Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe + norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-Ser-Asp-Lys(Tfa)-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe + Ser-Asp-Lys(Tfa)-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-Ser-Asp-Met(O)-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe + Ser-Asp-Met(O)-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe-norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe + norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe-norvaline-Asp-Met(O)2-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe + norvaline-Asp-Met(O)2-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
4-(((S)-3-methyl-1-((S)-2-(((S)-1-((4-nitrophenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamoyl)pyrrolidin-1-yl)-1-oxobutan-2-yl)amino)-4-oxobutanoic acid + H2O
?
-
-
-
-
?
4-carboxybutyryl-Phe-2-naphthyl ester + H2O
4-carboxybutyryrl-Phe + 2-naphthol
-
-
-
ir
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
Abz-APEEIMRRQ-EDDnp + H2O
Abz-APEEI + MRRQ-EDDnp
-
-
-
-
?
Abz-EPFWEDQ-EDDnp + H2O
?
-
-
-
?
Abz-GIAPFCDLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFCDLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFCMLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFCPLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFCRLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFDMLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFRMLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFSMLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIATFWMLMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIEPFSDPMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIEPKSDPMPEQ-EDDnp + H2O
?
-
-
-
?
Abz-GIEPKSDPMPEQ-N-EDDnp + H2O
?
-
-
-
?
Abz-TPFSALQ-EDDnp + H2O
?
-
-
-
?
Abz-TPKSALQ-EDDnp + H2O
?
-
-
-
?
Abz-TPWSALQ-YNO2 + H2O
?
-
-
-
?
Abz-VADnVRDRQ-EDDnp + H2O
Abz-VADnVR + DRQ-EDDnp
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-amino-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-amino-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-carboxy-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-carboxy-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-COOCH3-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-COOCH3-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-cyano-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-cyano-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-guanidyl-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-guanidyl-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-nitro-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-nitro-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Arg-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Arg + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Lys-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Lys + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Phe-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Phe + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Tyr-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Tyr + 5-amino-2-nitrobenzamide
-
-
-
-
?
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2 + H2O
?
-
chromogenic cathepsin G substrate
-
-
?
angiotensin I + H2O
angiotensin II + ?
angiotensinogen + H2O
angiotensin I + ?
angiotensinogen + H2O
angiotensin II + ?
CD40L + H2O
?
-
low activity
-
-
?
complement component C3 + H2O
complement component C3a + complement component C3b
-
-
-
?
Elastin + H2O
Fragments of elastin
-
-
-
-
?
factor IX + H2O
?
-
-
-
-
?
factor VII + H2O
?
-
-
-
-
?
factor VIII + H2O
factor VIIIa + peptide
factor VIIIa + H2O
factor VIII + peptide
Fibronectin + H2O
?
-
hydrolysis after methionine, leucine, phenylalanine, lysine, or arginine residues
-
?
fibronectin + H2O
fragments of fibronectin
fibronectin + H2O
peptide fragments
glycoprotein Ibalpha subunit + H2O
?
-
from the glycoprotein Ib-IX receptor of human platelets
-
-
?
hemagglutinin + H2O
?
-
assay at pH 5.0, 37°C
-
-
?
high molecular mass kininogen + H2O
peptide fragments
-
human, 120 kDa
after 1 min reaction: 110, 100, and 75 kDa fragments, after 5 min reaction: 10 to 70 kDa fragments, after 60 min: less than 20 kDa fragments
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
human recombinant B-cell activating factor + H2O
?
-
low activity
-
-
?
intercellular adhesion molecule-1 + H2O
fragments
interleukin-15 + H2O
?
-
-
-
-
?
interleukin-17A + H2O
?
-
low activity
-
-
?
interleukin-18 + H2O
?
-
-
-
-
?
interleukin-2 + H2O
?
-
low activity
-
-
?
interleukin-21 + H2O
?
-
low activity
-
-
?
interleukin-22 + H2O
?
-
low activity
-
-
?
interleukin-24 + H2O
?
-
low activity
-
-
?
interleukin-3 + H2O
?
-
-
-
-
?
interleukin-31 + H2O
?
-
efficient substrate
-
-
?
interleukin-33 + H2O
?
-
-
-
-
?
interleukin-36gamma + H2O
?
-
-
-
-
?
interleukin-6 + H2O
?
-
efficient substrate
-
-
?
interleukin-7 + H2O
?
-
efficient substrate
-
-
?
Laminin + H2O
?
-
hydrolysis after methionine, leucine, phenylalanine, lysine, or arginine residues
-
?
laminin + H2O
fragments of laminin
low-density lipoprotein + H2O
?
MARS123 + H2O
?
-
i.e. bis(4-methoxyphenyl) (1-((S)-1-((5-((3aS,4S,6aR)-3a,6a-dimethyl-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoyl)-L-valyl)pyrrolidine-2-carboxamido)-3-methylbutyl)phosphonate. The reaction occurs in the presence of lactoferrin only
-
-
?
MARS125 + H2O
?
-
i.e. diphenyl(1-((S)-1-((5-((3aS,4S,6aR)-3a,6adimethyl-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoyl)-L-valyl)pyrrolidine-2-carboxamido)-2-methylpropyl)phosphonate. The reaction occurs in the presence of lactoferrin only
-
-
?
membrane-bound stem cell factor + H2O
?
-
-
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
myelin basic protein + H2O
myelin basic protein peptide fragments
N-acetyl-L-Phe-p-nitrophenyl ester + H2O
?
N-acetyl-L-phenylalanyl-L-valyl-L-threonyl-N-(5-amino-2-nitrobenzoyl)-3-pyridin-4-yl-L-alaninamide) + H2O
N-acetyl-L-phenylalanyl-L-valyl-L-threonyl-3-pyridin-4-yl-L-alanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
N-carbobenzyloxy-L-Lys-thiobenzylester + H2O
?
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
-
chromogenic substrate
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
N-succinyl-Phe-Leu-Phe-thiobenzyl ester + H2O
?
-
chromogenic substrate
-
?
protease-activated receptor-1 + H2O
?
-
i.e. PAR1, activation of platelets by hydrolysis of the receptor protein
-
?
protease-activated receptor-4 + H2O
?
-
i.e. PAR4, activation of platelets by hydrolysis of the receptor protein
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
serum amyloid P + H2O
?
-
-
-
-
?
succinyl-AAPF-4-nitroanilide + H2O
succinyl-AAPF + 4-nitroaniline
-
-
-
-
?
succinyl-AAPL-4-nitroanilide + H2O
succinyl-AAPL + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
-
-
-
ir
succinyl-alanyl-alanyl-prolyl-phenylalanyl-aminomethyl-coumarin + H2O
?
-
a fluorogenic substrate
-
-
?
succinyl-LLVY-4-nitroanilide + H2O
succinyl-LLVY + 4-nitroaniline
-
-
-
-
?
succinyl-Phe-Leu-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Phe-Leu-Phe-thiobenzyl ester + H2O
?
-
-
-
-
?
tetanus toxin C-fragment + H2O
?
-
assay at pH 5.0, 37°C
-
-
?
thrombospondin + H2O
peptide fragments
von Willebrand factor + H2O
peptide fragments
additional information
?
-
angiotensin I + H2O
angiotensin II + ?
-
-
-
?
angiotensin I + H2O
angiotensin II + ?
-
-
-
?
angiotensinogen + H2O
angiotensin I + ?
-
-
-
?
angiotensinogen + H2O
angiotensin I + ?
-
-
-
?
angiotensinogen + H2O
angiotensin II + ?
-
-
-
?
angiotensinogen + H2O
angiotensin II + ?
-
-
-
?
cadherin + H2O
?
-
-
-
?
cadherin + H2O
?
-
-
-
-
?
cadherin + H2O
?
