
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
filaggrin + H2O
?
-
-
-
-
?
filaggrin + H2O
?
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
?
hemojuvelin + H2O
?
inactivation
-
-
?
hemojuvelin + H2O
?
a glycosylphosphatidylinositol-linked membrane protein. inactivation
-
-
?
hemojuvelin + H2O
?
bone morphogenetic protein co-receptor
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, physiological function, overview
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
activation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
the enzyme is involved in tumor progression and metastasis
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
an adhesion factor
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding protein related protein-1
?
-
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein related protein-1
?
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
activation
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
proteolytical cleavage on the cell surface of a a single-chain IGFB-rP1 to a two-chain form, consisting of a 25 kDa chain and an 8 kDa chain, changing its biological in modulation of cellular adhesion and growth in an IGF/insulin-dependent or independent manner, as well as tumor-suppressive activity, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium, overview
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1 or angiomodulin or mac25
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
matrix metalloprotease-3 + H2O
?
-
-
-
-
?
matrix metalloprotease-3 + H2O
?
-
activation
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
PAR-2 + H2O
?
-
-
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation, prostasin is also a regulator of the epidermal sodium channel like matriptase
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
-
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
preferred subtype H1N1
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
-
pro-HGF/SF
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF/SF
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
soluble matriptase efficiently converts soluble prostasin zymogen to an active two-chain form, prostasin is exclusively found in the zymogen form in matriptase-deficient epidermis
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
the channel activating protease prostasin/CAP1/PRSS8, a glycosylphosphatidylinositol-anchored membrane serine protease, is co-localized with matriptase
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
activation, cleavage after Arg12 within the amino acid sequence QPR12-ITG
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
cleavage after Arg12 within the amino acid sequence QPR12-ITG
-
-
?
pro-uPA + H2O
?
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
the enzyme is involved in tumor progression and metastasis
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase, when expressed without matriptase, prostasin remains in the zymogen form and no prostasin-PN-1 complex is formed, overview
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase
-
-
?
prostatin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
-
PAR2
-
-
?
protease-activated receptor-2
?
PAR2
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
activation
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
i.e. MMP-3 or matrix metalloproteinase-3, recombinant human substrate, activation
-
-
?
trask + H2O
?
-
-
-
-
?
trask + H2O
?
-
a transmembrane glycoprotein
-
-
?
trask + H2O
?
-
i.e. CDCP1 or SIMA 135, a transmembrane glycoprotein
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation on THP-1 cells
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
-
enzyme inactivation by HAI-1 is required for epithelial integrity of the zebrafish epidermis, Hai1 and matriptase1a are involved in regualtion of skin homeostasis and remodeling, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
-
?
additional information
?
-
-
cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
-
?
additional information
?
-
-
preferred amino acid residues: at P4 position: Lys and Arg, at P3 position: basic residues and Glu, at P2 position: Gly, Ser and Phe
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
involved in multiple aspects of tumor progression and cancer invasion
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, overview
-
-
?
additional information
?
-
-
matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
-
?
additional information
?
-
-
matriptase cleaves and activates proteins implicated in the progression of cancer
-
-
?
additional information
?
-
-
matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
-
-
?
additional information
?
-
-
matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth, matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression, that is unopposed by HAI-1, potently promotes carcinogenesis and metastatic dissemination in animal models, matriptase dramatically increases apoptosis of immature thymocytes in the thymus, leading to thymocyte depletion, physiological functions of matriptase, the enzyme is involved in epithelial carcinogenesis, detailed overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease and highly regulated in leukocytes, and correlates with the presence of active uPA on their surface, it is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments, overview
-
-
?
additional information
?
-
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
mutation in gene ST14 causes autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is a type II transmembrane serine protease implicated in a range of cancers including those of the breast, cervix, ovaries, prostate, colon and gastrointestinal tract, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
physiological regulatory mechanisms, overview, matriptase is involved in cancer invasion and metastasis by serving as a membrane activator directly on cancer cell surfaces to recruit and activate urokinase type plasminogen activator, MMP-3, hepatocyte growth factor, and insulin-like growth factor binding protein-related protein-1, all of which are important in various aspects of cancers, including extracellular matrix degradation, adhesion, cellular motility and tumor vascularization
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation
-
-
?
additional information
?
-
-
the G827R mutation in patients with autosomal recessive ichthyosis with hypotrichosis leads to the expression of an inactive protease
-
-
?
additional information
?
-
-
matriptase binds cytosolic proteins to regulate enzymatic activity and cellular distribution of the protease
-
-
?
additional information
?
-
-
matriptase performs autoactivation
-
-
?
additional information
?
-
-
R/KXSR-/-A is the cleavage sequence of matriptase
-
-
?
additional information
?
-
-
the enzyme is a type II transmembrane serine protease
-
-
?
additional information
?
-
-
the enzyme performs autoproteolysis
-
-
?
additional information
?
-
-
matriptase does not cleave acid-sensing ion channel 2
-
-
?
additional information
?
-
-
the P1 residue for MT-SP1 substrates is either arginine or lysine
-
-
?
additional information
?
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
-
-
?
additional information
?
-
-
matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
-
-
?
additional information
?
-
the enzyme shows low rate cleavage of the A/Japan/305/57 (H2) peptide mimic (VPQIESRGL) compared to that for the H1 consensus
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation, involved in lipid matrix formation, cornified envelope morphogenesis and stratum corneum desquamation
-
?
additional information
?
-
-
a matriptase-prostasin zymogen activation cascade may be functionally operative in multiple epithelial tissues, but matriptase promotes epithelial carcinogenesis independent of prostasin, overview
-
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, the protease is essential for postnatal survival, matriptase has pleiotropic functions in the development of the epidermis, hair follicles, and cellular immune system, the protease is essential for postnatal survival, overview
-
-
?
additional information
?
-
-
matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development, mechanism, overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease, that is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formation, and acquisition of epidermal barrier function, matriptase, an autoactivating protease, acts upstream from prostasin to initiate a zymogen cascade that is essential for epidermal differentiation, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is critical for proper epidermal development and postnatal survival, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation, spatial dysregulation of matriptase leads to the activation of the PI3K-Akt signaling pathway, and dysregulated matriptase synergizes strongly with activated ras to promote epithelial carcinogenesis
-
-
?
additional information
?
-
-
matriptase performs autoactivation
-
-
?
additional information
?
-
-
R/KXSR-/-A is the cleavage sequence of matriptase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acid-sensing ion channel 1 + H2O
?
-
the matriptase recognition sites Arg-145, Lys-185, and Lys-384 are identified in the specific substrate acid-sensing ion channel 1
-
-
?
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide + H2O
butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
the epidermal growth factor receptor, EGFR is proteolytically cleaved in the N-terminal extracellular domain by the matriptase-prostasin serine protease cascade in cultured epithelial cells
fragments of 135 and 110 kDa, no longer responsive to EGF stimulation
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
growth factor macrophage-stimulating protein 1 + H2O
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
HGF/SF + H2O
?
-
i.e. hepatocyte growth factor/scatter factor, growth factor
-
-
?
influenza A H1 virus hemagglutinin + H2O
?
the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range
-
-
?
insulin-like growth factor binding protein related protein-1
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
insulin-like growth factor binding-related protein-1 + H2O
?
matriptase-2 + H2O
?
autocatalysis
-
-
?
matrix metalloprotease-3 + H2O
?
-
activation
-
-
?
MSP-1 + H2O
?
-
i.e. macrophage-stimulating protein 1, a growth factor
-
-
?
pro matrix metalloproteinase 1 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro matrix metalloproteinase 3 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation, prostasin is also a regulator of the epidermal sodium channel like matriptase
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
-
-
-
?
pro-form matriptase + H2O
mature matriptase + ?
autocatalytic activation
-
-
?
pro-hepatocyte growth factor + H2O
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF + H2O
?
-
matriptase is an efficient activator of hepatocyte growth factor
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
pro-urokinase-type plasminogen activator + H2O
?
profilaggrin + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform hepatocyte growth factor + H2O
mature hepatocyte growth factor + ?
-
-
-
-
?
proform matriptase + H2O
mature matriptase
matriptase is expressed as a zymogen and is autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence
-
-
?
proform matriptase-2 + H2O
mature matriptase
matriptase-2 is expressed as zymogen form and undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
-
-
?
proform prostasin + H2O
mature prostasin + ?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase, when expressed without matriptase, prostasin remains in the zymogen form and no prostasin-PN-1 complex is formed, overview
-
-
?
protease activated receptor 2 + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
proteinase-activated receptor 2 + H2O
?
-
-
-
-
?
serine protease uPA + H2O
?
single-chain urokinase-type plasminogen activator + H2O
?
-
sc-uPA
-
-
?
stromelysin + H2O
?
-
MMP-3
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
activation
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
additional information
?
-
CDCP1 + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
?
hemojuvelin + H2O
?
a glycosylphosphatidylinositol-linked membrane protein. inactivation
-
-
?
hemojuvelin + H2O
?
bone morphogenetic protein co-receptor
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, physiological function, overview
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
activation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
the enzyme is involved in tumor progression and metastasis
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
an adhesion factor
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding protein related protein-1
?
-
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein related protein-1
?
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
activation
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
proteolytical cleavage on the cell surface of a a single-chain IGFB-rP1 to a two-chain form, consisting of a 25 kDa chain and an 8 kDa chain, changing its biological in modulation of cellular adhesion and growth in an IGF/insulin-dependent or independent manner, as well as tumor-suppressive activity, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium, overview
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
-
pro-HGF/SF
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF/SF
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
soluble matriptase efficiently converts soluble prostasin zymogen to an active two-chain form, prostasin is exclusively found in the zymogen form in matriptase-deficient epidermis
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
the channel activating protease prostasin/CAP1/PRSS8, a glycosylphosphatidylinositol-anchored membrane serine protease, is co-localized with matriptase
-
-
?
pro-uPA + H2O
?
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
the enzyme is involved in tumor progression and metastasis
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
-
PAR2
-
-
?
protease-activated receptor-2
?
PAR2
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
trask + H2O
?
-
-
-
-
?
trask + H2O
?
-
a transmembrane glycoprotein
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation on THP-1 cells
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
-
enzyme inactivation by HAI-1 is required for epithelial integrity of the zebrafish epidermis, Hai1 and matriptase1a are involved in regualtion of skin homeostasis and remodeling, overview
-
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
involved in multiple aspects of tumor progression and cancer invasion
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, overview
-
-
?
additional information
?
-
-
matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
-
?
additional information
?
-
-
matriptase cleaves and activates proteins implicated in the progression of cancer
-
-
?
additional information
?
-
-
matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
-
-
?
additional information
?
-
-
matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth, matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression, that is unopposed by HAI-1, potently promotes carcinogenesis and metastatic dissemination in animal models, matriptase dramatically increases apoptosis of immature thymocytes in the thymus, leading to thymocyte depletion, physiological functions of matriptase, the enzyme is involved in epithelial carcinogenesis, detailed overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease and highly regulated in leukocytes, and correlates with the presence of active uPA on their surface, it is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments, overview
-
-
?
additional information
?
