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((Gly-Pro-4-hydroxyproline)5-Gly-Pro-Lys(7-methoxycoumarin-4-yl) acetyl)-Gly-Pro-Gln-Gly-Cys(4-methoxybenzyl)-Arg-Gly-Gln-Lys(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-4-hydroxyproline)5-NH2 + H2O
?
triple-helical substrate fTHP-9
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-L-Lys-Pro-Leu-Gly-Leu-Lys(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Ala-Cys(p-OmeBz)-Trp-Ala-Arg(Dpa)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly + Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-GTQGQEARGS-dinitrophenol NH2 + H2O
?
substrate covering the aggrecanase cleavage site of aggrecan
-
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-(3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-LAQAVRSSK-dinitrophenol NH2 + H2O
?
quenched fluorescent substrate mimicking the cleavage site of pro tumor necrosis factor alpha
-
-
?
(7-methoxycoumarin-4-yl)acetyl-P-3-cyclohexylalanyl-norvalyl-HA-dinitrophenol NH2 + H2O
?
collagenase substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-norvaline-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
degradation of synthetic substrate is pH-independent
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Cys(p-OMeBz)-Trp-Ala-Arg(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Gln-Ala-Val-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Arg-Ser-Ser-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Nva-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Leu-Ala-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2 + H2O
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly + Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
triple-helical substrate fTHP-9
-
-
?
alpha subunit of low density lipoprotein receptor-related protein + H2O
?
-
-
-
-
?
alpha-1 microglobulin + H2O
?
-
-
-
-
?
alpha-2 macroglobulin + H2O
?
-
-
-
-
?
alpha-2-HS-glycoprotein + H2O
?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
alpha1-proteinase inhibitor + H2O
?
-
-
-
-
?
alpha2-macroglobulin + H2O
?
-
-
-
-
?
alpha5 integrin + H2O
?
-
-
-
-
?
apolipoprotein A-I + H2O
?
-
-
-
-
?
apolipoprotein A-IV + H2O
?
-
-
-
-
?
apolipoprotein J + H2O
?
-
-
-
-
?
betaglycan + H2O
?
-
-
-
-
?
brain-specific angiogenesis inhibitor 1 + H2O
vasculostatin-120 + vasculostatin-40
-
the N terminus of BAI1 is cleaved extracellularly to generate a truncated receptor (vasculostatin-120) and a 40000 Da fragment (vasculostatin-40)
-
-
?
CCN3 + H2O
CPPQCPGR + DGQIGCVPR + KVEVPGECCEK + KPVMVIGTCTCHTNCPK + ?
-
-
-
?
collagen I alpha-1 chain + H2O
?
-
overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain
-
-
?
collagen I alpha-2 chain + H2O
?
-
overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain
-
-
?
collagen type I alpha-1 chain + H2O
?
-
the MMP-14 ectodomain preferentially cleaves the alpha-1 chain of collagen type I
-
-
?
collagen type I alpha-2 chain + H2O
?
-
-
-
-
?
complement component 3 + H2O
?
-
-
-
-
?
cross-linked fibrin II + H2O
?
des-fibrinopeptides A and B, prepared by clotting fibrinogen with thrombin in the presence of factor XIIIa
-
-
?
dabcyl-Gly-Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln-Lys(fluorescein)-Ahx-Cys + H2O
?
-
-
-
?
dermatan sulfate proteoglycan + H2O
?
-
-
-
?
endoglin + H2O
soluble endoglin + ?
-
MMP-14 cleaves membrane-bound endoglin at a site in close proximity to the transmembrane domain between Gly586-Leu-587
-
-
?
entactin + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
-
the enzyme plays a role in transactivation
-
-
?
extracellular matrix metalloproteinase inducer + H2O
?
-
-
-
-
?
extracellular matrix metalloproteinase inducer + H2O
extracellular matrix metalloproteinase inducer fragment + ?
-
-
22000 Da in length
-
?
F-gelatin + H2O
?
-
-
-
?
fibrillin + H2O
?
-
-
-
-
?
fibroblast growth factor receptor-1 + H2O
?
-
-
-
?
fibroblast growth factor receptor-4 + H2O
?
-
-
-
?
galectin-3
?