-
-
-
-
?
factor VIII + H2O
factor VIIIa + peptide
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, overview
-
-
?
factor VIII + H2O
factor VIIIa + peptide
-
cleavage releases the bound von-Willebrand factor and the corresponding peptide sequence, determination of cleavage sites, overview
-
-
?
factor VIIIa + H2O
factor VIII + peptide
-
-
-
-
?
factor VIIIa + H2O
factor VIII + peptide
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, inactivation occurs due to decreased stability by subsequent dissociation of the A2 subunit following proteolytic cleavage by cathepsin G, overview
-
-
?
fibronectin + H2O
fragments of fibronectin
-
-
-
-
?
fibronectin + H2O
fragments of fibronectin
-
-
-
ir
fibronectin + H2O
fragments of fibronectin
-
degradation, involved in inflammation process
-
ir
fibronectin + H2O
peptide fragments
-
220 kDa substrate in extracellular matrix of human umbilical vein endothelial cells and platelets
162 kDa, 122 kDa, and 92 kDa
?
fibronectin + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
-
i.e. hbrm, cleavage in vitro after induction of apoptosis, cleavage pattern
the 20 kDa fragment contains a bromodomain from the C-terminus of hbrm, the 160 kDa binds less tightly to he nuclear matrix than the full length protein
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
-
i.e. hbrm, nuclear protein in volved in regulation of chromatin conformation
-
?
intercellular adhesion molecule-1 + H2O
fragments
-
i.e. ICAM-1, a membrane glycoprotein consisting of five extracellular Ig-like domains, a transmembrane domain, and a short cytoplasmic tail, all alternate substrate isoforms or mutant substrate forms but the common form, from mouse and human, substrate specificity is influenced by the ability of the ICAM-1 isoforms to form dimers and larger multimeric complexes
-
?
intercellular adhesion molecule-1 + H2O
fragments
-
i.e. ICAM-1, the substrate plays an important role in inflammation and immune response, e.g. to sustain neutrophil infiltration and to confer susceptibility to septic shock, all alternate substrate isoforms but the common form, in model mouse mutants, and in cystic fibrosis patients
-
?
laminin + H2O
fragments of laminin
-
-
-
?
laminin + H2O
fragments of laminin
-
degradation, involved in inflammation process
-
ir
low-density lipoprotein + H2O
?
-
-
-
?
low-density lipoprotein + H2O
?
-
-
-
?
MARS116 + H2O
?
-
i.e. Bt-LC-Suc-Val-Pro-PheP(OPh)2
-
-
?
MARS116 + H2O
?
-
i.e. diphenyl(1-((S)-1-((4-oxo-4-((5-(5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamido)pentyl)amino)butanoyl)-L-valyl)pyrrolidine-2-carboxamido)-2-phenylethyl)phosphonate. The reaction occurs in the presence of lactoferrin only
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
-
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
the serine protease cathepsin G dominates the proteolytic processing of the multiple sclerosis-associated autoantigen myelin basic protein in lysosomes from primary B cells and dendritic cells, overview
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
when microglia are treated with interferon-gamma to mimic a T helper type 1-biased cytokine milieu in multiple sclerosis, CatG is drastically down-regulated resulting in significantly increased stability of myelin basic protein and a selective lack of CatG-derived proteolytic fragments
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
substrate is recombinant purified human myelin basic protein, differential processing patterns, overview
determination of proteolysis products
-
?
N-acetyl-L-Phe-p-nitrophenyl ester + H2O
?
-
-
-
-
?
N-acetyl-L-Phe-p-nitrophenyl ester + H2O
?
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
assay at pH 7.5, 37°C
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
assay at 37°C
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
assay at pH 7.4, 25°C
-
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
-
cell-associated N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
-
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
-
N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
thrombospondin + H2O
peptide fragments
-
preferred substrate, 180 kDa substrate in extracellular matrix of human umbilical vein endothelial cells and platelets
155 kDa and 25 kDa
?
thrombospondin + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
von Willebrand factor + H2O
peptide fragments
-
280 kDa substrate in extracellular matrix of human umbilical vein endothelial cells and platelets
260-177 kDa and 177-136 kDa
?
von Willebrand factor + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
additional information
?
-
-
no activity with PAR1-mutant A2F and PAR4 mutant G1P
-
?
additional information
?
-
-
enzyme causes platelet secretion and aggregation mediated by protease-activated receptor-4, i.e. PAR4, triggers calcium mobilization in PAR4-transfected fibroblasts, PAR4-expressing Xenopus oocytes, and washed human platelets, enzyme might mediate platelet-neutrophil interaction at sites of vascular injury or inflammation, regulation of enzyme activity on platelets and protease-activated receptors-1 and -4
-
?
additional information
?
-
-
enzyme is involved in pathological processes of inflammation
-
?
additional information
?
-
-
the enzyme can directly alter platelet function and/or participate in coagulation cascade reactions on the platelet or neutrophil surface to enhance fibrin formation, coagulation pathway overview
-
?
additional information
?
-
-
the enzyme induces cell proliferation, cytokine productionand IFN-gamma production in normal spleen cells and T lymphocytes from mice
-
?
additional information
?
-
-
the enzyme induces chemotaxis and production of proinflammatory cytokines by macrophages but not by CD4+ T cells, pretreatment of macrophages, but not CD4+ T cells, increases susceptibility to acute HIV-infection, the enzyme has mutiple activities in HIV-type1 infection of macrophages, long-term exposure to cathepsin G suppresses HIV infection of macrophages, the effect is neutralized by serine protease inhibitors
-
?
additional information
?
-
-
the enzyme probably represents an alternative pathway that modulates the expression of intercellular adhesion molecule-1 on the cell surface
-
?
additional information
?
-
-
cathepsin G and neutrophil elastase are involved in responses of polymorphonucleocytes to various stimuli. When released at sites of inflammation, they participate in the degradation of numerous proteins involved in the regulation of the immune response. the ability of cathepsin G and neutrophil elastase to modulate levels of membrane and soluble forms of tumor necrosis factor alpha may contribute to the proinflammatory activity of neutrophils
-
-
?
additional information
?
-
-
cathepsin G controls the processing of myelin basic protein in lysosomes from human B lymphocytes
-
-
?
additional information
?
-
-
cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
-
-
?
additional information
?
-
-
hypochlorous acid, a specific product of myeloperoxidase, potently inactivates cathepsin G by a pathway that involves oxidation of a specific methionine residue, which in turn may disrupt the catalytic charge relay system and introduce proteolytic cleavage sites into the enzyme. This finding raises the possibility that myeloperoxidase might restrain the activity of cathepsin G near the surface of neutrophils
-
-
?
additional information
?
-
-
in stenotic aortic valves, mast cell-derived cathepsin G may cause adverse valve remodelling and progression of aortic stenosis
-
-
?
additional information
?
-
-
Mycobacterium tuberculosis infection results in a cathepsin switch with down-regulation of cathepsin G rendering Mycobacterium tuberculosis bacilli more viable. Downregulation of cathepsin G in macrophages is advantageous to Mycobacterium tuberculosis bacilli and possibly is an important mechanism by which Mycobacterium tuberculosis is able to evade the host immune defense
-
-
?
additional information
?
-
-
neutrophil elastase and cathepsin G induce the formation of highly aggregated multicellular 3-D spheroids of MCF-7 cells. Neutrophil elastase and cathepsin G might be involved in the dissemination of tumor clumps and formation of emboli in tumor metastasis
-
-
?
additional information
?
-
-
release of leukocyte elastase or cathepsin G from neutrophils specifically down-regulates the responsiveness of neutrophils to C5a. Elastase and cathepsin G may therefore play an important role in the down-regulation of acute inflammation
-
-
?
additional information
?
-
-
the enzyme is a chemotactic agonist for G protein-coupled formyl peptide receptor
-
-
?
additional information
?
-
-
cathepsin G acts as a monocyte chemoattractant in rheumatoid arthritis inducing monocyte migration, overview
-
-
?
additional information
?
-
the enzyme is one of the major components of the neutrophil primary granules that participate in the non-oxidative pathway of intracellular pathogen destruction, it helps kill bacterial cells and is involved in the degradation of extracellular matrix components during acute and chronic inflammation, the enzyme is important in regulation of immune response, control of cellular signaling through the procession of cytokines and modulation of the cytokine network, biological functions and roles in diseases of cathepsin G, overview
-
-
?
additional information
?
-
-
the enzyme is one of the major components of the neutrophil primary granules that participate in the non-oxidative pathway of intracellular pathogen destruction, it helps kill bacterial cells and is involved in the degradation of extracellular matrix components during acute and chronic inflammation, the enzyme is important in regulation of immune response, control of cellular signaling through the procession of cytokines and modulation of the cytokine network, biological functions and roles in diseases of cathepsin G, overview
-
-
?
additional information
?
-
cathepsin G prefers aromatic or positively charged residues at P1 position, e.g. Phe, Tyr, Lys, or Arg, substrate specificity and active site structure analysis, overview
-
-
?
additional information
?
-
-
cathepsin G prefers aromatic or positively charged residues at P1 position, e.g. Phe, Tyr, Lys, or Arg, substrate specificity and active site structure analysis, overview
-
-
?
additional information
?
-
-
specificity with synthetic fluorogenic/chromogenic substrates, preference for aromatic residues at P1 position, specificity at other positions, overview
-
-
?
additional information
?
-
-
specificity with synthetic fluorogenic/chromogenic substrates, the enzyme prefers Ser at P1' position and Trp at the P2' position, overview
-
-
?
additional information
?
-
-
cathepsin G shows a concentration-dependent induction of monocyte chemotaxis. At the highest concentrations, it induced chemotaxis similar to MCP-1, a known monocyte chemoattractant
-
-
?
additional information
?