-
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
mutation in gene ST14 causes autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is a type II transmembrane serine protease implicated in a range of cancers including those of the breast, cervix, ovaries, prostate, colon and gastrointestinal tract, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
physiological regulatory mechanisms, overview, matriptase is involved in cancer invasion and metastasis by serving as a membrane activator directly on cancer cell surfaces to recruit and activate urokinase type plasminogen activator, MMP-3, hepatocyte growth factor, and insulin-like growth factor binding protein-related protein-1, all of which are important in various aspects of cancers, including extracellular matrix degradation, adhesion, cellular motility and tumor vascularization
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation
-
-
?
additional information
?
-
-
the G827R mutation in patients with autosomal recessive ichthyosis with hypotrichosis leads to the expression of an inactive protease
-
-
?
additional information
?
-
-
matriptase does not cleave acid-sensing ion channel 2
-
-
?
additional information
?
-
-
the P1 residue for MT-SP1 substrates is either arginine or lysine
-
-
?
additional information
?
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
-
component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation, involved in lipid matrix formation, cornified envelope morphogenesis and stratum corneum desquamation
-
?
additional information
?
-
-
a matriptase-prostasin zymogen activation cascade may be functionally operative in multiple epithelial tissues, but matriptase promotes epithelial carcinogenesis independent of prostasin, overview
-
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, the protease is essential for postnatal survival, matriptase has pleiotropic functions in the development of the epidermis, hair follicles, and cellular immune system, the protease is essential for postnatal survival, overview
-
-
?
additional information
?
-
-
matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development, mechanism, overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease, that is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formation, and acquisition of epidermal barrier function, matriptase, an autoactivating protease, acts upstream from prostasin to initiate a zymogen cascade that is essential for epidermal differentiation, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is critical for proper epidermal development and postnatal survival, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation, spatial dysregulation of matriptase leads to the activation of the PI3K-Akt signaling pathway, and dysregulated matriptase synergizes strongly with activated ras to promote epithelial carcinogenesis
-
-
?
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(1r,4r)-4-amino-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)cyclohexanecarboxamide
-
(1r,4r)-4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
-
(2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
(2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
1-(2-aminoethyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
-
1-(3,5-bis(4-carbamimidoylphenoxy)benzoyl)piperidine-4-carboxylic acid
-
1-(3-aminopropanoyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
-
1-(N-[[3-(b-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-3-carboxamide
-
-
1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-4-carboxamide
-
-
1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine
-
2-(L-alanyl-L-arginyl)-1,3-benzothiazole
-
2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide
-
3,5-bis(4-carbamimidoylphenoxy)-N-((4-hydroxycyclohexyl)methyl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-(1-(2-hydroxyethyl)piperidin-4-yl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-(4-fluorophenyl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-(4-hydroxycyclohexyl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-(4-methylcyclohexyl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-(cyclohexylmethyl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-cyclohexylbenzamide
-
3,5-bis(4-carbamimidoylphenoxy)benzamide
-
3-(3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl)benzenecarboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
3-[(2R)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2R)-3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]propyl]benzenecarboximidamide
-
-
3-[(2S)-2-([[3-(4-aminobutyl)phenyl]sulfonyl]amino)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-2-[[(2',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-(4-[2-(methylcarbamoyl)aminoethyl]piperidin-1-yl)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(1H-indol-5-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(2-methylpyrimidin-4-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[4'-(1-methylethoxy)biphenyl-3-yl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(biphenyl-3-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropoxy]benzenecarboximidamide
higher cytotoxic effect, enzyme-bound structure, crystal structure analysis, overview
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[([3-[(3-aminopropyl)amino]phenyl]sulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2',4'-dichlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-methoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4-cyclohexylphenyl)sulfonyl]amino]-3-oxopropoxy]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
higher cytotoxic effect
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-3-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-4-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(4-aminobutanoyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
-
3-[(2S)-3-[4-(b-alanyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
-
3-[(2S)-3-[4-(N-carbamimidoyl-b-alanyl)piperazin-1-yl]-3-oxo-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propyl]benzenecarboximidamide
-
3-[3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
4,4'-((5-(1,2,3,4-tetrahydroisoquinoline-2-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(4-(2-aminoethyl)piperidine-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(4-fluorophenylsulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(decahydroquinoline-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(naphthalene-2-sulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-[(3-[[(4-fluorophenyl)sulfonyl]amino]pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide
-
4,4'-[(5-aminobenzene-1,3-diyl)bis(oxy)]dibenzenecarboximidamide
-
4,4'-[benzene-1,4-diylbis(oxy)]dibenzenecarboximidamide
binding structure, overview
4-(1-[3-carbamimidoyl-N-[(3-pyrrolidin-1-ylphenyl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethoxybiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
4-(1-[N-[(4'-tert-butylbiphenyl-3-yl)sulfonyl]-3-carbamimidoyl-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(2-aminoethyl)-benzenesulfonylfluoride hydrochloride
-
AEBSF
4-(2-aminoethyl)-benzosulphonylfluoride
nonselective inhibitor
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
inhibition of IGFBP-rP1 processing
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-[[(4-cyclohexylphenyl)sulfonyl]amino]propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitor reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-aminobenzamidine
-
weak competitive inhibition, competition assay with antibody inhibitors, overview
4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
-
4-[(2-[[(2S)-6-carbamimidamido-1-oxohexan-2-yl]amino]-2-oxoethyl)carbamoyl]-6-methoxy-6-oxo-4-[3-(prop-1-en-2-yl)benzyl]hexanoic acid
-
4-[1-(3-carbamimidoyl-N-[[3-(1H-imidazol-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperazin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperidin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(6-oxopyridazin-1(6H)-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoic acid
-
-
4-[4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazin-1-yl]-N-methyl-4-oxobutanamide
-
-
9-fluorenylmethyloxycarbonyl-GR-ketobenzothiazole
potent and selective inhibitor for matriptase over hepsin
alpha1 proteinase
-
formation of a stable inhibitor complex
-
alpha1-antitrypsin
-
AAT
-
anti-matriptase LDL receptor domain 3-specific monoclonal antibodies
-
complete inhibition of enzyme activation
-
antisense-matripase
-
significantly reduces matripase protein expression by 70-80%, anti-tumoral activity on HRA cells intraperitoneal injected into nude mice
-
ARCTKSIPPICFPD
a mutant of sunflower trypsin inhibitor-18
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
-
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
-
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
-
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
-
Bovine pancreatic trypsin inhibitor
-
BPTI
-
CJ-730
-
3-amidinophenylalanine-based inhibitor CJ-730, completely inhibits pro-HGF activation in PC3 cells
CVS-3983
a selective arginal-derived matriptase inhibitor
D-hTyr-Ala-4-amidinobenzylamide
compound has a 10fold reduced activity against thrombin and factor Xa
diisopropylfluorophosphate
-
complete inhibition at 5 mM
ethyl (3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)carbamate
-
ethyl 4-(3,5-bis(4-carbamimidoylphenoxy)benzamido)piperidine-1-carboxylate
-
ethyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
GACTKSIPPICFPD
a mutant of sunflower trypsin inhibitor-17
GAVCPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGACPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGRCPKALKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGRCPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCAKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPAILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKALKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKIAKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILAKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKACRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGAGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGACGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGYCASGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGYCGAGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKRLKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPRILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GKCTKSIPPICFPD
a mutant of sunflower trypsin inhibitor-6
GRCAKSIPPICFPD
a mutant of sunflower trypsin inhibitor-16
GRCTASIPPICFPD
a mutant of sunflower trypsin inhibitor-15
GRCTKAIPPICFPD
a mutant of sunflower trypsin inhibitor-14
GRCTKSAPPICFPD
a mutant of sunflower trypsin inhibitor-13
GRCTKSAPPRCFPD
a mutant of sunflower trypsin inhibitor-1
GRCTKSIAPICFPD
a mutant of sunflower trypsin inhibitor-12
GRCTKSIPAICFPD
a mutant of sunflower trypsin inhibitor-11
GRCTKSIPPACFPD
a mutant of sunflower trypsin inhibitor-10
GRCTKSIPPDCFPD
a mutant of sunflower trypsin inhibitor-3
GRCTKSIPPGCFPD
a mutant of sunflower trypsin inhibitor-2
GRCTKSIPPICAPD
a mutant of sunflower trypsin inhibitor-9
GRCTKSIPPICFAD
a mutant of sunflower trypsin inhibitor-8
GRCTKSIPPICFPA
a mutant of sunflower trypsin inhibitor-7
GRCTKSIPPKCFPD
a mutant of sunflower trypsin inhibitor-0
GRCTKSIPPRCFPD
a mutant of sunflower trypsin inhibitor-1
GRCTKSRPPICFPD
a mutant of sunflower trypsin inhibitor-4
GRCTRSIPPICFPD
a mutant of sunflower trypsin inhibitor-5
HAI-1
-
inhibitor of matriptase in skin
hepatcyte growth factor activator inhibitor-1
-
in normal skin matriptase is complexed to hepatcyte growth factor activator inhibitor-1 wheras in squamous cell carcinoma the enzyme is present in an unassociated form
-
hepatocyte activation inhibitor 1
HAI-1, inhibition of matriptase
-
hepatocyte growth factor activator inhibitor
-
hepatocyte growth factor activator inhibitor 1
-
hepatocyte growth factor activator inhibitor I
-
-
-
hepatocyte growth factor activator inhibitor type 1
-
physiological inhibitor of matriptase. Hepatocyte growth factor activator inhibitor type 1 (HAI-1) is required for the extracellular appearance of the protease in an expression system using a monkey kidney COS-1 cell line. In COS-1 cells co-expressing a variant form of HAI-1 without the responsible inhibition domain, matriptase does not appear in the conditioned medium
-
hepatocyte growth factor activator inhibitor type 2
HAI-2
-
hepatocyte growth factor activator inhibitor type I
-
hepatocyte growth factor activator inhibitor type-1
-
-
-
hepatocyte growth factor activator inhibitor-1
-
hepatocyte growth factor activator inhibitor-2
-
hexamidine
and its structural analogs
KNAR
more selective for matriptase compared to matriptase-2
L-arginyl-L-glutaminyl-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-alaninamide
-
L-arginyl-N1-[(2S)-1-[[(2R)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
L-arginyl-N1-[(2S)-1-[[(2S)-6-amino-1-(1,3-benzothiazol-2-yl)-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
LWWR
2-fold selectivity for matriptase-2 against matriptase
methyl (2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
methyl (2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
methyl 4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoate
-
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((3-carbamimidoylbenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((4-carbamimidoylbenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis(4-(aminomethyl)phenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((3-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((4-bromobenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((4-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((6-aminopyridin-3-yl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((6-bromopyridin-3-yl)methoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(3-aminopropanamido)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(aminomethyl)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-aminophenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-((4-chlorobenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-(4-carbamoylphenoxy)benzamide
-
N-(1-(3-aminopropyl)piperidin-4-yl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
-
N-(2-aminoethyl)-1-(3-carbamimidoyl-N-[[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]-L-phenylalanyl)piperidine-4-carboxamide
-
N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)-1-(2-hydroxyethyl)piperidine-4-carboxamide
-
N-(3-[[(1R)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)ethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(2-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(4-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperazin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperidin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-[4-[4-(methylamino)-4-oxobutyl]piperidin-1-yl]-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
-
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-3-phenylpropyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-4-phenylbutyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-2-(4-benzylpiperidin-1-yl)-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-3-hydroxypropanamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-b-alaninamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)propanamide