-
cleaved to the 22 kDa degradation product when exposed to cells expressing membrane-anhored wild type MT1-MMP or the recombinant 50 kDa enzyme form
-
-
?
gelsolin + H2O
?
-
-
-
-
?
growth differentiation factor-1 + H2O
?
-
-
-
?
heparin-binding epidermal growth factor + H2O
?
heparin-binding epidermal growth factor + H2O
heparin-binding epidermal growth factor mN3-fragment + ?
-
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
inactive pro-matrix metalloproteinase-2 + H2O
active matrix metalloproteinase-2 + ?
-
-
-
-
?
inter-alpha inhibitor H4 + H2O
?
-
-
-
-
?
intercellular cell adhesion molecule-1 + H2O
?
-
-
-
-
?
kidney injury molecule-1 + H2O
?
the enzyme cleaves and sheds the substrate's ectodomain
-
-
?
KiSS-1/metastin + H2O
?
-
-
-
-
?
laminin-5 + H2O
?
-
-
-
?
laminin-5 beta3 chain + H2O
?
-
-
-
-
?
mannose-binding lectin + H2O
?
-
-
-
-
?
MCP-3/CCL7 + H2O
?
-
-
-
-
?
membrane-bound Semaphorin 4D + H2O
soluble Semaphorin 4D + ?
-
-
-
-
?
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 + H2O
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly + Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
-
-
-
?
MOCAcPLGLA2pr-dinitrophenol-A-RNH2 + H2O
?
fluorogenic substrate
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
N-hexanoyl((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGLRGQK(2,4-dinitrophenyl)GVR(GP-4-hydroxy-L-proline)5-NH2 + H2O
N-hexanoyl((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGL + RGQK(2,4-dinitrophenyl)GVR(GP-4-hydroxy-L-proline)5-NH2
-
-
-
-
?
neuronal glial antigen 2 + H2O
?
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
PA83
?
-
efficiently cleaved by MT1-MMP at the substrate-enzyme ratio as low as 1: 50
-
-
?
peptide IAG + H2O
?
enzyme binding structure, modelling, overview
-
-
?
pericentrin + H2O
?
-
-
-
-
?
pro-alpha v integrin + H2O
?
-
-
-
?
pro-alpha5 integrin subunit + H2O
?
-
-
-
-
?
pro-alpha5beta3 integrin subunit + H2O
?
-
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
?
-
activation
-
-
?
pro-matrix metalloproteinase-8 + H2O
?
-
activation
-
-
?
pro-MMP-2
?
-
MT1-MMP accomplishes full pro-MMP-2 activation, cleavage within the prodomain at the Asn37-Leu38 peptide bond
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
pro-MMP-2 + H2O
MMP-2 + ?
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
pro-MMP-2 + H2O
MMP-2 + propeptide
-
-
-
?
pro-MMP2 + H2O
MMP-2 + ?
-
activation in the presence of TIMP-2
-
-
?
pro-tissue necrosis factor alpha + H2O
?
-
-
-
-
?
pro-transforming growth factor beta + H2O
?
-
-
-
-
?
progelatinase A + H2O
gelatinase A + ?
-
activation, gelatinase A is matrix metalloproteinase-2
-
-
?
progelatinase A E375A + H2O
?
syn: pro-matrix metalloproteinase 2, cleaves at N37-L38 only
-
-
?
proMMP-13 + H2O
?
-
activation
-
-
?
proMMP-2 + H2O
MMP-2 + ?
-
activation
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
proMMP-2 + H2O
MMP-2 + pro-peptide
proMMP-8 + H2O
?
-
activation
-
-
?
rat-tail tendon type I collagen + H2O
?
-
degraded by deltaTM-MT1-MMP at 37°C
-
-
?
receptor of complement component 1q + H2O
?
cleaves at Gly79-Gln80, cleavage with CAT/PEX domain leads to fragments with the following MW: 17 kDa, 12 kDa and 11 kDa
-
-
?
receptor-activator of NF-kB ligand + H2O
?
-
-
-
-
?
recombinant mutated aggrecan fusion protein 1 + H2O
?
-
-
-
?
SDF-1/CXCL12 + H2O
?
-
-
-
-
?
stromal cell-derived factor 1 + H2O
?
-
-
-
?
syndecan + H2O
?