-
-
human cathepsin G has broad chymotryptic activity, cleaving after Trp, Phe, and Tyr, with little preference for Tyr versus Phe. It also has substantial Leu-ase and Met-ase activity, with little or no ability to cleave after P1 acidic residues (granzyme B-like Asp-ase activity) and small aliphatic residues (neutrophil elastase-like activity). Its most unique feature, however, is tryptic activity, which is as strong as its Tyr-cleaving chymotryptic activity and is largely Lys-specific
-
-
?
additional information
?
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
The enzyme has a dual specificity consisting of chymase and tryptase-type activities. Phe, Tyr, Trp and Leu are preferred in the P1 position. The enzyme has a preference for negatively charged amino acids in the P2A position of substrates and a preference for aliphatic amino acids both upstream and downstream of the cleavage site
-
-
?
additional information
?
-
-
the extended cleavage sites for the enzyme contain about 8 amino acids, and cleavage normally occurs after an aromatic amino acid (phenylalanine, tyrosine and tryptophan or leucine) in the P1 substrate position
-
-
?
additional information
?
-
-
lactoferrin is not proteolytically degraded by the enzyme
-
-
?
additional information
?
-
-
no activity with interleukin-4, interleukin-5, or interleukin-10
-
-
?
additional information
?
-
-
no activity with succinyl-AAPI-4-nitroanilide, succinyl-AAPA-4-nitroanilide, succinyl-AAPV-4-nitroanilide, succinyl-VLGR-4-nitroanilide, Z-GPR-4-nitroanilide, acetyl-YVAD-4-nitroanilide, acetyl-VEID-4-nitroanilide, and acetyl-IEPD-4-nitroanilide
-
-
?
additional information
?
-
-
cathepsin G as a critical component sustaining neutrophil-mediated acute tissue pathology and subsequent fibrosis after renal ischemia/reperfusion injury, cathepsin G is required for sustained inflammation and tissue injury after reperfusion of ischemic kidneys, overview
-
-
?
additional information
?
-
-
the neutrophil-derived serine protease cathepsin G inhibits the murine hosts ability to clear Pseudomonas aeruginosa, an infection in cystic fibrosis airways causing intense inflammation, from the lung, murine model of endobronchial inflammation, overview
-
-
?
additional information
?
-
-
cathepsin G shows a concentration-dependent induction of monocyte chemotaxis. At the highest concentrations, it induced chemotaxis similar to MCP-1, a known monocyte chemoattractant
-
-
?
additional information
?
-
-
enzyme enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-KB ligand. It is significantly up-regulated at the tumor-bone interface and is capable of generating sRANKL, which potentially enhances osteoclast activation and osteolysis
-
-
?
additional information
?
-
-
the mouse enzyme lacks the tryptic, Leu-ase and Met-ase activity of the human enzyme, and even its chymotryptic profile is narrower, showing preference for Tyr over Phe and little inclination to cleave after Trp
-
-
?
additional information
?
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
enzyme enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-KB ligand. It is significantly up-regulated at the tumor-bone interface and is capable of generating sRANKL, which potentially enhances osteoclast activation and osteolysis
-
-
?
additional information
?
-
-
the neutrophil-derived serine protease cathepsin G induces neonatal cardiomyocyte detachment and apoptosis by anoikis, which requires matrix metalloproteinase-dependent membrane shredding of epidermal growth factor, signaling induction by the enzyme via epidermal growth factor receptor induction and transactivation, mechanism, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
angiotensin I + H2O
angiotensin II + ?
angiotensinogen + H2O
angiotensin I + ?
angiotensinogen + H2O
angiotensin II + ?
CD40L + H2O
?
-
low activity
-
-
?
Elastin + H2O
Fragments of elastin
-
-
-
-
?
factor VIII + H2O
factor VIIIa + peptide
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, overview
-
-
?
factor VIIIa + H2O
factor VIII + peptide
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, inactivation occurs due to decreased stability by subsequent dissociation of the A2 subunit following proteolytic cleavage by cathepsin G, overview
-
-
?
fibronectin + H2O
fragments of fibronectin
fibronectin + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
-
i.e. hbrm, nuclear protein in volved in regulation of chromatin conformation
-
?
human recombinant B-cell activating factor + H2O
?
-
low activity
-
-
?
intercellular adhesion molecule-1 + H2O
fragments
-
i.e. ICAM-1, the substrate plays an important role in inflammation and immune response, e.g. to sustain neutrophil infiltration and to confer susceptibility to septic shock, all alternate substrate isoforms but the common form, in model mouse mutants, and in cystic fibrosis patients
-
?
interleukin-15 + H2O
?
-
-
-
-
?
interleukin-17A + H2O
?
-
low activity
-
-
?
interleukin-18 + H2O
?
-
-
-
-
?
interleukin-2 + H2O
?
-
low activity
-
-
?
interleukin-21 + H2O
?
-
low activity
-
-
?
interleukin-22 + H2O
?
-
low activity
-
-
?
interleukin-24 + H2O
?
-
low activity
-
-
?
interleukin-3 + H2O
?
-
-
-
-
?
interleukin-31 + H2O
?
-
efficient substrate
-
-
?
interleukin-33 + H2O
?
-
-
-
-
?
interleukin-36gamma + H2O
?
-
-
-
-
?
interleukin-6 + H2O
?
-
efficient substrate
-
-
?
interleukin-7 + H2O
?
-
efficient substrate
-
-
?
laminin + H2O
fragments of laminin
-
degradation, involved in inflammation process
-
ir
low-density lipoprotein + H2O
?
membrane-bound stem cell factor + H2O
?
-
-
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
RANTES 1-68 + H2O
RANTES 4-68 + peptide
-
cell-associated N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
-
-
?
serum amyloid P + H2O
?
-
-
-
-
?
thrombospondin + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
von Willebrand factor + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
additional information
?
-
angiotensin I + H2O
angiotensin II + ?
-
-
-
?
angiotensin I + H2O
angiotensin II + ?
-
-
-
?
angiotensinogen + H2O
angiotensin I + ?
-
-
-
?
angiotensinogen + H2O
angiotensin I + ?
-
-
-
?
angiotensinogen + H2O
angiotensin II + ?
-
-
-
?
angiotensinogen + H2O
angiotensin II + ?
-
-
-
?
cadherin + H2O
?
-
-
-
?
cadherin + H2O
?
-
-
-
-
?
cadherin + H2O
?
-
-
-
-
?
fibronectin + H2O
fragments of fibronectin
-
-
-
-
?
fibronectin + H2O
fragments of fibronectin
-
degradation, involved in inflammation process
-
ir
low-density lipoprotein + H2O
?
-
-
-
?
low-density lipoprotein + H2O
?
-
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
the serine protease cathepsin G dominates the proteolytic processing of the multiple sclerosis-associated autoantigen myelin basic protein in lysosomes from primary B cells and dendritic cells, overview
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
when microglia are treated with interferon-gamma to mimic a T helper type 1-biased cytokine milieu in multiple sclerosis, CatG is drastically down-regulated resulting in significantly increased stability of myelin basic protein and a selective lack of CatG-derived proteolytic fragments
-
-
?
additional information
?
-
-
enzyme causes platelet secretion and aggregation mediated by protease-activated receptor-4, i.e. PAR4, triggers calcium mobilization in PAR4-transfected fibroblasts, PAR4-expressing Xenopus oocytes, and washed human platelets, enzyme might mediate platelet-neutrophil interaction at sites of vascular injury or inflammation, regulation of enzyme activity on platelets and protease-activated receptors-1 and -4
-
?
additional information
?
-
-
enzyme is involved in pathological processes of inflammation
-
?
additional information
?
-
-
the enzyme can directly alter platelet function and/or participate in coagulation cascade reactions on the platelet or neutrophil surface to enhance fibrin formation, coagulation pathway overview
-
?
additional information
?
-
-
the enzyme induces cell proliferation, cytokine productionand IFN-gamma production in normal spleen cells and T lymphocytes from mice
-
?
additional information
?
-
-
the enzyme induces chemotaxis and production of proinflammatory cytokines by macrophages but not by CD4+ T cells, pretreatment of macrophages, but not CD4+ T cells, increases susceptibility to acute HIV-infection, the enzyme has mutiple activities in HIV-type1 infection of macrophages, long-term exposure to cathepsin G suppresses HIV infection of macrophages, the effect is neutralized by serine protease inhibitors
-
?
additional information
?
-
-
the enzyme probably represents an alternative pathway that modulates the expression of intercellular adhesion molecule-1 on the cell surface
-
?
additional information
?
-
-
cathepsin G and neutrophil elastase are involved in responses of polymorphonucleocytes to various stimuli. When released at sites of inflammation, they participate in the degradation of numerous proteins involved in the regulation of the immune response. the ability of cathepsin G and neutrophil elastase to modulate levels of membrane and soluble forms of tumor necrosis factor alpha may contribute to the proinflammatory activity of neutrophils
-
-
?
additional information
?