-
N-(3-[[(1S)-2-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
N-(4-aminocyclohexyl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
-
N-(4-aminocyclohexyl)-O-(3-carbamimidoylphenyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
-
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
inhibitor modeling in the wild-type enzyme active site, overview
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
N-[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]-4'-methoxybiphenyl-3-sulfonamide
-
N-[3-([(1S)-1-(3-carbamimidoylbenzyl)-2-[4-(4-hydroxyphenyl)piperazin-1-yl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-benzyl-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[4-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl)phenyl]-b-alaninamide
-
N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
O-(3-carbamimidoylphenyl)-N-(4-methylcyclohexyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
-
plasminogen activator inhibitor I
-
-
-
plasminogen activator inhibitor-1
-
formation of a stable inhibitor complex
Protein C inhibitor
-
formation of a stable inhibitor complex
-
R1K'4-eglin
-
different eglin c variants with differing inhibitory potential versus matriptase, construction, expression and purification of eglin c variants and screening for inhibitory potency, overview, R1K'4-eglin has the wild-type Pro45 at P1 position and Tyr49 at P4' position residues replaced with Arg and Lys, respectively, leads to the production of a selective, high affinity and proteolytically stable inhibitor of matriptase, molecular modeling of enzyme-inhibitor complex, overview
R1K4-eglin
-
wild type eglin c with Pro45 at P1 position and Tyr49 residues at P4 position replaced with Arg and Lys respectively, most potent, selective, high affinity and proteolytically stable inhibitor
R4R1-eglin
-
with substituted P42 and L45 for arginine residues, variants containing an Arg or Lys at position 49 instead of the original Tyr residue show enhanced inhibition
RNPR
more selective for matriptase compared to matriptase-2
scFv antibody E2
-
competitive mechanism of inhibition of the scFv antibody enzyme inhibitors, which competes with substrate binding in the S1 site, the antibody binds to a number of residues flanking the active site, forming a unique three-dimensional binding epitope
-
scFv antibody S4
-
competitive mechanism of inhibition of the scFv antibody enzyme inhibitors, which competes with substrate binding in the S1 site, the antibody binds to a number of residues flanking the active site, forming a unique three-dimensional binding epitope
-
SFTI1
-
serine protease inhibitor can only inhibit Epi/MTP and cathepsin G. Mammary epithelial growth and morphogenesis in the presence of the latent form hepatocyte growth factor (pro-HGF) is blocked by addition of SFTI1 an inhibitor of the Epi/MTP protease activity
single chain variable fragment of antibodies
-
different variants
-
sulfated 3-amidinophenylalanine derivatives
deiverse variants, overview
-
sulfonylated 3-amidino-phenylalanine inhibitors
-
-
-
sunflower trypsin inhibitor
-
SFTI-1
-
sunflower trypsin inhibitor-1
sunflower trypsin inhibitor-2
-
SFTI-2
sunflower trypsin inhibitor-3
-
SFTI-3
WCYR
more selective for matriptase compared to matriptase-2
WRER
more selective for matriptase compared to matriptase-2
YYVR
13times more selective for matriptase-2 than matriptase
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
alpha-1-antitrypsin
-
-
-
alpha-1-antitrypsin
-
-
-
alpha-2-Antiplasmin
-
-
-
alpha-2-Antiplasmin
-
-
-
alpha2-antiplasmin
-
-
-
alpha2-antiplasmin
-
formation of a stable inhibitor complex
-
antithrombin III
-
-
-
antithrombin III
-
formation of a stable inhibitor complex
-
Aprotinin
-
inhibition of IGFBP-rP1 processing
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
hepatocyte growth factor activator inhibitor
-
HAI-1, the cognate transmembrane inhibitor of the enzyme, which is coexpressed with matriptase in epithelium
-
hepatocyte growth factor activator inhibitor
HAI-1, conventional protease inhibitor
-
hepatocyte growth factor activator inhibitor
-
HAI-1
-
hepatocyte growth factor activator inhibitor
-
active protease is inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1)
-
hepatocyte growth factor activator inhibitor 1
-
following matriptase activation, the active enzyme is immediately inhibited by binding to hepatocyte growth factor activator inhibitor 1, resulting in stable matriptase-hepatocyte growth factor activator inhibitor 1 complexes that are rapidly secreted
-
hepatocyte growth factor activator inhibitor 1
-
HAI-1, a Kunitz-type inhibitor that functions both as a chaperone and a reversible inhibitor
-
hepatocyte growth factor activator inhibitor type I
-
inhibition activities of a cell membrane-anchored form of recombinant HAI-1 (maHAI-1) against different matriptase variants in the hydrolysis of peptidyl-4-methyl-coumaryl-7-amide (MCA) substrates are compared: stem domain of matriptase affects the interaction between this protease and HAI-1
-
hepatocyte growth factor activator inhibitor type I
-
hepatocyte growth factor activator inhibitor type I (HAI-1) is shown to be required for the extracellular appearance of matriptase using COS-1 cells. Co-expression of recombinant variants of HAI-1 with the inhibition activity toward matriptase, including a variant consisting only of Kunitz domain I (the domain responsible for inhibition of matriptase), allows for the appearance of matriptase in the conditioned medium, whereas that of the variants without the inhibitory activity does not
-
hepatocyte growth factor activator inhibitor-1
-
Hai1a, i.e. Spint1Ia, enzyme inactivation by HAI-1 is required for epithelial integrity of the zebrafish epidermis, inhibitor mutant zebrafish show disrupted epidermal integrity, enhanced upon combined loss of hai1a and the paralogue hai1b, overview
-
hepatocyte growth factor activator inhibitor-1
i.e. HAI-1, binding is reversible and acid labile
-
hepatocyte growth factor activator inhibitor-1
-
-
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, forms complexes wih the enzyme in vivo
-
hepatocyte growth factor activator inhibitor-1
-
-
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
is required for proper development of placenta, overview
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, a Kunitz-type transmembrane serine protease inhibitor, cognate inhibitor of matriptase with regulatory function, molecular mechanism of inhibition, domain structure of HAI-1, proteolytic processing during maturation, activation, and shedding, enzyme-inhibitor complex structure, overview, the level of HAI-1 expression seems to be an important factor in the regulation of matriptase zymogen activation
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, without HAI-1 active matriptase may become unstable, leading to its degradation and low protein expression
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
activated matriptase is immediately inhibited by and forms complex with hepatocyte growth factor activator inhibitor-1
-
hepatocyte growth factor activator inhibitor-1
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, the cognate matriptase inhibitor is able to compensate for the effect of augmented matriptase activity, providing a rationale for the inhibition of matriptase to prevent tumor growth in vivo
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
is required for proper development of placenta, overview
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, a Kunitz-type transmembrane serine protease inhibitor, complex formation with the enzyme, enzyme inhibition is essential for placental development, overview
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, an extremely effective inhibitor of matriptase in vitro, that has a high affinity for matriptase binding and is typically co-expressed with matriptase in vivo. Matriptase activation appears to require physical interaction with its related inhibitor, HAI-1, which may serve to protect against aberrant matriptase proteolysis. Deletion or mutation of the LDLA domain of HAI-1 results in both a reduction in surface matriptase expression and abolishment of matriptase activity
-
hepatocyte growth factor activator inhibitor-2
-
HAI-2
-
hepatocyte growth factor activator inhibitor-2
-
HAI-2
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
docking of the inhibitor in the active site of matriptase, structure, overview
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
EC50 is 0.00564-0.0068 mM, the inhibitor contains a ketobenzothiazole serine trap designed based on matriptase's auto-catalytic domain (RQAR), it is a selective, slow, tight-binding inhibitor of matriptase that significantly reduces viral replication of H1N1 influenza virus, including the 2009 pandemic virus
sunflower trypsin inhibitor-1
-
and several derivatives with different amino acid side chains, overview
sunflower trypsin inhibitor-1
-
SFTI-1, isolated from sunflower seeds
sunflower trypsin inhibitor-1
SFTI-1, GRCTKSIPPICFPD, the plant-derived cyclic peptide is a promising drug scaffold with potent matriptase inhibitory activity, three-dimensional structure of the inhibitor and the protease domain of matriptase, molecular modeling, overview
additional information
-
no inhibition of IGFBP-rP1 processing by leupeptin, pepstatin, and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-3-(2'-naphthyl)alaninyl-l-alanine 2-aminoethyl amide, i.e. TAPI-1; not inhibited by leupeptin, pepstatin and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-3-(2'-naphthyl)alaninyl-L-alanine 2-aminoethyl amide
-
additional information
-
wild type eglin c has no effect
-
additional information
-
inhibition of matriptase activation in vitro and in vivo, overview
-
additional information
-
inhibitor design and synthesis, inhibitory potency and structure-activity relationships, overview, matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
additional information
-
autoinhibitory role of the LDLRA modules that may prevent premature activation of matriptase in the absence of appropriate activation stimuli
-
additional information
-
inhibitor synthesis and validation, overview
-
additional information
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
the enzyme is competitively inhibited by the anti-MT-SP1 antibody FabE2
-
additional information
design and synthesis of potent, selective inhibitors of matriptase, overview. Design of a class of potent and selective peptidomimetic inhibitors of matriptase based on the P4-P1 (Arg-Gln-Ala-Arg) portion of the activation peptide of matriptase, to which is linked a C-terminal serine trap in the form of a ketobenzothiazole group. The ketobenzothiazole serine trap is selected to form a covalent and reversible bond with the catalytic serine residue of the enzyme. Importance of stereochemistry at the P1 position for inhibitory potency
-
additional information
O-(3-carbamimidoylphenyl)-L-serine amides as matriptase inhibitors, overview. Analysis of cytotoxic effects of inhibitors
-
additional information
inhibitor design, synthesis of diverse 5-substituted phenylene1,3-bis(oxy) dibenzimidamide analogues, overview. Anaysis of cytotoxic effects of inhibitors
-
additional information
-
inhibitor design, synthesis of diverse 5-substituted phenylene1,3-bis(oxy) dibenzimidamide analogues, overview. Anaysis of cytotoxic effects of inhibitors
-
additional information
analysis of interaction of matriptase-2 with prototype low-molecular weight ligands using site-directed mutagenesis, kinetic analysis and molecular modeling, substrate/inhibitor-enzyme interactions, overview
-
additional information
analysis of interaction of matriptase-2 with prototype low-molecular weight ligands using site-directed mutagenesis, kinetic analysis and molecular modeling, substrate/inhibitor-enzyme interactions, overview
-
additional information
synthesis of high-affinity cyclic peptide matriptase inhibitors. An analogue of Momordica cochinchinensis trypsin inhibitor-II (MCoTI-II) is one of the most potent inhibitors of matriptase, structure-activity relationships of SFTI-1 and MCoTI-II, which is a structurally divergent trypsin inhibitor also containing a cyclic backbone
-
additional information
peptide inhibitor docking study with matriptase and matriptase-2, overview
-
additional information
generation of monoclonal antibodies against mutant N164Q/R614A and use as inhibitors. Two antibodies are competitive inhibitors and able to block the activity of wild-type full-length matriptase in complex biological samples by binding near the active site
-
additional information
-
generation of monoclonal antibodies against mutant N164Q/R614A and use as inhibitors. Two antibodies are competitive inhibitors and able to block the activity of wild-type full-length matriptase in complex biological samples by binding near the active site
-
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0.000003
(1r,4r)-4-amino-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)cyclohexanecarboxamide
pH 8.5, temperature not specified in the publication
0.000001
(1r,4r)-4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
pH 8.5, temperature not specified in the publication
0.00018
(2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
0.011
(2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
0.000018
1-(2-aminoethyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.000061
1-(3-aminopropanoyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.000031
1-(N-[[3-(b-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-3-carboxamide
-
-
0.000013
1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-4-carboxamide
-
-
0.000457
1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine
matriptase, pH and temperature not specified in the publication
0.0000014
2-(L-alanyl-L-arginyl)-1,3-benzothiazole
matriptase, pH and temperature not specified in the publication
0.00005
2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide
pH 8.0, recombinant catalytic enzyme domain
0.001182
3,5-bis(4-carbamimidoylphenoxy)-N-((4-hydroxycyclohexyl)methyl)benzamide
pH 8.5, temperature not specified in the publication
0.000204
3,5-bis(4-carbamimidoylphenoxy)-N-(1-(2-hydroxyethyl)piperidin-4-yl)benzamide
pH 8.5, temperature not specified in the publication
0.000591
3,5-bis(4-carbamimidoylphenoxy)-N-(4-fluorophenyl)benzamide
pH 8.5, temperature not specified in the publication
0.000301
3,5-bis(4-carbamimidoylphenoxy)-N-(4-hydroxycyclohexyl)benzamide
pH 8.5, temperature not specified in the publication
0.00077
3,5-bis(4-carbamimidoylphenoxy)-N-(4-methylcyclohexyl)benzamide
pH 8.5, temperature not specified in the publication
0.000411
3,5-bis(4-carbamimidoylphenoxy)-N-(cyclohexylmethyl)benzamide
pH 8.5, temperature not specified in the publication
0.000592
3,5-bis(4-carbamimidoylphenoxy)-N-cyclohexylbenzamide
pH 8.5, temperature not specified in the publication
0.00162
3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.0000025
3-(3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl)benzenecarboximidamide
-
-
0.000046
3-[(2R)-3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]propyl]benzenecarboximidamide
-
-
0.000001
3-[(2S)-2-([[3-(4-aminobutyl)phenyl]sulfonyl]amino)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxopropyl]benzenecarboximidamide
-
0.000013
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(1H-indol-5-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.000028
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(2-methylpyrimidin-4-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.00000008 - 0.0000001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
0.0000016
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.000012
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[4'-(1-methylethoxy)biphenyl-3-yl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.00011
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(biphenyl-3-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
0.0003
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0000067
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[([3-[(3-aminopropyl)amino]phenyl]sulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
0.000029
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0000054
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000091
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000026
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000006
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0000025
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000007
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-methoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0003
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4-cyclohexylphenyl)sulfonyl]amino]-3-oxopropoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.000047
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-3-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
0.00006
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-4-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
0.0015
3-[(2S)-3-[4-(4-aminobutanoyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0017
3-[(2S)-3-[4-(b-alanyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.000082
3-[(2S)-3-[4-(N-carbamimidoyl-b-alanyl)piperazin-1-yl]-3-oxo-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propyl]benzenecarboximidamide
pH 8.0, recombinant catalytic enzyme domain
0.00073
4,4'-((5-(1,2,3,4-tetrahydroisoquinoline-2-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000094
4,4'-((5-(4-(2-aminoethyl)piperidine-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.00198
4,4'-((5-(4-fluorophenylsulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000305
4,4'-((5-(decahydroquinoline-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.00179
4,4'-((5-(naphthalene-2-sulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000218
4,4'-[(3-[[(4-fluorophenyl)sulfonyl]amino]pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide
pH 8.5, temperature not specified in the publication
0.00106
4,4'-[(5-aminobenzene-1,3-diyl)bis(oxy)]dibenzenecarboximidamide
pH 8.5, temperature not specified in the publication
0.000177
4-(1-[3-carbamimidoyl-N-[(3-pyrrolidin-1-ylphenyl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000028
4-(1-[3-carbamimidoyl-N-[(4'-ethoxybiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000024 - 0.0000245
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
0.000087
4-(1-[N-[(4'-tert-butylbiphenyl-3-yl)sulfonyl]-3-carbamimidoyl-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000014
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
pH 8.0, recombinant catalytic enzyme domain
0.000026
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-[[(4-cyclohexylphenyl)sulfonyl]amino]propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
-
0.0288
4-aminobenzamidine
-
-
0.000545
4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
pH 8.5, temperature not specified in the publication
0.2
4-[1-(3-carbamimidoyl-N-[[3-(1H-imidazol-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000024
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperazin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00003
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperidin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000098
4-[1-(3-carbamimidoyl-N-[[3-(6-oxopyridazin-1(6H)-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00000043
4-[1-(N-[[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00001
4-[1-(N-[[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.0000063
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000012
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanamide
-
-
0.000255
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoic acid
-
-
0.000053
4-[4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazin-1-yl]-N-methyl-4-oxobutanamide
-
-
0.00000013
9-fluorenylmethyloxycarbonyl-GR-ketobenzothiazole
pH not specified in the publication, temperature not specified in the publication
0.000005 - 0.000013
Aprotinin
0.00019
ARCTKSIPPICFPD
pH 7,6, 37°C
0.0000061 - 0.0000075
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
0.00022 - 0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
0.000055 - 0.00019
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
0.0021 - 0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
0.00029 - 0.00077
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
0.0000000497
Bovine pancreatic trypsin inhibitor
-
-
-
0.00004
CJ-730
-
3-amidinophenylalanine-based inhibitor CJ-730
0.000026
D-hTyr-Ala-4-amidinobenzylamide
pH 8.0, temperature not specified in the publication
0.000041
ethyl (3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)carbamate
-
0.00185
ethyl 4-(3,5-bis(4-carbamimidoylphenoxy)benzamido)piperidine-1-carboxylate
pH 8.5, temperature not specified in the publication
0.000065
ethyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.01
GACTKSIPPICFPD
pH 7,6, 37°C
0.00018
GAVCPKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0000023
GGACPKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0000035
GGRCPKALKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.00000029
GGRCPKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000039
GGVCAKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.01
GGVCPAILKKCRRDSDCPGACICRGNGYCGSGSD
above, pH 7,6, 37°C
0.0000098
GGVCPKALKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000012
GGVCPKIAKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000076
GGVCPKILAKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0000041
GGVCPKILKACRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000012
GGVCPKILKKCRRDSDCPGACICRGAGYCGSGSD
pH 7,6, 37°C
0.000011
GGVCPKILKKCRRDSDCPGACICRGNGACGSGSD
pH 7,6, 37°C
0.0000037
GGVCPKILKKCRRDSDCPGACICRGNGYCASGSD
pH 7,6, 37°C
0.000098
GGVCPKILKKCRRDSDCPGACICRGNGYCGAGSD
pH 7,6, 37°C
0.00011
GGVCPKRLKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000039
GGVCPRILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0012
GKCTKSIPPICFPD
pH 7,6, 37°C
0.0015
GRCAKSIPPICFPD
pH 7,6, 37°C
0.01
GRCTASIPPICFPD
above, pH 7,6, 37°C
0.0016
GRCTKAIPPICFPD
pH 7,6, 37°C
0.000084
GRCTKSAPPICFPD
pH 7,6, 37°C
0.000051
GRCTKSAPPRCFPD
pH 7,6, 37°C
0.000027
GRCTKSIAPICFPD
pH 7,6, 37°C
0.00037
GRCTKSIPAICFPD
pH 7,6, 37°C
0.000073
GRCTKSIPPACFPD
pH 7,6, 37°C
0.01
GRCTKSIPPDCFPD
pH 7,6, 37°C
0.0037
GRCTKSIPPGCFPD
pH 7,6, 37°C
0.00032
GRCTKSIPPICAPD
pH 7,6, 37°C
0.00024
GRCTKSIPPICFAD
pH 7,6, 37°C
0.0015
GRCTKSIPPICFPA
pH 7,6, 37°C
0.0002
GRCTKSIPPICFPD
pH 7,6, 37°C
0.00004
GRCTKSIPPKCFPD
pH 7,6, 37°C
0.0000064
GRCTKSIPPRCFPD
pH 7,6, 37°C
0.0045
GRCTKSRPPICFPD
pH 7,6, 37°C
0.00031
GRCTRSIPPICFPD
pH 7,6, 37°C
0.000924
hexamidine
pH 8.5
0.0061
L-arginyl-L-glutaminyl-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-alaninamide
matriptase, pH and temperature not specified in the publication
0.0000046
L-arginyl-N1-[(2S)-1-[[(2R)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000000011 - 0.0000033
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
0.0000095
L-arginyl-N1-[(2S)-1-[[(2S)-6-amino-1-(1,3-benzothiazol-2-yl)-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.0019 - 0.0041
leupeptin
0.0001
methyl (2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
0.0024
methyl (2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
0.0000061
methyl 4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoate
-
-
0.000003
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((3-carbamimidoylbenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.000023
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((4-carbamimidoylbenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.001698
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis(4-(aminomethyl)phenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000006
N-((1r,4r)-4-aminocyclohexyl)-3-((3-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00026
N-((1r,4r)-4-aminocyclohexyl)-3-((4-bromobenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00001
N-((1r,4r)-4-aminocyclohexyl)-3-((4-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00203
N-((1r,4r)-4-aminocyclohexyl)-3-((6-aminopyridin-3-yl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000793
N-((1r,4r)-4-aminocyclohexyl)-3-((6-bromopyridin-3-yl)methoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000116
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(3-aminopropanamido)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00004
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(aminomethyl)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00113
N-((1r,4r)-4-aminocyclohexyl)-3-(4-aminophenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00047
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-((4-chlorobenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.000824
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-(4-carbamoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000141
N-(1-(3-aminopropyl)piperidin-4-yl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000026
N-(2-aminoethyl)-1-(3-carbamimidoyl-N-[[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]-L-phenylalanyl)piperidine-4-carboxamide
pH 8.0, recombinant catalytic enzyme domain
0.000018
N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)-1-(2-hydroxyethyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.0000067
N-(3-[[(1R)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)ethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00047
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(2-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000053
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(4-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000037
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperazin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000033
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperidin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000016
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-[4-[4-(methylamino)-4-oxobutyl]piperidin-1-yl]-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
-
1
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-3-phenylpropyl]sulfamoyl]phenyl)-beta-alaninamide
larger than 1
1
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-4-phenylbutyl]sulfamoyl]phenyl)-beta-alaninamide
larger than 1
0.000017
N-(3-[[(1S)-2-(4-benzylpiperidin-1-yl)-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00012
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-3-hydroxypropanamide
-
0.0000066
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-b-alaninamide
pH 8.0, recombinant catalytic enzyme domain
0.0000038
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
0.000003
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
0.00018
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)propanamide
-
0.0000018
N-(3-[[(1S)-2-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.0000038
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000036
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00001
N-(4-aminocyclohexyl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.0037
N-(4-aminocyclohexyl)-O-(3-carbamimidoylphenyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
pH and temperature not specified in the publication
0.000052 - 0.1
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
0.0021 - 0.28
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
0.000145
N-[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]-4'-methoxybiphenyl-3-sulfonamide
-
0.00015
N-[3-([(1S)-1-(3-carbamimidoylbenzyl)-2-[4-(4-hydroxyphenyl)piperazin-1-yl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
-
0.01
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-benzyl-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.000056
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.0028
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[4-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.000000088
N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000046 - 0.03
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
0.00022 - 0.62
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
0.000004
R1K'4-eglin
-
pH 9.0, recombinant His-tagged amino acids 596-855 of matriptase
0.0000000123
scFv antibody E2
-
-
-
0.0000000704
scFv antibody S4
-
-
-
0.0000067 - 0.000046
sulfonylated 3-amidino-phenylalanines
-
-
-
0.00000092
sunflower trypsin inhibitor
-
-
-
0.00000092 - 0.0001
sunflower trypsin inhibitor-1
0.000025
sunflower trypsin inhibitor-2
-
-
0.0000025
sunflower trypsin inhibitor-3
-
-
additional information
additional information
-
0.00000008
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.0000001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
-
0.000024
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.0000245
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000005
Aprotinin
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0000098
Aprotinin
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000013
Aprotinin
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0000061
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.0000075
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.00022
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
Ki above 0.01 mM, matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
Ki above 0.01 mM, purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000055
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00017
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00019
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0021
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
Ki above 0.01 mM, matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
Ki above 0.01 mM, purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00029
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00046
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
purified enzyme, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00077
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000000011
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.0000033
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase-2, pH and temperature not specified in the publication
0.0019
leupeptin
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0024
leupeptin
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0041
leupeptin
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000052
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.00021
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.00029