-
-
cathepsin G controls the processing of myelin basic protein in lysosomes from human B lymphocytes
-
-
?
additional information
?
-
-
cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
-
-
?
additional information
?
-
-
hypochlorous acid, a specific product of myeloperoxidase, potently inactivates cathepsin G by a pathway that involves oxidation of a specific methionine residue, which in turn may disrupt the catalytic charge relay system and introduce proteolytic cleavage sites into the enzyme. This finding raises the possibility that myeloperoxidase might restrain the activity of cathepsin G near the surface of neutrophils
-
-
?
additional information
?
-
-
in stenotic aortic valves, mast cell-derived cathepsin G may cause adverse valve remodelling and progression of aortic stenosis
-
-
?
additional information
?
-
-
Mycobacterium tuberculosis infection results in a cathepsin switch with down-regulation of cathepsin G rendering Mycobacterium tuberculosis bacilli more viable. Downregulation of cathepsin G in macrophages is advantageous to Mycobacterium tuberculosis bacilli and possibly is an important mechanism by which Mycobacterium tuberculosis is able to evade the host immune defense
-
-
?
additional information
?
-
-
neutrophil elastase and cathepsin G induce the formation of highly aggregated multicellular 3-D spheroids of MCF-7 cells. Neutrophil elastase and cathepsin G might be involved in the dissemination of tumor clumps and formation of emboli in tumor metastasis
-
-
?
additional information
?
-
-
release of leukocyte elastase or cathepsin G from neutrophils specifically down-regulates the responsiveness of neutrophils to C5a. Elastase and cathepsin G may therefore play an important role in the down-regulation of acute inflammation
-
-
?
additional information
?
-
-
the enzyme is a chemotactic agonist for G protein-coupled formyl peptide receptor
-
-
?
additional information
?
-
-
cathepsin G acts as a monocyte chemoattractant in rheumatoid arthritis inducing monocyte migration, overview
-
-
?
additional information
?
-
the enzyme is one of the major components of the neutrophil primary granules that participate in the non-oxidative pathway of intracellular pathogen destruction, it helps kill bacterial cells and is involved in the degradation of extracellular matrix components during acute and chronic inflammation, the enzyme is important in regulation of immune response, control of cellular signaling through the procession of cytokines and modulation of the cytokine network, biological functions and roles in diseases of cathepsin G, overview
-
-
?
additional information
?
-
-
the enzyme is one of the major components of the neutrophil primary granules that participate in the non-oxidative pathway of intracellular pathogen destruction, it helps kill bacterial cells and is involved in the degradation of extracellular matrix components during acute and chronic inflammation, the enzyme is important in regulation of immune response, control of cellular signaling through the procession of cytokines and modulation of the cytokine network, biological functions and roles in diseases of cathepsin G, overview
-
-
?
additional information
?
-
-
cathepsin G shows a concentration-dependent induction of monocyte chemotaxis. At the highest concentrations, it induced chemotaxis similar to MCP-1, a known monocyte chemoattractant
-
-
?
additional information
?
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
The enzyme has a dual specificity consisting of chymase and tryptase-type activities. Phe, Tyr, Trp and Leu are preferred in the P1 position. The enzyme has a preference for negatively charged amino acids in the P2A position of substrates and a preference for aliphatic amino acids both upstream and downstream of the cleavage site
-
-
?
additional information
?
-
-
the extended cleavage sites for the enzyme contain about 8 amino acids, and cleavage normally occurs after an aromatic amino acid (phenylalanine, tyrosine and tryptophan or leucine) in the P1 substrate position
-
-
?
additional information
?
-
-
cathepsin G as a critical component sustaining neutrophil-mediated acute tissue pathology and subsequent fibrosis after renal ischemia/reperfusion injury, cathepsin G is required for sustained inflammation and tissue injury after reperfusion of ischemic kidneys, overview
-
-
?
additional information
?
-
-
the neutrophil-derived serine protease cathepsin G inhibits the murine hosts ability to clear Pseudomonas aeruginosa, an infection in cystic fibrosis airways causing intense inflammation, from the lung, murine model of endobronchial inflammation, overview
-
-
?
additional information
?
-
-
cathepsin G shows a concentration-dependent induction of monocyte chemotaxis. At the highest concentrations, it induced chemotaxis similar to MCP-1, a known monocyte chemoattractant
-
-
?
additional information
?
-
-
enzyme enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-KB ligand. It is significantly up-regulated at the tumor-bone interface and is capable of generating sRANKL, which potentially enhances osteoclast activation and osteolysis
-
-
?
additional information
?
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
enzyme enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-KB ligand. It is significantly up-regulated at the tumor-bone interface and is capable of generating sRANKL, which potentially enhances osteoclast activation and osteolysis
-
-
?
additional information
?
-
-
the neutrophil-derived serine protease cathepsin G induces neonatal cardiomyocyte detachment and apoptosis by anoikis, which requires matrix metalloproteinase-dependent membrane shredding of epidermal growth factor, signaling induction by the enzyme via epidermal growth factor receptor induction and transactivation, mechanism, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11-oxo-beta-boswellic acid
0.01 mM, 30% cathepsin G activity compared to control
2-(N-methyl)benzylamino-3,1-benzoxazin-4-one
-
strongest inhibition
2-amino-3,1-benzoxazin-4-ones
-
non-covalent complex formation, hydrophobic and basic residues at position 2, kinetics of acylation and desacylation, binding at the enzyme's active site
3-O-acetyl-11-oxo-beta-boswellic acid
0.01 mM, 15% cathepsin G activity compared to control
3-O-acetyl-beta-boswellic acid
0.01 mM, 5% cathepsin G activity compared to control
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
-
6-((1'R)-camphanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-((1'R,2'S,5'R)-menthyloxycarbonyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-((1'S)-camphanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
selective inhibition
6-((1'S,2'R,5'S)-menthyloxycarbonyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-(benzoyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
selective inhibition
6-(N-tosyl-L-phenylalanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-(N-tosyl-L-valinyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
alpha-1 proteinase inhibitor
-
-
-
alpha-1-antichymotrypsin
-
-
-
alpha1-Aantichymotrypsin
-
alpha1-protease inhibitor
-
-
Alpha1-proteinase inhibitor
-
alpha1alpha2-macroglobulin
-
-
-
aspartyl protease inhibitor pepstatin
-
-
-
benzyloxycarbonyl-Gly-Leu-Phe-chloromethyl ketone
beta-boswellic acid
0.01 mM, 30% cathepsin G activity compared to control
bis(4-ethylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis(4-methoxyphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
bis(4-methylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis(4-tert-butylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis-naphthyl beta-ketophosphoric acid
-
moderately potent, competitive, reversible, the R-isomer occupies the active site of the enzyme
bis[4-(1,1,3,3-tetramethylbutyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
3% inhibition, 115 microM
bis[4-(1-methylethyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] ([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][(O-tert-butyl-L-threonyl)amino]methyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] [[4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl]([O-tert-butyl-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-threonyl]amino)methyl]phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
CatG-specific inhibitor I
-
reversible inhibitor
-
cathepsin G inhibitor I
-
chymotrypsin inhibitor 1
-
Apis mellifera
-
chymotrypsin inhibitor 2
-
Apis mellifera
-
chymotrypsin inhibitor 3
-
Apis mellifera
-
cysteine protease inhibitor E64
-
-
dermatan sulfate
-
25 kDa, protection of laminin and fibronectin against degradation by cathepsin G
diethyl 1-naphthylmethylphosphonate
-
-
diisopropylfluorophosphate
dinaphthalen-2-yl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
-
diphenyl (4-amino-1-[[(benzyloxy)carbonyl]amino]butyl)phosphonate
-
5% inhibition, 221 microM
diphenyl [(4-aminophenyl)[[(benzyloxy)carbonyl]amino]methyl]phosphonate
-
-
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidoylphenyl)methyl]phosphonate
-
30% inhibition, 112 microM
diphenyl [[[(benzyloxy)carbonyl]amino](6-carbamimidoylnaphthalen-2-yl)methyl]phosphonate
-
5% inhibition, 112 microM
diphenyl [[[(benzyloxy)carbonyl]amino](phenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
glut-11-oxo-beta-boswellic acid
0.01 mM 20% cathepsin G activity compared to control
heparan sulfate
-
60 kDa, protection of laminin and fibronectin against degradation by cathepsin G
heparin
-
12 kDa, 1:1 binding stoichiometry with cathepsin G, protection of laminin and fibronectin against degradation by cathepsin G
high molecular mass kininogen
-
i.e. HK, human, competitive, inhibits platelet activation by the enzyme completely by complex formation with the enzyme
-
JNJ-10311795
inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an opportunity in the treatment of asthma and chronic obstructive pulmonary disease
L-1-tosylamido-2-phenylethyl chloromethyl ketone
-
weak inhibition
L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
L-valyl-N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
-
monocyte neutrophil elastase inhibitor
-
-
mutant R346F of plasminogen activator inhibitor-1
-
-
-
N-acetyl-L-phenylalanyl-L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
N-acetyl-L-phenylalanyl-L-valyl-N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
-
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-chloromethylketone
irreversible inhibitor
N-succinyl-L-Val-L-Pro-L-Phe(OPh)2
-
irreversible CatG inhibitor, complete inhibition at 0.01 mM
N-succinyl-L-Val-L-Pro-L-Phe-(OPh)2
irreversible inhibitor
N-tosyl-L-phenylalanine chloromethyl ketone
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
two times more active against cathepsin G than against trypsin
Na-tosyl-Phe-chloromethylketone
pepstatin
-
15% inhibition after 30 min at 0.1 mM at 25°C
pepstatin A-penetratin
-
-
-
phenylmethylsulfonyl fluoride
plasma serine protease inhibitor ACT
-
-
-
protease inhibitor PI6
-
-
RG1150
-
i.e. carboxymethyl-benzylamide-dextran derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
RG1192
-
i.e. carboxymethyl-benzylamide-dextran sulfate derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
RG1503
-
i.e. carboxymethyl-dextran sulfate derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
secretory leukocyteprotease inhibitor
-
-
Soybean trypsin inhibitor
-
specific Cat-G inhibitor
-
1 microM, decrease of enzyme activity by 43%
-
squamous cell carcinoma antigen 2
-
-
tosylphenylalanyl chloromethane
-
-
ursolic acid
0.01 mM, 80% cathepsin G activity compared to control
[2-(3-methylcarbamoyl-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[2-(3-[(3-benzoylamino-propyl)-methyl-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[2-(3-[(piperidin-4-yl)-methyl-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
reversible, selective, competitive inhibition
[2-(3-[methyl-(diphenyl-ethylcarbamoyl-methyl)-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
strong inhibition
[2-(3-[methyl-(phenethylcarbamoyl-methyl)-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[2-(3-[methyl[1-(2-naphthoyl)piperidin-4-yl]amino]carbonyl]-2-naphthyl)-1-(1-naphthyl)-2-oxoethyl]phosphonic acid
0.0005 mM, 10% cathepsin G activity compared to control
[2-[3-(benzyl-methyl-carbamoyl)-naphthalen-2-yl]-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[Nphe,Npip,Nleu]SFTI-1
-
0.1 mM
[Phe(4-guanidine)]SFTI-1
-
0.1 mM
alpha1-Aantichymotrypsin
-
-
-
alpha1-Aantichymotrypsin
-
acute phase reactant which is up-regulated during inflammation episodes to compensate for the excess of enzymes released from the actvated neutrophils
-
alpha1-Aantichymotrypsin
-
-
alpha1-Aantichymotrypsin
-
-
-
alpha1-Aantichymotrypsin
-
-
-
Alpha1-proteinase inhibitor
-
-
-
Alpha1-proteinase inhibitor
-
-
-
Alpha1-proteinase inhibitor
-
-
-
Alpha1-proteinase inhibitor
-
-
-
alpha2-Macroglobulin
-
-
-
benzyloxycarbonyl-Gly-Leu-Phe-chloromethyl ketone
-
-
benzyloxycarbonyl-Gly-Leu-Phe-chloromethyl ketone
-
i.e. CK-08, specific for cathepsin G
cathepsin G inhibitor I
-
-
-
cathepsin G inhibitor I
-
-
-
cathepsin G inhibitor I
-
-
cathepsin G inhibitor I
-
-
-
cathepsin G inhibitor I
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
Eglin c
-
-
Lys16-aprotinin
-
-
-
Lys16-aprotinin
-
inhibits mutant enzymes A226E and S189A/A226E
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
TPCK, inhibitor of the proteolytic activity of cathepsin G, effectively eliminated cathepsin G-induced chemotaxis of monocytes
N-tosyl-L-phenylalanine chloromethyl ketone
-
TPCK, inhibitor of the proteolytic activity of cathepsin G, effectively eliminated cathepsin G-induced chemotaxis of monocytes
N-tosyl-L-phenylalanine chloromethyl ketone
-
-
Na-tosyl-Phe-chloromethylketone
-
effectively inhibited the action of cathepsin G against the substrate at a concentration of 1 mmol/l
Na-tosyl-Phe-chloromethylketone
-
inhibition of Cathepsin G reduces tumor vascularity
phenylmethylsulfonyl fluoride
-
reversible CatG inhibitor, complete inhibition at 0.01 mM
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
PMSF
-
complete inhibition at 0.2 mM after 20 h at 25°C
PMSF
-
97% inactivation at 0.02 mM in isopropanol, 22°C, reversible
Soybean trypsin inhibitor
-
complete inhibition at 0.2 mM after 30 min at 25°C
-
Soybean trypsin inhibitor
-
-
-
additional information
-
no inhibition by EDTA and leupeptin both at 0.1 mM
-
additional information
-
inhibitors from soybean and lima-bean
-
additional information
-
inhibitors from soybean and lima-bean
-
additional information
-
inhibitors from soybean and lima-bean
-
additional information
-
-
-
additional information
-
-
-
additional information
-
kinetic mechanism of inhibition
-
additional information
-
5kD heparin fragment protects against inhibition by alpha1-antichymotrypsin inhibitor, eglin c and alpha1-proteinase inhibitor; kinetic mechanism of inhibition
-
additional information
-
kinetic mechanism of inhibition
-
additional information
-
sulfonate and phosphate esters
-
additional information
-
inhibition mechanism and kinetics, effect of ionic strength
-
additional information
-
structural features of inhibition, high-throughput screening of a diverse chemical library, lead structure is bis-naphthyl beta-ketophosphoric acid
-
additional information
-
no inhibition by plasminogen activator inhibitor-1
-
additional information
inhibition mechanisms, overview
-
additional information
-
inhibition mechanisms, overview
-
additional information
-
no inhibition by von-Willebrand factor
-
additional information
-
no inhibitory effect: diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate
-
additional information
-
when microglia are treated with interferon-gamma to mimic a T helper type 1-biased cytokine milieu in multiple sclerosis, CatG is drastically down-regulated resulting in significantly increased stability of myelin basic protein and a selective lack of CatG-derived proteolytic fragments, inhibition of serine proteases eliminates differences in lysosomal MBP-processing between resting and IFN-gamma-stimulated microglia
-
additional information
-
wild type mouse cathepsin G is not inhibited by Lys16-aprotinin
-
additional information
-
inhibitors from soybean and lima-bean
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Tschesche, H.; Wenzel, H.R.; Engelbrecht, S.; Schnabel, E.
Cathepsin G
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
164-170
1984
Homo sapiens
-
brenda
Barrett, A.J.
Cathepsin G
Methods Enzymol.
80
561-565
1981
Homo sapiens
brenda
Heck, L.W.; Rostand, K.S.; Hunter, F.A.; Bhown, A.
Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors
Anal. Biochem.
158
217-227
1986
Homo sapiens
brenda
Virca, G.D.; Metz, G.; Schnebli, H.P.
Similarities between human and rat leukocyte elastase and cathepsin G
Eur. J. Biochem.
144
1-9
1984
Homo sapiens, Rattus norvegicus
brenda
Starkey, P.M.; Barrett, A.J.
Human cathepsin G
J. Biochem.
155
273-278
1976
Homo sapiens
brenda
Starkey, P.M.; Barret, A.J.
Neutral proteinases of human spleen. Purification and criteria for homogeneity of elastase and cathepsin G
Biochem. J.
155
255-263
1976
Homo sapiens
brenda
Braun, N.J.; Bodmer, J.L.; Virca, G.D.; Metz-Virca, G.; Maschler, R.; Bieth, J.G.; Schnebli, H.P.
Kinetic studies on the interaction of eglin c with human leukocyte elastase and cathepsin G
Biol. Chem. Hoppe-Seyler
368
299-308
1987
Homo sapiens
brenda
Stein, R.L.; Strimpler, A.M.
Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin
Biochemistry
26
2611-2615
1987
Homo sapiens
brenda
Saklatvala, J.; Barrett, A.J.
Identification of proteinases in rheumatoid synovium. Detection of leukocyte elastase cathepsin G and another serine proteinase
Biochim. Biophys. Acta
615
167-177
1980
Homo sapiens
brenda
Lively, M.O.; Powers, J.C.