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.00077
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C
0.015
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.02
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.02
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.1
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.0021
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C
0.003
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.037
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.075
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.2
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.2
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.22
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.28
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.000046
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.000055
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C
0.00016
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.00019
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.0012
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.0016
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.02
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.03
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.00022
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C
0.0026
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.03
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.054
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.069
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.2
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.2
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.62
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.00000092
sunflower trypsin inhibitor-1
-
-
0.0001
sunflower trypsin inhibitor-1
-
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additional information
additional information
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additional information
additional information
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inhibition kinetics with antobodies E2 and S4 and point mutants thereof, overview
-
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ovary
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normal trophoblast cell line
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normal lung epithelial cells, matriptase-prostasin cascade
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liver
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benign prostate hyperplasia, matriptase-prostasin cascade
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of ductal carcinomas in situ, and grade I-III invasive ductal carcinomas
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low expression level
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amtripase gene expression in femoral head cartilage is analyzed
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skin
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kidney
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high level
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jejunum, ileum, colon
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overexpression of the enzyme
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colon
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ovary
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skin
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intestinal IPEC-J2 cell monolayer
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breast cancer cell line
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low level
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oral cavity
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Epi/MTP is expressed at low level in the mouse mammary epithelium of young animals and it accumulates at the terminal end-bud of the growing ducts. The level of Epi/MTP is elevated in the mammary glands at stages when epithelial proliferation and modeling occur. It is primarily present in the luminal epithelial cells of mouse mammary ducts and lobules
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RT-PCR analysis reveal a 1000fold higher matriptase expression in human pancreatic adenocarcinoma AsPC-1 cells than in the MDA-MB-435S cells
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skin
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low level
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low level
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high level
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low expression level
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primary epithelial cells
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low level
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keratinocytes in tongue, hard palate, bucca, gingiva, and lip
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oral cavity
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major amount of matripase
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ovarian clear cell adenocarcinoma cells, high level expression of IGFBP-rP1-cleaving enzyme
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glandular stomach
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using immunohistochemistry a significant overexpression of matriptase is shown in pancreatic carcinoma compared to normal pancreatic ducts
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pancreas
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subculture cell line of PC-3 cells
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enzyme inhibition is essential for placental development, overview
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expression determined by quantitative RT-PCR
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kidney
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kidney
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skin
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only matriptase-HAI-1 complexes and not latent matriptase are detected in urine and seminal fluid
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contains only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 or antithrombin III but no latent matriptase
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skin
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colon, uterus
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high level
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oral cavity
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bladder transitional cell carcinoma cell line
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bladder transitional cell carcinoma cell line
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normal bladder urothelial cell line
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uterus
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high level
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nontumorigenic mammary epithelial cells
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proportional increases or decreases in matripase and hepatocyte growth factor activator inhibitor-1
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mammary epithelial cell line
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co-expression of matriptase and its substrate serine protease prostasin
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strong expression association between matriptase and its substrate prostasin in breast cancer
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low level
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high expression level
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cells target latent matriptase to the basolateral plasma membrane where activation, inhibition, and secretion of matriptase take place. A proportion of matriptase-HAI-1 complexes, but not the latent matriptase, undergoes transcytosis to the apical plasma membrane for secretion
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latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney
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high enzyme expression level
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matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
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matriptase is up-regulated in a variety of cancers and correlates closely with disease progression
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the secretion of matriptase from cancer cells is increased via the action of GnT-V, i.e. UDP-N-acetylglucosamine:alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase, overview
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high enzyme expression level
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matriptase is up-regulated in a variety of cancers and correlates closely with disease progression
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high level
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major amount of matripase
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expression determined by quantitative RT-PCR
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expression pattern during development, overview
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expression pattern during development, overview
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the enzyme is co-expressed with hepatocyte growth factor activator inhibitor-1 in both extraembryonic and embryonic tissue
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occurs exclusively on the basolateral membrane of enterocytes
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enzyme expression in developing basal layer of the epidermis, enzyme inactivation by HAI-1 is required for epithelial integrity of the zebrafish epidermis, overview
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matriptase is detected in the suprabasal epidermis with the highest level of expression in the granular and transitional cell layers
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matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis, overview
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matriptase-prostasin cascade
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bronchial epithelial cells
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is expressed in epithelial cells as a zymogen
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matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis, overview
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basolateral sides
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surface epithelial cells
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co-expression and co-localization of both matriptase and HAI-1 in many epithelial cells, complex formation, overview
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expression in most human epithelia
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tracheal, esophageal, gastric, broncheal and alveolar, of scretory duct, intestinal, a dof the urogenityl tract, overview
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high expression level in epithelia
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matriptase and prostasin display a near identical spatial expression pattern in the epithelial compartment of breast cancer tissue
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tracheal, esophageal, gastric, broncheal and alveolar, of scretory duct, intestinal, a dof the urogenityl tract, overview
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esophagus and forestomach, suprabasal layer, trachea, bronchi, bronchioles, bladder
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in polarized epithelium, matriptase and prostasin co-localize briefly at the basolateral plasma membrane prior to HAI-1-mediated matriptase endocytosis
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in cancer tissue the expression of serine protease SNC19/matripase and hepatocyte growth factor activator inhibitor-1 is significantly lower than in the corresponding adjacent normal tissue, the ratio, however, shows no difference between normal and malingant tissue
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predominantly
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latent matriptase is localized at the basolateral plasma membrane of the ductal epithelial cells of the prostate and kidney
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latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney
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matriptase is almost exclusively expressed in liver
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matriptase-2 is exclusively expressed in the liver initially under zymogen form
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matriptase-2 is predominantly expressed in the liver
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expression determined by quantitative RT-PCR
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bronchial epithelium
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enzyme expression in normal and neoplastic mast cells, almost all different mast cells types in humans express matriptase, overview
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low level
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breast cancer cell line, matriptase-prostasin cascade
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contains only activated matriptase
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high level
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major amount of matripase
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gastric carcinoma cells, high level expression of IGFBP-rP1-cleaving enzyme
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HRA cell
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RT-PCR analysis reveal a 1000fold higher matriptase expression in human pancreatic adenocarcinoma AsPC-1 cells than in the MDA-MB-435S cells
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expression determined by quantitative RT-PCR, highest expression among different prostate cancer cell lines
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latent matriptase is localized at the basolateral plasma membrane of the ductal epithelial cells of the prostate and kidney
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latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney
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matriptase co-localizes with hepatocyte growth factor activator inhibitor-1 (HAI-1) in the epidermis
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44.1% of papillary carcinomas, 15.4% of follicular adenomas, none follicular or anaplastic carcinomas
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co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues, analysis of expression of GnT-V and matriptase in thyroid neoplasm tissues, papillary carcinoma and follicular carcinoma, overview
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contains only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 but no latent matriptase
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only matriptase-HAI-1 complexes and not latent matriptase are detected in urine and seminal fluid