Specificity and reactivity of human granulocyte elastase and cathepsin G, porcine pancreatic elastase, bovine chymotrypsin and trypsin toward inhibition with sulfonyl fluorides
Biochim. Biophys. Acta
525
171-179
1978
Homo sapiens
brenda
Powers, J.C.; Gupton, B.F.; Harley, A.D.; Nishino, N.; Whitley, R.J.
Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones
Biochim. Biophys. Acta
485
156-166
1977
Homo sapiens
brenda
Duranton, J.; Adam, C.; Bieth, J.G.
Kinetic mechanism of the inhibition of cathepsin G by alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor
Biochemistry
37
11239-11245
1998
Homo sapiens
brenda
Bania, J.; Stachowiak, D.; Polanowski, A.
Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera
Eur. J. Biochem.
262
680-687
1999
Homo sapiens
brenda
Ermolieff, J.; Boudier, C.; Laine, A.; Meyer, B.; Bieth, J.G.
Heparin protects cathepsin G against inhibition by protein proteinase inhibitor
J. Biol. Chem.
269
29502-29508
1994
Homo sapiens
brenda
Pidard, D.; Renesto, P.; Berndt, M.C.; Rabhi, S.; Clemetsons, K.J.; Chignard, M.
Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ib alpha subunit
Biochem. J.
303
489-498
1994
Homo sapiens
brenda
Hogg, P.J.; Owensby, D.A.; Chesterman, C.N.
Thrombospondin 1 is a tight-binding competitive inhibitor of neutrophil cathepsin G. Determination of the kinetic mechanism of inhibition and localization of cathepsin G binding to the thrombospondin 1 type 3 repeats
J. Biol. Chem.
268
21811-21818
1993
Homo sapiens
brenda
Groutas, W.C.; Brubaker, M.J.; Verkataraman, R.; Epp, J.B.; Stang, M.A.; McClenahan, J.J.
Inhibitors of human neutrophil cathepsin G: structural and biochemical studies
Arch. Biochem. Biophys.
294
114-146
1992
Homo sapiens
-
brenda
Turkington, P.T.
Cathepsin G, a regulator of human vitamin K, dependent clotting factors and inhibitors
Thromb. Res.
67
147-155
1992
Homo sapiens
brenda
Hof, P.; Mayr, I.; Huber, R.; Korzus, E.; Potempa, J.; Travis, J.; Powers, J.C.; Bode, W.
The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities
EMBO J.
15
5481-5491
1996
Homo sapiens
brenda
Mistry, R.; Snashall, P.D.; Totty, N.; Guz, A.; Tetley, T.D.
Purification and N-terminal amino acid sequence of sheep neutrophil cathepsin G and elastase
Arch. Biochem. Biophys.
368
7-13
1999
Ovis aries
brenda
Cavarra, E.; Santucci, A.; Lungarella, G.
Purification and N-terminal amino-acid sequence analysis of rabbit neutrophil cathepsin G
Biol. Chem. Hoppe-Seyler
376
371-377
1995
Oryctolagus cuniculus
brenda
Bjoerk, P.; Ohlsson, K.
Release of dog polymorphonuclear leukocyte cathepsin G, normally and in endotoxin and pancreatitic shock. Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin G
Biol. Chem. Hoppe-Seyler
372
419-426
1991
Canis lupus familiaris
brenda
Bjoerk, P.; Ohlsson, K.
Purification and N-terminal amino-acid sequence analysis of rat polymorphonuclear leukocyte cathepsin G
Biol. Chem. Hoppe-Seyler
371
595-601
1990
Rattus norvegicus
brenda
Maison, C.M.; Villiers, C.L.; Colomb, M.G.
Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G
J. Immunol.
147
921-926
1991
Homo sapiens
brenda
Gutschow, M.; Kuerschner, L.; Pietsch, M.; Ambrozak, A.; Neumann, U.; Gunther, R.; Hofmann, H.J.
Inhibition of cathepsin G by 2-amino-3,1-benzoxazin-4-ones: kinetic investigations and docking studies
Arch. Biochem. Biophys.
402
180-191
2002
Homo sapiens
brenda
Tani, K.; Murphy, W.J.; Chertov, O.; Oppenheim, J.J.; Wang, J.M.
The neutrophil granule protein cathepsin G activates murine T lymphocytes and upregulates antigen-specific IG production in mice
Biochem. Biophys. Res. Commun.
282
971-976
2001
Homo sapiens
brenda
Berlov, M.N.; Lodygin, P.A.; Andreeva, Y.V.; Kokryakov, V.N.
Isolation and some physical and chemical properties of elastase and cathepsin G from dog neutrophils
Biochemistry (Moscow)
66
1008-1013
2001
Canis lupus familiaris
brenda
Vagnoni, L.M.; Gronostaj, M.; Kerrigan, J.E.
6-Acylamino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-diones mechanism-based inhibitors of human leukocyte elastase and cathepsin G: effect of chirality in the 6-acylamino substituent on inhibitory potency and selectivity
Bioorg. Med. Chem.
9
637-645
2001
Homo sapiens
brenda
Robledo, O.; Papaioannou, A.; Ochietti, B.; Beauchemin, C.; Legault, D.; Cantin, A.; King, P.D.; Daniel, C.; Alakhov, V.Y.; Potworowski, E.F.; St-Pierre, Y.
ICAM-1 isoforms: specific activity and sensitivity to cleavage by leukocyte elastase and cathepsin G
Eur. J. Immunol.
33
1351-1360
2003
Homo sapiens
brenda
Ledoux, D.; Merciris, D.; Barritault, D.; Caruelle, J.P.
Heparin-like dextran derivatives as well as glycosaminoglycans inhibit the enzymatic activity of human cathepsin G
FEBS Lett.
537
23-29
2003
Homo sapiens
brenda
Selim, T.E.; Ghoneim, H.R.; Abdel Ghaffar, H.A.; Colman, R.W.; Dela Cadena, R.A.
High molecular mass kininogen inhibits cathepsin G-induced platelet activation by forming a complex with cathepsin G
Hematol. J.
2
371-377
2001
Homo sapiens
brenda
Greco, M.N.; Hawkins, M.J.; Powell, E.T.; Almond, H.R., Jr.; Corcoran, T.W.; de Garavilla, L.; Kauffman, J.A.; Recacha, R.; Chattopadhyay, D.; Andrade-Gordon, P.; Maryanoff, B.E.
Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design
J. Am. Chem. Soc.
124
3810-3811
2002
Homo sapiens
brenda
Sambrano, G.R.; Huang, W.; Faruqi, T.; Mahrus, S.; Craik, C.; Coughlin, S.R.
Cathepsin G activates protease-activated receptor-4 in human platelets
J. Biol. Chem.
275
6819-6823
2000
Homo sapiens
brenda
Goel, M.S.; Diamond, S.L.
Neutrophil cathepsin G promotes prothrombinase and fibrin formation under flow conditions by activating fibrinogen-adherent platelets
J. Biol. Chem.
278
9458-9463
2003
Homo sapiens
brenda
Moriuchi, H.; Moriuchi, M.; Fauci, A.S.
Cathepsin G, a neutrophil-derived serine protease, increases susceptibility of macrophages to acute human immunodeficiency virus type 1 infection
J. Virol.
74
6849-6855
2000
Homo sapiens
brenda
Biggs, J.R.; Yang, J.; Gullberg, U.; Muchardt, C.; Yaniv, M.; Kraft, A.S.
The human brm protein is cleaved during apoptosis: the role of cathepsin G
Proc. Natl. Acad. Sci. USA
98
3814-3819
2001
Homo sapiens
brenda
Bonnefoy, A.; Legrand, C.
Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase
Thromb. Res.
98
323-332
2000
Homo sapiens
brenda
Sissi, C.; Lucatello, L.; Naggi, A.; Torri, G.; Palumbo, M.
Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G
Biochem. Pharmacol.
71
287-293
2006
Homo sapiens
brenda
Mezyk-Kope?, R.; Bzowska, M.; Bzowska, M.; Mickowska, B.; Mak, P.; Potempa, J.; Bereta, J.
Effects of elastase and cathepsin G on the levels of membrane and soluble TNFalpha
Biol. Chem.
386
801-811
2005
Homo sapiens
brenda
Yui, S.; Tomita, K.; Kudo, T.; Ando, S.; Yamazaki, M.
Induction of multicellular 3-D spheroids of MCF-7 breast carcinoma cells by neutrophil-derived cathepsin G and elastase
Cancer Sci.
96
560-570
2005
Homo sapiens
brenda
Helske, S.; Syvaeranta, S.; Kupari, M.; Lappalainen, J.; Laine, M.; Lommi, J.; Turto, H.; Maeyraenpaeae, M.; Werkkala, K.; Kovanen, P.T.; Lindstedt, K.A.
Possible role for mast cell-derived cathepsin G in the adverse remodelling of stenotic aortic valves
Eur. Heart J.