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additional information
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COS cell
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additional information
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no activity in foreskin fibroblasts or HT-1080 fibrosacroma cells
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additional information
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not in normal thyroid tissue
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additional information
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stomach carcinoma cell line, low level in AZ521 cell, SCH cell, STKM-2 cell, MDA-MB cell, MMK-29 cell, YLC cell, KKI-cell, LU-65 cell and A549 cell,high level in STKM-1, RCM-1 cell, LU-99 cell and VMRC-LCP cell
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additional information
-
enzyme expression analysis in cancer cells, overview
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additional information
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expression profile of matriptase in cancer tissues, overview
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additional information
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matriptase-1 expression analysis, no matriptase-1 expression in cell lines: MDA-MB-157, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, G-361, ECV-304, PLC-PRF-5, and in endothelial cells, overview
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additional information
matriptase-1 expression analysis, no matriptase-1 expression in cell lines: MDA-MB-157, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, G-361, ECV-304, PLC-PRF-5, and in endothelial cells, overview
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additional information
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matriptase-2 expression analysis, no matriptase-2 expression in cell lines: MDA-MB-157, MDA-MB-231, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, BT549, PC-3, DU-145, CA-HPV-10, HT-115, HRT-18, MRC5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, A-549, G-361, ECV-304, and in endothelial cells, overview
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additional information
matriptase-2 expression analysis, no matriptase-2 expression in cell lines: MDA-MB-157, MDA-MB-231, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, BT549, PC-3, DU-145, CA-HPV-10, HT-115, HRT-18, MRC5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, A-549, G-361, ECV-304, and in endothelial cells, overview
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additional information
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no activity in chondrocytes within cartilage, in stromal fibroblasts, hepatocytes, pneumocytes, cardiac muscle, and smooth muscle of uterine myometrium
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additional information
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no endogenous expression of matriptase, prostasin or EGFR in HEK-293 cells
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additional information
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no IGFBP-rP1 processing activity in HSC-4 cells, HEK-293 cells, HLE cells, MKN-45 cells, HT-1080 cells, EJ-1 cells, and ECV-304 cells, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium
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additional information
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tissue distribution, overview, postnatal expression pattern, overview
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additional information
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tissue expression pattern, overview
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additional information
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matriptase is expressed in prostate, breast and colorectal cancers in vitro and in vivo
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additional information
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not detected in MDA-MB-231, SUM1315, BT-549, and SUM-159 cells
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additional information
not detected in MDA-MB-231, SUM1315, BT-549, and SUM-159 cells
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additional information
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expression of matriptase and prostasin in breast cancer cell lines, overview. No activity in MDA-MB-231 cells, SUM-159 cells, SUM-1315cells, and BT-549 cells
brenda
additional information
expression of matriptase and prostasin in breast cancer cell lines, overview. No activity in MDA-MB-231 cells, SUM-159 cells, SUM-1315cells, and BT-549 cells
brenda
additional information
matriptase co-localizes with hemagglutinin at the apical surface of human epithelial cells and within endosomes. No expression in A-549 cells
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additional information
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matriptase co-localizes with hemagglutinin at the apical surface of human epithelial cells and within endosomes. No expression in A-549 cells
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additional information
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the enzyme is co-expressed with hepatocyte growth factor activator inhibitor-1 in both extraembryonic and embryonic tissue, overview
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additional information
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tissue distribution, overview, postnatal expression pattern, overview
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additional information
tissue expression pattern, overview
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additional information
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in nearly all murine epithelial tissues, matriptase is coexpressed with the membrane serine protease prostasin
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additional information
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tissue expression pattern, overview
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metabolism
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the matriptase zymogen is capable of intermolecular autoproteolytic activation, and the active enzyme is also an effective activator of the prostasin zymogen through direct proteolytic cleavage at its zymogen activation site. Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway. Activated prostasin appears to target several downstream effector proteins, including the epithelial sodium channel and the G protein-coupled protease activated receptor-2, which are both matriptase substrates. Matriptase and not prostasin is the primary effector protease of tight junction assembly in simple columnar epithelia
evolution
matriptase shares high sequence similarity with matriptase-2, particularly in the catalytic domain which is about 45% identical
evolution
matriptase-2 belongs to the family of type II transmembrane serine proteases
evolution
matriptase-2 belongs to the family of type II transmembrane serine proteases, representing an emerging class of cell surface proteolytic enzymes. Matriptase-2 shares high sequence similarity with matriptase, particularly in the catalytic domain which is about 45% identical
evolution
the enzyme is a member of the TTSP family
malfunction
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hepatocyte growth factor activator inhibitor-1 knockout mice with one or two wild-type matriptase alleles die in utero. Knockout mice on the matriptase hypomorphic mouse background complete embryonic development, are viable, healthy, and display normal long-term survival. Matriptase is identified as a critical inhibitory target for hepatocyte growth factor activator inhibitor-1 in keratinized squamous epithelium and a delicate balance between matriptase and hepatocyte growth factor activator inhibitor-1 maintains homeostasis of adult mammalian tissues
malfunction
-
mammary epithelial growth and morphogenesis in the presence of the latent form hepatocyte growth factor (pro-HGF) is blocked either by addition of SFTI1 an inhibitor of the Epi/MTP protease activity or by siRNA knockdown of the Epi/MTP expression
malfunction
-
matriptase expression down-regulated with matriptase-targeting siRNA effectively abolishes pro-HGF activation
malfunction
matriptase-2 is important for iron homeostasis. Human patients with iron-refractory iron deficiency anemia show mutation in the TMPRSS6 gene
malfunction
-
mice lacking the protease domain of matriptase-2 are crossed with mice lacking hemojuvelin in order to examine the relationship between hemojuvelin and matriptase-2 in vivo. Mice lacking functional matriptase-2 and hemojuvelin exhibit low Hamp (Hepcidin encoding gene) expression, high serum and liver iron, and high transferrin saturation. Double mutant mice also exhibit lower levels of iron in the heart compared to hemojuvelin-deficient mice, demonstrating a possible cardioprotective effect resulting from the loss of matriptase-2
malfunction
-
Tmprss6-/- mice knockout mice exhibit an iron deficiency phenotype. Tmprss6 -/- mice exhibit reduced ferroportin immunostaining and iron accumulation in intestinal enterocytes
malfunction
-
two novel heterozygous mutations are described within the matriptase-2 gene of monozygotic twin girls exhibiting an iron-refractory iron deficiency anemia phenotype. A frameshift mutation (P686fs) caused by the insertion of the four nucleotides CCCC in exon 16 (2172_2173insCCCC) that is predicted to terminate translation before the catalytic serine. A di-nucleotide substitution c.467C to A and c.468C to T in exon 3 that causes the missense mutation A118D in the sea urchin sperm protein, enteropeptidase, agrin (SEA) domain of the extracellular stem region of matriptase-2
malfunction
-
the genetic elimination of matriptase completely abolishes the aberrant caseinolytic activity that is caused by lympho-epithelial Kazal-type-related inhibitor (LEKTI) deficiency in both the lower epidermal layers as well as in the dermis. Matriptase elimination prevents spontaneous stratum corneum loss, restores keratohyalin granules, and improves the barrier function of LEKTI-deficient epidermis. Loss of matriptase restores corneodesmosome integrity to LEKTI-deficient epidermis. Matriptase ablation prevents kallikrein hyperactivity-mediated inflammation caused by LEKTI-deficiency
malfunction
a mutation in matriptase is implicated in autosomal recessive ichtyosis withhypotrichosis a rare skin disease
malfunction
downregulation of the enzyme stabilizes fetuin-A in the unprocessed form
malfunction
expression of matriptase is frequently dysregulated in human cancers
malfunction
lack of the putative endocytosis motif in the cytoplasmic domain largely abolishes the sensitivity of the enzyme to iron depletion
malfunction
-
matriptase and prostasin null mice have identical phenotypes, mice deficient for matriptase phenocopy mice deficient for epidermal prostasin and show impaired corneocyte differentiation, imparied lipid matrix formation, loss of profilaggrin processing and loss of tight junction formation and function. Matriptase-deficient mice present with a variety of epidermal defects, including a generalized disruption of the stratum corneum architecture, loss of vesicular bodies that generate intercorneocyte lipids and hypoplasia and dysgenesis of hair follicles. Together, these defects lead to a compromised epidermal barrier and result in fatal dehydration during the neonatal period. Targeted postnatal ablation of matriptase in mice perturbs the function of multiple adult tissues, indicating an ongoing requirement for matriptase proteolysis in the maintenance of diverse types of epithelia. Matriptase-deficient Caco-2 monolayers as well as matriptase hypomorphic mice are shown to express abnormally high levels of the tight junction protein claudin-2, which is associated with the formation of ion channels that decrease the cohesion between adjacent epithelial cells. Matriptase pathophysiology, overview
malfunction
siRNA knockdown of matriptase by 80.0% in human bronchial epithelial cells significantly blocks influenza virus replication in these cells
malfunction
-
siRNA silencing of matriptase expression or inhibition of matriptase activity impairs development of transepithelial electrical resistance and increases the permeability of Caco-2 epithelial barriers
physiological function
-
both matriptase and a specific peptide agonist for proteinase-activated receptor 2 are able to induce intracellular calcium mobilization and inhibition of proliferation in cultured human HaCaT keratinocytes. Results suggest that proteinase-activated receptor 2 is a substrate for matriptase in human skin in vivo. Deregulation of these proteins delineates squamous cell carcinoma progression
physiological function
-
Epi/MTP participates in mammary epithelial growth and modeling through activation of pro-hepatocyte growth factor
physiological function
-
exogenous matriptase significantly enhances cytokine-stimulated cartilage collagenolysis, while matriptase alone causes significant collagenolysis from osteoarthritis cartilage, which is metalloproteinase-dependent. Matriptase also induces metalloproteinase-1, -3, -13 gene expression. Synovial perfusion data confirm that matriptase activates proteinase activated receptor-2, and matriptase-dependent enhancement of collagenolysis from osteoarthritis cartilage is blocked by proteinase activated receptor-2 inhibition
physiological function
-
hepatocyte growth factor activator inhibitor type-1 is not required for activation of matriptase in stably transfected Madin-Darby canine kidney cells
physiological function
-
matriptase efficiently activates hepatocyte growth factor
physiological function
-
matriptase-2 regulates iron metabolism through proteolytic cleavage of hemojuvelin, a cell surface protein that regulates hepcidin expression through a bone morphogeneic protein/SMAD pathway
physiological function
matriptase-2 regulates iron metabolism through proteolytic cleavage of hemojuvelin, a cell surface protein that regulates hepcidin expression through a bone morphogeneic protein/SMAD pathway
physiological function
-
matriptase initiates Netherton syndrome in a lympho-epithelial Kazal-type-related inhibitor (LEKTI)-deficient mouse model by premature activation of a pro-kallikrein-related cascade. Matriptase is an efficient activator of epidermal pro-kallikreins that co-localize with LEKTI at the granular-transitional layer boundary
physiological function
the matriptase-prostasin cascade plays a critical role in breast cancer
physiological function
-
TMPRSS6 controls iron homeostasis through its negative regulation of expression of hepcidin, a key hormone involved in iron metabolism
physiological function
deregulation of matriptase can lead to various pathologies. Matriptase is thought to be implicated in osteoarthritis by initiating and inducting cartilage destruction
physiological function
-