27
1495-1504
2006
Homo sapiens
brenda
Tralau, T.; Meyer-Hoffert, U.; Schroeder, J.M.; Wiedow, O.
Human leukocyte elastase and cathepsin G are specific inhibitors of C5a-dependent neutrophil enzyme release and chemotaxis
Exp. Dermatol.
13
316-325
2004
Homo sapiens
brenda
Raptis, S.Z.; Shapiro, S.D.; Simmons, P.M.; Cheng, A.M.; Pham, C.T.
Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
Immunity
22
679-691
2005
Homo sapiens
brenda
Rivera-Marrero, C.A.; Stewart, J.; Shafer, W.M.; Roman, J.
The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli
Infect. Immun.
72
5712-5721
2004
Homo sapiens
brenda
Stefansson, S.; Yepes, M.; Gorlatova, N.; Day, D.E.; Moore, E.G.; Zabaleta, A.; McMahon, G.A.; Lawrence, D.A.
Mutants of plasminogen activator inhibitor-1 designed to inhibit neutrophil elastase and cathepsin G are more effective in vivo than their endogenous inhibitors
J. Biol. Chem.
279
29981-29987
2004
Homo sapiens
brenda
de Garavilla, L.; Greco, M.N.; Sukumar, N.; Chen, Z.W.; Pineda, A.O.; Mathews, F.S.; Di Cera, E.; Giardino, E.C.; Wells, G.I.; Haertlein, B.J.; Kauffman, J.A.; Corcoran, T.W.; Derian, C.K.; Eckardt, A.J.; Damiano, B.P.; Andrade-Gordon, P.; Maryanoff, B.E.
A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo
J. Biol. Chem.
280
18001-18007
2005
Homo sapiens (P08311), Homo sapiens
brenda
Shao, B.; Belaaouaj, A.; Verlinde, C.L.; Fu, X.; Heinecke, J.W.
Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase
J. Biol. Chem.
280
29311-29321
2005
Homo sapiens
brenda
Legedz, L7.; Randon, J.; Sessa, C.; Baguet, J.P.; Feugier, P.; Cerutti, C.; McGregor, J.; Bricca, G.
Cathepsin G is associated with atheroma formation in human carotid artery
J. Hypertens.
22
157-166
2004
Homo sapiens
brenda
Burster, T.; Beck, A.; Tolosa, E.; Marin-Esteban, V.; Roetzschke, O.; Falk, K.; Lautwein, A.; Reich, M.; Brandenburg, J.; Schwarz, G.; Wiendl, H.; Melms, A.; Lehmann, R.; Stevanovic, S.; Kalbacher, H.; Driessen, C.
Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes
J. Immunol.
172
5495-5503
2004
Homo sapiens
brenda
Sun, R.; Iribarren, P.; Zhang, N.; Zhou, Y.; Gong, W.; Cho, E.H.; Lockett, S.; Chertov, O.; Bednar, F.; Rogers, T.J.; Oppenheim, J.J.; Wang, J.M.
Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor
J. Immunol.
173
428-436
2004
Homo sapiens
brenda
Shimoda, N.; Fukazawa, N.; Nonomura, K.; Fairchild, R.L.
Cathepsin G is required for sustained inflammation and tissue injury after reperfusion of ischemic kidneys
Am. J. Pathol.
170
930-940
2007
Mus musculus
brenda
Lesner, A.; Wysocka, M.; Guzow, K.; Wiczk, W.; Legowska, A.; Rolka, K.
Development of sensitive cathepsin G fluorogenic substrate using combinatorial chemistry methods
Anal. Biochem.
375
306-312
2008
Homo sapiens
brenda
Korkmaz, B.; Moreau, T.; Gauthier, F.
Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions
Biochimie
90
227-242
2008
Homo sapiens (P08311), Homo sapiens
brenda
Rafiq, K.; Hanscom, M.; Valerie, K.; Steinberg, S.F.; Sabri, A.
Novel mode for neutrophil protease cathepsin G-mediated signaling: membrane shedding of epidermal growth factor is required for cardiomyocyte anoikis
Circ. Res.
102
32-41
2008
Rattus norvegicus
brenda
Burster, T.; Beck, A.; Poeschel, S.; Oren, A.; Baechle, D.; Reich, M.; Roetzschke, O.; Falk, K.; Boehm, B.O.; Youssef, S.; Kalbacher, H.; Overkleeft, H.; Tolosa, E.; Driessen, C.
Interferon-gamma regulates cathepsin G activity in microglia-derived lysosomes and controls the proteolytic processing of myelin basic protein in vitro
Immunology
121
82-93
2007
Homo sapiens, Mus musculus
brenda
Campbell, E.J.; Owen, C.A.
The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
J. Biol. Chem.
282
14645-14654
2007
Homo sapiens
brenda
Rykl, J.; Thiemann, J.; Kurzawski, S.; Pohl, T.; Gobom, J.; Zidek, W.; Schlueter, H.
Renal cathepsin G and angiotensin II generation
J. Hypertens.
24
1797-1807
2006
Homo sapiens (P08311), Sus scrofa (Q95284), Sus scrofa
brenda
Lim, J.K.; Lu, W.; Hartley, O.; DeVico, A.L.
N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
J. Leukoc. Biol.
80
1395-1404
2006
Homo sapiens
brenda
Wysocka, M.; Legowska, A.; Bulak, E.; Jaskiewicz, A.; Miecznikowska, H.; Lesner, A.; Rolka, K.
New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P1 selected by combinatorial chemistry methods
Mol. Divers.
11
93-99
2007
Homo sapiens
brenda
Sedor, J.; Hogue, L.; Akers, K.; Boslaugh, S.; Schreiber, J.; Ferkol, T.
Cathepsin-G interferes with clearance of Pseudomonas aeruginosa from mouse lungs
Pediatr. Res.
61
26-31
2006
Mus musculus
brenda
Miyata, J.; Tani, K.; Sato, K.; Otsuka, S.; Urata, T.; Lkhagvaa, B.; Furukawa, C.; Sano, N.; Sone, S.
Cathepsin G: the significance in rheumatoid arthritis as a monocyte chemoattractant
Rheumatol. Int.
27
375-382
2007
Homo sapiens
brenda
Gale, A.J.; Rozenshteyn, D.
Cathepsin G, a leukocyte protease, activates coagulation factor VIII
Thromb. Haemost.
99
44-51
2008
Homo sapiens
brenda
Peterszegi, G.; Texier, S.; Robert, A.M.; Moulias, R.; Robert, L.
Increased elastase and cathepsin G activity in activated lymphocytes from aged patients Role of denutrition and dementia
Arch. Gerontol. Geriatr.
25
285-298
2008
Homo sapiens
brenda
Sienczyk, M.; Lesner, A.; Wysocka, M.; Legowska, A.; Pietrusewicz, E.; Rolka, K.; Oleksyszyn, J.
New potent cathepsin G phosphonate inhibitors
Bioorg. Med. Chem.
16
8863-8867
2008
Homo sapiens
brenda
Wilson, T.J.; Nannuru, K.C.; Futakuchi, M.; Sadanandam, A.; Singh, R.K.
Cathepsin G enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-kappaB ligand
Cancer Res.
68
5803-5811
2008
Mus musculus, Mus musculus BALB/c
brenda
Wilson, T.J.; Nannuru, K.C.; Singh, R.K.
Cathepsin G recruits osteoclast precursors via proteolytic activation of protease-activated receptor-1
Cancer Res.
69
3188-3195
2009
Homo sapiens, Mus musculus
brenda
Stoeckle, C.; Sommandas, V.; Adamopoulou, E.; Belisle, K.; Schiekofer, S.; Melms, A.; Weber, E.; Driessen, C.; Boehm, B.O.; Tolosa, E.; Burster, T.
Cathepsin G is differentially expressed in primary human antigen-presenting cells
Cell. Immunol.
255
41-45
2009
Homo sapiens
brenda
Mambole, A.; Baruch, D.; Nusbaum, P.; Bigot, S.; Suzuki, M.; Lesavre, P.; Fukuda, M.; Halbwachs-Mecarelli, L.
The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase
J. Biol. Chem.
283
23627-23635
2008
Homo sapiens (P08311)
brenda
Korkmaz, B.; Attucci, S.; Juliano, M.A.; Kalupov, T.; Jourdan, M.L.; Juliano, L.; Gauthier, F.
Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates
Nat. Protoc.
3
991-1000
2008
Homo sapiens
brenda
Dabek, M.; Ferrier, L.; Roka, R.; Gecse, K.; Annahazi, A.; Moreau, J.; Escourrou, J.; Cartier, C.; Chaumaz, G.; Leveque, M.; Ait-Belgnaoui, A.; Wittmann, T.; Theodorou, V.; Bueno, L.
Luminal cathepsin g and protease-activated receptor 4: a duet involved in alterations of the colonic epithelial barrier in ulcerative colitis
Am. J. Pathol.
175
207-214
2009
Homo sapiens
brenda
Wilson, T.J.; Nannuru, K.C.; Futakuchi, M.; Singh, R.K.
Cathepsin G-mediated enhanced TGF-beta signaling promotes angiogenesis via upregulation of VEGF and MCP-1
Cancer Lett.
288
162-169
2010
Mus musculus
brenda
Farberman, M.M.; Akers, K.T.; Malone, J.P.; Erdman-Gilmore, P.; Townsend, R.R.; Ferkol, T.
Airway proteins involved in bacterial clearance susceptible to cathepsin G proteolysis
Eur. Respir. J.
35
410-417
2010
Mus musculus
brenda
Burster, T.; Macmillan, H.; Hou, T.; Schilling, J.; Truong, P.; Boehm, B.O.; Zou, F.; Lau, K.; Strohman, M.; Schaffert, S.; Busch, R.; Mellins, E.D.
Masking of a cathepsin G cleavage site in vivo contributes to the proteolytic resistance of major histocompatibility complex class II molecules
Immunology
130
436-46
2010
Homo sapiens
brenda
Tausch, L.; Henkel, A.; Siemoneit, U.; Poeckel, D.; Kather, N.; Franke, L.; Hofmann, B.; Schneider, G.; Angioni, C.; Geisslinger, G.; Skarke, C.; Holtmeier, W.; Beckhaus, T.; Karas, M.; Jauch, J.; Werz, O.
Identification of human cathepsin G as a functional target of boswellic acids from the anti-inflammatory remedy frankincense
J. Immunol.
183
3433-3442
2009
Homo sapiens (P08311), Homo sapiens
brenda
Kudo, T.; Kigoshi, H.; Hagiwara, T.; Takino, T.; Yamazaki, M.; Yui, S.
Cathepsin G, a neutrophil protease, induces compact cell-cell adhesion in MCF-7 human breast cancer cells
Mediators Inflamm.
2009
850940
2009
Homo sapiens
brenda
Wilson, T.J.; Nannuru, K.C.; Singh, R.K.
Cathepsin G-mediated activation of pro-matrix metalloproteinase 9 at the tumor-bone interface promotes transforming growth factor-beta signaling and bone destruction
Mol. Cancer Res.
7
1224-1233
2009
Mus musculus
brenda
Reich, M.; Lesner, A.; Legowska, A.; Sienczyk, M.; Oleksyszyn, J.; Boehm, B.O.; Burster, T.
Application of specific cell permeable cathepsin G inhibitors resulted in reduced antigen processing in primary dendritic cells
Mol. Immunol.
46
2994-2999
2009
Homo sapiens
brenda
Burster, T.; Macmillan, H.; Hou, T.; Boehm, B.O.; Mellins, E.D.
Cathepsin G: roles in antigen presentation and beyond
Mol. Immunol.
47
658-665
2010
Homo sapiens, Mus musculus
brenda
Palesch, D.; Sienczyk, M.; Oleksyszyn, J.; Reich, M.; Wieczerzak, E.; Boehm, B.O.; Burster, T.
Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?
Acta Biochim. Pol.
58
39-44
2011
Bos taurus
brenda
Korkmaz, B.; Jegot, G.; Lau, L.C.; Thorpe, M.; Pitois, E.; Juliano, L.; Walls, A.F.; Hellman, L.; Gauthier, F.
Discriminating between the activities of human cathepsin G and chymase using fluorogenic substrates
FEBS J.
278
2635-2646
2011
Homo sapiens (P08311), Homo sapiens
brenda
Raymond, W.W.; Trivedi, N.N.; Makarova, A.; Ray, M.; Craik, C.S.; Caughey, G.H.
How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution
J. Immunol.
185
5360-5368
2010
Homo sapiens, Mus musculus
brenda
Siao, S.C.; Li, K.J.; Hsieh, S.C.; Wu, C.H.; Lu, M.C.; Tsai, C.Y.; Yu, C.L.
Tamm-Horsfall glycoprotein enhances PMN phagocytosis by binding to cell surface-expressed lactoferrin and cathepsin G that activates MAP kinase pathway
Molecules
16
2119-2134
2011
Homo sapiens
brenda
Zou, F.; Schaefer, N.; Palesch, D.; Bruecken, R.; Beck, A.; Sienczyk, M.; Kalbacher, H.; Sun, Z.; Boehm, B.O.; Burster, T.
Regulation of cathepsin G reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients
PLoS ONE
6
e22815
2011
Homo sapiens
brenda
Perrin, J.; Lecompte, T.; Tournier, A.; Morlon, L.; Marchand-Arvier, M.; Vigneron, C.
In vitro effects of human neutrophil cathepsin G on thrombin generation: Both acceleration and decreased potential
Thromb. Haemost.
104
514-522
2010
Homo sapiens
brenda
Wang, J.; Sjoeberg, S.; Tang, T.T.; Ooerni, K.; Wu, W.; Liu, C.; Secco, B.; Tia, V.; Sukhova, G.K.; Fernandes, C.; Lesner, A.; Kovanen, P.T.; Libby, P.; Cheng, X.; Shi, G.P.
Cathepsin G activity lowers plasma LDL and reduces atherosclerosis
Biochim. Biophys. Acta
1842
2174-2183
2014
Homo sapiens (P08311), Homo sapiens, Mus musculus (P28293)
brenda
Cohen-Mazor, M.; Mazor, R.; Kristal, B.; Sela, S.
Elastase and cathepsin G from primed leukocytes cleave vascular endothelial cadherin in hemodialysis patients
BioMed Res. Int.
2014
459640
2014
Homo sapiens (P08311), Homo sapiens
brenda
Woloszynek, J.C.; Hu, Y.; Pham, C.T.
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions
J. Biol. Chem.
287
34101-34109
2012
Homo sapiens (P08311)
brenda
Faraday, N.; Schunke, K.; Saleem, S.; Fu, J.; Wang, B.; Zhang, J.; Morrell, C.; Dore, S.
Cathepsin G-dependent modulation of platelet thrombus formation in vivo by blood neutrophils
PLoS ONE
8
e71447
2013
Homo sapiens (P08311), Homo sapiens, Mus musculus (P28293), Mus musculus
brenda
Gudmann, N.S.; Manon-Jensen, T.; Sand, J.M.B.; Diefenbach, C.; Sun, S.; Danielsen, A.; Karsdal, M.A.; Leeming, D.J.
Lung tissue destruction by proteinase 3 and cathepsin G mediated elastin degradation is elevated in chronic obstructive pulmonary disease
Biochem. Biophys. Res. Commun.
503
1284-1290
2018
Homo sapiens
brenda
Groborz, K.; Kolt, S.; Kasperkiewicz, P.; Drag, M.
Internally quenched fluorogenic substrates with unnatural amino acids for cathepsin G investigation
Biochimie
166
103-111
2019
Homo sapiens
brenda
Gao, S.; Zhu, H.; Yang, H.; Zhang, H.; Li, Q.; Luo, H.
The role and mechanism of cathepsin G in dermatomyositis
Biomed. Pharmacother.
94
697-704
2017
Homo sapiens
brenda
Guo, J.; Tu, J.; Hu, Y.; Song, G.; Yin, Z.
Cathepsin G cleaves and activates IL-36gamma and promotes the inflammation of psoriasis
Drug Des. Devel. Ther.
13
581-588
2019
Homo sapiens
brenda
Penczek, A.; Sienczyk, M.; Wirtz, C.R.; Burster, T.
Cell surface cathepsin G activity differs between human natural killer cell subsets
Immunol. Lett.
179
80-84
2016
Homo sapiens
brenda
Fu, Z.; Thorpe, M.; Alemayehu, R.; Roy, A.; Kervinen, J.; de Garavilla, L.; Abrink, M.; Hellman, L.
Highly selective cleavage of cytokines and chemokines by the human mast cell chymase and neutrophil cathepsin G
J. Immunol.
198
1474-1483
2017
Homo sapiens
brenda
Eipper, S.; Steiner, R.; Lesner, A.; Sienczyk, M.; Palesch, D.; Halatsch, M.E.; Zaczynska, E.; Heim, C.; Hartmann, M.D.; Zimecki, M.; Wirtz, C.R.; Burster, T.
Lactoferrin is an allosteric enhancer of the proteolytic activity of cathepsin G
PLoS ONE
11
e0151509
2016
Homo sapiens
brenda
Thorpe, M.; Fu, Z.; Chahal, G.; Akula, S.; Kervinen, J.; de Garavilla, L.; Hellman, L.
Extended cleavage specificity of human neutrophil cathepsin G A low activity protease with dual chymase and tryptase-type specificities
PLoS ONE
13
e0195077
2018
Homo sapiens
brenda