matriptase is a potential oncogene, its expression correlates with the severity of tumors in the breast and prostate and de novo matriptase expression has been found in both ovarian and cervical carcinomas. The ratio of matriptase/HAI-1 mRNA is increased in ovarian and colorectal cancer, indicating that deregulated matriptase proteolysis may contribute to tumor formation or metastasis. In the epidermis, the glycosylphosphatidylinositol anchored membrane serine protease prostasin is activated by matriptase to initiate a proteolytic cascade that is required for the development of the stratum corneum barrier function. Matriptase in epidermal barrier and epidermal development, detailed overview. Proteolytic activity of the matriptase-prostasin cascade is regulated in the epidermis via inhibition by the Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-1
physiological function
matriptase is a regulator of the epidermal sodium channel
physiological function
matriptase is a serine protease implicated in cancer invasion and metastasis, matriptase activates latent growth factors such as hepatocyte growth factor/scatter factor, and proteases such as urokinase plasminogen activator
physiological function
matriptase is a trypsin-like serine protease with specific proteolytic activity downstream of an arginine residue at the cleavage site. Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium. Influenza viruses do not encode any proteases and must rely on host proteases for the proteolytic activation of their surface hemagglutinin proteins in order to fuse with the infected host cells
physiological function
matriptase is involved in tumor pathogenesis
physiological function
matriptase performs cleavage activation of the human-adapted influenza virus subtypes exhibiting both subtype and strain specificities
physiological function
-
matriptase promotes intestinal epithelial barrier formation
physiological function
matriptase-2 is a regulatory protease controlling iron homeostasis
physiological function
the enzyme controls the expression of hepcidin, the key regulator of iron homeostasis. By cleaving hepcidin, the enzyme supresses bone morphogenetic protein against decapentaplegic signaling
physiological function
the enzyme suppresses the expression of hepatic hepcidin, an iron regulatory hormone, by cleaving membrane hemojuvelin into an inactive form. Hemojuvelin is a bone morphogenetic protein coreceptor. Regulation of the enzyme occurs at the level of protein degradation rather than by changes in the rate of internalization and translational or transcriptional mechanisms, the cytoplasmic enzyme domain is necessary for its regulation
physiological function
the enzyme suppresses the expression of hepcidin, the main regulator of systemic iron homeostasis, through cleavage of the bone morphogenetic protein co-receptor hemojuvelin, matriptase-2 plays an important role in iron homeostasis
physiological function
the type II transmembrane serine protease matriptase is a key activator of multiple signaling pathways associated with cell proliferation and modification of the extracellular matrix
physiological function
-
HAI-1 but not HAI-2 is the prominent inhibitor for prostasin and matriptase in skin. The limited role for HAI-2 in the inhibition of matriptase and prostasin is the result of its primarily intracellular localization in basal and spinous layer keratinocytes, which probably prevents the HAI-2 from interacting with active prostasin or matriptase
physiological function
hepsin alone and not matriptase or HGFA plays a key role in diminishing epithelial cell membrane integrity through degradation of desmogelin-2 in breast cancer cells
physiological function
-
loss of cell surface protease inhibitor HAI-2 in intestinal epithelial cells leads to unrestrained matriptase activity and efficient cleavage of epithelial cell adhesion molecule EPCAM. Congenital tufting enteropathy-associated HAI-2 mutant proteins exhibit reduced ability to inhibit matriptase and also fail to efficiently stabilize claudin-7 in intestinal epithelial cells
physiological function
notopleural is a functional homologue of matriptase. Notopleural mediates morphogeneisis and remodeling of apical extracellular matrix during tracheal system development and is essential for maintenance of the transepithelial barrier function. Notopleural degrades the zona pellucida-domain protein Dumpy, a component of the transient tracheal apical extracellular matrix. Notopleural cleaves tracheal-prostasin zymogen and the zona pellucida-domain of the extracellular matrix protein Piopio in vitro
physiological function
suppression of matriptase activity by inhibitors 3-[(2S)-2-[[(2',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-(4-[2-(methylcarbamoyl)aminoethyl]piperidin-1-yl)-3-oxopropyl]benzenecarboximidamide and 3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2',4'-dichlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide leads to decreased transepithelial electrical resistance of the cell monolayer and to an enhanced transport of fluorescently labelled dextran
additional information
a three-pronged model for the action of matriptase: activation of incoming viruses in the extracellular space in its shed form, upon viral attachment or exit in its membrane-bound and/or shed forms at the apical surface of epithelial cells, and within endosomes by its membrane-bound form where viral fusion takes place
additional information
-
a three-pronged model for the action of matriptase: activation of incoming viruses in the extracellular space in its shed form, upon viral attachment or exit in its membrane-bound and/or shed forms at the apical surface of epithelial cells, and within endosomes by its membrane-bound form where viral fusion takes place
additional information
comparison of trypsin and matriptase active sites, overview
additional information
in Hep-G2 cells stably expressing the coding sequence of gene TMPRSS6, encoding the enzyme, incubation with apo-transferrin or the membrane-impermeable iron chelator deferoxamine mesylate salt, increases enzyme levels. This increase does not result from the inhibition of enzyme shedding from the cells
additional information
putative substrate binding mode, molecular docking, overview
additional information
-
putative substrate binding mode, molecular docking, overview
additional information
-
spatial and temporal co-expression of matriptase and prostasin
additional information
structural differences between matriptase-2 and matriptase, the enzyme-ligand interactions of matriptase-2 involve four important amino acids, His 665, Glu 712, Ala 757, Leu785. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region. Location of His665, Glu712, Ala757 and Leu785 in the active site of matriptase-2, overview
additional information
structural differences between matriptase-2 and matriptase, the enzyme-ligand interactions of matriptase-2 involve four important amino acids, His 665, Glu 712, Ala 757, Leu785. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region. Location of His665, Glu712, Ala757 and Leu785 in the active site of matriptase-2, overview
additional information
structural differences between matriptase-2 and matriptase. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region
additional information
structural differences between matriptase-2 and matriptase. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region
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100000
-
immunoblotting, matripase-hepatocyte growth factor activator inhibitor-1 complex
110
-
Western blot analysis using seminal fluid, seminal fluid contains only activated matriptase in complex with antithrombin III, supposed 70 kDa active matriptase and a 40 kDa antithrombin III-fragment
130000
-
SDS-PAGE and Western blot, reducing conditions, matriptase-hepatcyte growth factor activator inhibitor-1 complex
240000
1 * 70000 + 1 * 240000, complex purified from milk, SDS-PAGE
25000
serine protease domain, identified by SDS-PAGE, Western blot analysis and LC-MS,MS, without serpin complex
26000
-
determined by SDS-PAGE
32000
-
SDS-PAGE reducing and non-reducing conditions and Western blot using anti-rat matriptase catalytic domain anibody, designated pseudozymogen His6t-S-CD consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase, before cleavage with enterokinase
35000
-
catalytic domain, Asp603 - Val855, before treatment with enteropeptidase, determined by SDS-PAGE and Western blot analysis
40000
-
catalytic domain, Asp603 - Val855, before treatment with enteropeptidase, determined by SDS-PAGE and Western blot analysis
43000
-
under non-reducing conditions in a sample of medium three bands 61 kDa, 55 kDa, 43 kDa are visible using Western blotting with a anti-myc antibody
45000
noncatalytic domain, identified by SDS-PAGE, Western blot analysis and LC-MS,MS
55000
-
under non-reducing conditions in a sample of medium three bands 61 kDa, 55 kDa, 43 kDa are visible using Western blotting with a anti-myc antibody
60000
-
serine protease domain, dimer, determined by SDS-PAGE and Western blot analysis
61000
-
under non-reducing conditions in a sample of medium three bands 61 kDa, 55 kDa, 43 kDa are visible using Western blotting with a anti-myc antibody
84000
-
calculated molecular mass
110000
-
gelatin zymography or immunoblotting, matripase/hepatocyte growth factor activator inhibitor complex
110000
-
Western blot analysis, unprocessed enzyme
120000
-
complexed form, SDS-PAGE
120000
-
immunoblotting, 70000 active matripase plus full-length hepatocyte growth factor activator inhibitor-1
120000
-
SDS-PAGE, reducing condition, and Western blot, activated form of matriptase in complex with hepatocyte growth factor activator inhibitor 1
120000
-
x * 95000, single-chain latent enzyme, SDS-PAGE, x * 120000, active enzyme in complex with inhibitor HAI-1, SDS-PAGE
28000
-
catalytic domain, Asp603 - Val855, after treatment with enteropeptidase, determined by SDS-PAGE and Western blot analysis
28000
-
extracellular domains, Tyr81 - Val855, after treatment with enteropeptidase, determined by SDS-PAGE and Western blot analysis
28000
-
SDS-PAGE and Western blot analysis, reducing conditions, activated matriptase, disulfide-linked two-chain C-terminal fragment
28000
-
SDS-PAGE under reducing conditions followed by Western blotting using an anti-matriptase catalytic domain antibody, activated C-terminal part consiting of the catalytic domain
28000
-
SDS-PAGE under reducing conditions followed by Western blotting using an anti-matriptase catalytic domain antibody, activated form of matriptase
28000
-
Western blot analysis using conditioned medium, catalytic domain of proteolytically active two-chain matriptase C-terminal fragment
29000
-
refolded zymogen
29000
-
amino acids 596-855, theoretical molecular mass
30000
-
catalytic domain, Asp603 - Val855, before treatment with enteropeptidase, determined by SDS-PAGE and Western blot analysis
30000
-
serine protease domain, determined by SDS-PAGE and Western blot analysis
30000
-
SDS-PAGE reducing conditions and Western blot using anti-rat matriptase catalytic domain anibody, designated pseudozymogen His6t-S-CD consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase, after cleavage with enterokinase
30000
-
x * 30000, catalytic domain of matriptase-2, SDS-PAGE
30000
-
x * 70000, matriptase zymogen, SDS-PAGE, x * 30000, matriptase serine protease domain, SDS-PAGE
33000
-
SDS-PAGE and Western blot, reducing conditions, proteolytically active, disulfide two-chain matriptase C-terminal fragment found in both the apical and basolateral media of stably transfected Madin-Darby canine kidney cells
33000
-
SDS-PAGE, reducing condition, protease inhibitor cocktail, Western blotting using an anti-myc antibody in a sample of medium, two bands 93 kDa and 33 kDa are visible, 33 kDa fragment is a cleavage product of the carboxyl-terminal part
70000
SDS-PAGE
70000
-
non-complexed form, SDS-PAGE
70000
-
immunoblotting, latent NH2 terminal processed form matripase
70000
-
SDS-PAGE, reducing condition, and Western blot, latent form of matriptase
70000
-
x * 70000, SDS-PAGE
70000
x * 70000, SDS-PAGE
70000
1 * 70000 + 1 * 240000, complex purified from milk, SDS-PAGE
70000
-
x * 70000, inactive zymogen, SDS-PAGE
70000
-
x * 70000, matriptase zymogen, SDS-PAGE, x * 30000, matriptase serine protease domain, SDS-PAGE
75000
calculated from nucleic acid sequence
75000
-
by immunoblotting or zymography
75000
-
gelatin zymography, soluble active enzyme
75000
-
x * 75000, native enzyme, SDS-PAGE
80000
noncomplexed form purified from T47D cells, SDS-PAGE
80000
-
SDS-PAGE, recombinant protease domain
80000
-
immunoblotting, membrane-bound enzyme
80000
serine protease domain, identified by SDS-PAGE, Western blot analysis and LC-MS,MS, including serpin complex
80000
-
x * 95000, full-length transmembrane isoform, SDS-PAGE, x * 80000, Gly149-early processed isoform, SDS-PAGE, x * 26000-29000, activated recombinant truncated wild-type catalytic domain, SDS-PAGE
85000
-
and 95000 Da, SDS-PAGE, complex derived from milk
85000
-
SDS-PAGE, full length enzyme
85000
-
immunoblotting, full-length hepatocyte growth factor activator inhibitor-1 complexed with the serine protease domain of matripase
85000
-
SDS-PAGE and Western blot, reducing conditions, cleaved form of the enzyme
85000
-
Western blot analysis using seminal fluid, seminal fluid contains only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 (HAI-1), supposed 70 kDa active matriptase and a 15 kDa HAI-fragment
90000
-
Western blot analysis, post-translational processed enzyme, cleavage between Gly149 and Ser150 within the SEA domain
90000
-
SDS-PAGE and Western blot analysis, reducing conditions, non-activated enzyme, single-chain C-terminal fragment
90000
-
SDS-PAGE under reducing conditions followed by Western blotting using an anti-matriptase catalytic domain antibody, non-activated C-terminal part
90000
-
SDS-PAGE under reducing conditions followed by Western blotting using an anti-matriptase catalytic domain antibody, non-activated form of matriptase
90000
-
Western blot analysis using conditioned medium, proteolytically inactive single-chain C-terminal fragment
90000
-
x * 90000, SDS-PAGE
93000
-
immunoblotting, latent full-length matripase
93000
-
SDS-PAGE and Western blot, reducing conditions, proteolytically inactive, single-chain matriptase C-terminal fragment found in both the apical and basolateral media of stably transfected Madin-Darby canine kidney cells
93000
-
SDS-PAGE, reducing condition, protease inhibitor cocktail, Western blotting using an anti-myc antibody in a sample of medium, two bands 93 kDa and 33 kDa are visible. 93 kDa fragment represents released single-chain carboxyl-terminal part
95000
-
and 85000 Da, SDS-PAGE, complex derived from milk
95000
complex can be converted by boiling to matriptase plus a 40000 Da protein doublet
95000
complexed with HAI-1, purified from milk, SDS-PAGE
95000
-
gelatin zymography or immunoblotting, matripase/hepatocyte growth factor activator inhibitor complex
95000
-
extracellular domains, Tyr81 - Val855, before treatment with enteropeptidase, determined by SDS-PAGE and Western blot analysis
95000
-
Western blot analysis using seminal fluid or urine, seminal fluid or urine contain only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 (HAI-1), supposed 70 kDa active matriptase and a 25 kDa HAI-fragment
95000
-
Western blot analysis, reducing conditions
95000
-
x * 95000, full-length transmembrane isoform, SDS-PAGE, x * 80000, Gly149-early processed isoform, SDS-PAGE, x * 26000-29000, activated recombinant truncated wild-type catalytic domain, SDS-PAGE
95000
-
x * 95000, single-chain latent enzyme, SDS-PAGE, x * 120000, active enzyme in complex with inhibitor HAI-1, SDS-PAGE
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A118D
-
mutation causes an intra-molecular structural imbalance that impairs matriptase-2 activation
A757S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
A757S/L785S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
D217A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
D482Y
-
inhibited activation of matriptase
D519Y
-
inhibited activation of matriptase
D521N
point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin
D555Y
-
inhibited activation of matriptase
D598Y
-
inhibited activation of matriptase
D60A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
D799A
-
matripase mutant altered in the substrate binding pocket, is able to traffic in the absence of hepatocyte growth factor activator inhibitor-1
D96A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
E169A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
E522K
point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin
E712Y
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
E712Y/A757S/L785S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
F94A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
F97A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
F99A
-
site-directed mutagenesis, inactive mutant
G149N
-
results in production of only nonprocesse, full-lenth matriptase
G442R
matriptase-2 containing the point mutation G442R located in the second CUB domain demonstrate impaired autoactivation, are still able to bind but demonstrate reduced cleavage of coexpressed hemojuvelin, and exhibit reduced ability to repress HAMP reporter expression
H143A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
H665F
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
I41A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
I60A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
K224A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
L153A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
L785S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
N109Q
-
no reduced formation of matriptase-HAI-1-complex
N164Q
mutation introduced to avoid N-glycosylation
N164Q/R614A
mutation at activation cleavage site, variant is locked in the zymogen form, about 3% of wild-type activity
N164Q/R614A/S805A
mutation at activatio, plus mutant cleavage site, variant is locked in the zymogen form, plus mutation S805A to prevent unwanted proteolytic degradation during crystallization
N95A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q145A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q174A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q175A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q192A
-
site-directed mutagenesis, inactive mutant
Q221A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q38A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
R222A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
R60A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
R87A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
T150A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
T98A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
W215A
-
site-directed mutagenesis, inactive mutant
Y146A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
MT2MASK
-
matriptase-2 mutant lacking the serine protease domain
R599X
-
point mutation identified in zorro mice causing premature termination of matriptase-2 and an iron deficiency phenotype
W783X
-
point mutation identified in masquerade mice causing premature termination of matriptase-2 and an iron deficiency phenotype
D603-V855
-
using CHO-K1 cells, a secreted variant of rat r-matriptase consisting of the of the catalytic domain (and its N-terminal spacer region) (Asp603Val855) L-matriptase is produced. HL-matriptase and L-matriptase are inhibited by purified maHAI-1 with a similar extent when t-butyloxycarbonyl-Gln-Ala-Arg-MCA and acetyl-Lys-Thr-Lys-Gln-Leu-Arg-MCA are were used as substrates
DELTA1-603
-
variant in which the catalytic domain and its N-terminal spacer region (Cys604-Val855) are deleted from matriptase: variant indicates that the catalytic domain is critical for the release of the C-terminal fragment from the cell surface
G149N
-
mutant G149 fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus. This mutant is impaired with respect to the generation of an N-terminus at Ser-150. When probed with an anti-Myc antibody no signals for matriptase C-terminal fragment is detected
N772Q
-
Asn772 is N-glycosylated. Mutant N772Q consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus is not detected in the medium conditioned by transfected cells but is on the cell surface and purified mutant N772Q exhibits markedly reduced activity toward peptide substrate methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide acetate
Y81-V855
-
using CHO-K1 cells, a secreted variant of rat r-matriptase consisting of the entire extracellular domains (Tyr81-Val855) HL-matriptase is produced (variant contains the stem domain). HL-matriptase and L-matriptase are inhibited by purified maHAI-1 with a similar extent when t-butyloxycarbonyl-Gln-Ala-Arg-MCA and acetyl-Lys-Thr-Lys-Gln-Leu-Arg-MCA are were used as substrates. HL-matriptase is inhibited more strongly than L-matriptase by maHAI-1 in the hydrolysis of t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-MCA. The stem domain of matriptase facilitates the inhibitory interaction of this protease with maHAI-1 in the hydrolysis of t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-MCA
G827R
a naturally occuring missense mutation in the highly conserved peptidase S1S6 domain, causing autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, phenotype, overview
G827R
-
naturally occurring mutation, the rare congenital human disorder, autosomal recessive ichthyosis with hypotrichosis is linked to homozygosity for a C2672GA mutation located in exon 19 of the ST14 gene, phenotype, overview
G827R
-
the mutation in the catalytic domain causes autosomal recessive Ichthyosis with hypotrichosis, the G827R mutant is catalytically inactive and does not perform autoproteolysis due to a blockade of access to the binding/catalytic cleft of the enzyme, molecular modeling, overview, elevated expression levels compared to the wild-type enzyme, the G827R substitution does not impair the ability of the protease to localize at the cell surface
N302Q
-
reduced formation of matriptase-HAI-1-complex
N302Q
-
significant resistance to degradation in the N-acetylglucosminyltransferase V transfectants
N485Q
-
no reduced formation of matriptase-HAI-1-complex
N485Q
-
significant resistance to degradation in the N-acetylglucosminyltransferase V transfectants
N772Q
-
reduced formation of matriptase-HAI-1-complex
N772Q
-
completely degraded in the N-acetylglucosminyltransferase V transfectants
R774C
-
inactive mutant
R774C
point mutation identified in an iron-refractory iron deficiency anemia patient is located in the protease domain and disrupts accurate C32/C36 or C35/C37 disulfide bonding within the protease domain
S762A
-
catalytically inactive
S762A
protease dead mutation is shown in vitro to be ineffective in repressing Hamp1 reporter expression
S805A
-
inactive
S805A
-
matripase mutant altered in the catalytic triad, is able to traffic in the absence of hepatocyte growth factor activator inhibitor-1
S805A
-
mutation of a catalytic residue, inactive mutant, elevated expression levels compared to the wild-type enzyme
S805A
-
active-site serine is mutated to alanine, no 28 kDa is produced form either medium or cell membrane samples when expressed in COS-1 cells, suggesting that activation cleavage of wild-type-matriptase in COS-1 cells occurs via a mechanism requiring its active site
S805A
-
mutant is unable to undergo activation when expressed in MDCK cells
additional information
-
enzyme and hepatocyte growth factor activator inhibitor-1, Hai1, deficient phenotype, hai1 mutant defects are rescued by inactivation of matriptase1a, overview
additional information
-
enzyme overexpressions and clinical outcome, overview
additional information
-
generation of the 26 kDa soluble form in matriptase expressing cells is not strictly autocatalytic and may involve other proteases
additional information
genotyping and mutation mapping, overview
additional information
-
mutations in any of the residues of the catalytic triad render matriptase unable to undergo activation site cleavage, inactivating mutations in the Ca2+-binding motifs of any or all of the four LDLRA domains prevents the activation of matriptase
additional information
-
pathogenesis of dysregulated matriptase activity, dysregulated matriptase potently supports epithelial transformation, overview
additional information
-
small interfering RNAs for matriptase efficiently block both the matriptase expression and the cleavage of IGBP-rP1 in OVISE cells
additional information
-
when implanting enzyme overexpressing Mat-AZ521 cells into nude mice subcutaneously or intraperitoneally, Mat-AZ521 cells grew faster and produced much larger solid tumors than the control cells, overexpression shortened the survival time of tumor-bearing mice, number and the size of blood vessels in tumor tissues are significantly higher in the Mat-AZ521 tumors than in the control cells
additional information
-
penta-alanine mutants 2-8 and 7-11 show 4 and 4.5fold enhanced proteolytic activity as compared to the wild type enzyme, respectively
additional information
costruction of enzyme mutants with deletion of first 9 amino acids or the first 46 amino acids
additional information
-
siRNA knockdown of the enzyme in MCF-7 cells using three independent non-overlapping synthetic RNA duplexes
additional information
siRNA knockdown of the enzyme in MCF-7 cells using three independent non-overlapping synthetic RNA duplexes
additional information
-
siRNA silencing of matriptase expression
additional information
-
construction of matriptase knockout mice
additional information
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genetic ablation of the enzyme in hepatocyte growth factor activator inhibitor-1-deficient embryos restores the integrity of chorionic trophoblasts and enables placental labyrinth formation and development in turn, which otherwise is prevented, overview, phenotype of single enzyme knockout and double enzyme and inhibitor knockout mutant embryos, overview
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matriptase depletion results in postnatal death of the mice due to dehydration which is caused by a lack of epithelial barrier function in the skin of newborns, these matriptase knockout mice also have abnormal hair follicle development and disturbed thymic homeostasis showing increased lymphocyte apoptosis in the thymuses and profilaggrin accumulation in epidermal tissue, transgenic mice with increased expression of matriptase in the epidermis show induction of spontaneous squamous cell carcinomas and strongly potentiated chemical skin carcinogenesis, possibly through activation of the tumor-promoting PI3K-Akt pathway, while double transgenic mice co-expressing matriptase and its cognate inhibitor HAI-1 do not develop spontaneous skin cancers and do not show increased susceptibility to chemical carcinogenesis
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matriptase-deficient mice develop normally, but do not survive postnatally owing to an epidermal barrier defect, transgenic mice with a very modest overexpression of matriptase in the skin become remarkably susceptible to carcinogen-induced tumour formation
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null mice show impaired development of the hair follicles and immune system and are unable to survive 48 hours past birth due to rapid dehydration through an abnormally formed epidermal barrier
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phenotype of enzyme-deficient mice and pathogenesis of dysregulated matriptase activity, overview, early lethality of ST14 null mice, transgenic mice expressing modest levels of matriptase in basal keratinocytes display progressive epidermal hyperplasia with fibrosis and dermal inflammation, which spontaneously progresses to invasive squamous cell carcinoma
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a construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus shows comparable kinetic activity to the full-length rat matriptase toward peptide substrate methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide acetate
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a full-length rat matriptase and a chimera consisting of the cytoplasmic and transmembrane regions of the matriptase and green fluorescent protein (designated as 1-86GFP) are found to localize exclusively to the basolateral membrane domain when expressed in Madin-Darby canine kidney epithelial cells
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engineered L-Matriptase is a secreted variant of r-matriptase in which the cytosolic, signal anchor, and stem domains (Met1-Asp603) are replaced with the human immunoglobulin kappa-chain signal peptide and S-tag (ST). L-Matriptase is produced in CHO-K1 cells and is converted to an active form via cleavage with recombinant enterokinase
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four matriptase pseudozymogens containing at least the catalytic domain are constructed. Each plasmid is expressed as His-tagged fusion proteins and contains a site for activation by recombinant enterokinase. Pseudozymogens with His6-tag at their C-termini form multimers linked by intermolecular disulfide bonds. After treatment with r-EK, they exhibit no detectable hydrolytic activity. Designated pseudozymogen His6t-S-CD consisting of a spacer and the catalytical domain with an N-terminal His6-tag is secreted as a monomer. After recombinant enterokinase treatment pseudozymogen His6t-S-CD exhibits enzymatic activity comparable to secreted variant L-matriptase
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preparation of a matriptase pseudozymogen (HL-matriptase zymogen): secreted variant of matriptase consisting of the entire extracellular domain (Tyr81 to Val855), activation-cleavage sequence (Thr-Lys-Gln-Ala-Arg614) is replaced with the enterokinase recognition sequence (Asp-Asp-Asp-Asp-Lys). Pseudozymogen is converted to HL-matriptase enzyme (activated) by incubation with enterokinase. Pseudozymogen exhibits optimal activity toward substrate acetyl-Lys-Thr-Lys-Gln-Leu-Arg-methyl-coumaryl-7-amide at pH 6.0 (mildly acidic). Substrate hydrolysis at pH 6.0 with 145 mM NaCl is inhibited. In a buffer of pH 6.0 containing 5 mM NaCl (low ionic strength), the activity of pseudozymogen is only 30times lower than that of the respective two-chain form (activated form after enterokinase treatment). This finding indicates that the in vivo activation of matriptase occurs via a mechanism involving the activity of zymogen
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