-
-
-
-
?
syndecan-1 core protein + H2O
?
syndecan-1 G245L glutathione transferase protein + H2O
?
cleaves at G82-L83 peptide bond
-
-
?
testican-1 + H2O
?
-
-
-
-
?
tissue transglutaminase + H2O
?
-
-
-
-
?
transforming growth factor-beta + H2O
?
-
-
-
?
type 1 collagen + H2O
?
-
-
-
-
?
type I collagen + H2O
denatured type I collagen
-
bound by recombinant linker/hemopexin C domain of MT1-MMP
-
-
?
type I collagen chain alpha-1 + H2O
?
-
-
-
-
?
type I collagen chain alpha-2 + H2O
?
-
-
-
-
?
type III collagen + H2O
?
type-I collagen + H2O
?
-
-
-
-
?
additional information
?
-
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
fluorescent peptide
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
fluorescent peptide
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
cdMT1-MMP is catalytically more efficient towards small peptide substrates than deltaTM-MT1-MMP and the haemopexin domain of MT1-MMP facilitates the hydrolysis of triple-helical substrates
-
-
?
aggrecan + H2O
?
-
-
-
-
?
aggrecan + H2O
?
recombinant fusion protein with G332A mutation, substrate is cleaved at the aggrecanase site in its interglobular domain sequence segment, products are fragments with the following MW: 72 kDa, 66 kDA and 42 kDa
-
-
?
alpha1-antitrypsin + H2O
?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
-
-
-
?
apolipoprotein E + H2O
?
-
-
-
-
?
apolipoprotein E + H2O
?
-
the 34 kDa apoE protein is initially processed by MMP-14 into fragments with molecular masses of 28, 23, 21, and 11 kDa. The primary MMP-14 cleavage sites are Ala176-Ile177, Pro183-Leu184, Pro202-Leu203, and Gln249-Ile250. The MMP-14-mediated cleavage of apoE is consistent regardless of whether apoE exists in its lipid-bound or lipid-free form. Upon digestion with MMP-14, apoE loses its ability to suppress the platelet-derived growth factor-induced migration of rat vascular smooth muscle cells
-
-
?
CCN5 + H2O
?
-
-
-
?
CCN5 + H2O
?
UniProt ID O76076, CCN5 lacks the CTCK domain
-
-
?
CD44 + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
collagen I + H2O
?
-
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
collagen I + H2O
?
-
degradation, substrate from rat tail
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
-
MT1-MMP sheds E-cadherin at cell-cell adherens junctions
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
alpha, beta and gamma chains
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
cell surface active pMMP-2 cDNAs bound to MT1-MMP enhances substrate digestion, cytoplasmic tail of MT1-MMP not required for digestion
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
poor activity
-
-
?
Gelatin + H2O
?
-
rat-tail tendon type I collagen boiled for 5 min and denatured to gelatin, when degraded by deltaTM-MT1-MMP and cdMT1-MMP
-
-
?
Gelatin + H2O
?
-
-
-
-
?
heparin-binding epidermal growth factor + H2O
?
-
the enzyme removes the NH2-terminal 20 amino acids by cleaving between A-83LC
-
-
?
heparin-binding epidermal growth factor + H2O
?
-
the enzyme removes the NH2-terminal 20 amino acids by cleaving between A-83LC
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
the 66 kDa protein is cleaved to 58, 42, and 16 kDa fragments
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin-1 + H2O
?
-
-
-
-
?
Laminin-1 + H2O
?
-
-
-
?
pro-MMP-2 + H2O
?
-
-
-
?
pro-MMP-2 + H2O
?
-
MT-MMP1 activates MMP-2, EC 3.4.24.24
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
-
-
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
-
activation of MMP-2
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
MMP14 is essential for proMMP-2 activation: pro-MMP-2 activation by MMP14/TIMP complex is realized in an environment of low TIMP concentration
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
pro-MMP-2 is cleaved by an adjacent TIMP-2-free MT1-MMP between Asn37 and Leu38, generating an activated intermediate form that is further processed to the fully activated form by an intermolecular auto-cleavage when an intermediate form is present at a sufficiently high concentration at the cell surface, mechanism, overview. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP (TIMP)-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
pro-MMP-2 is cleaved by an adjacent TIMP-2-free MT1-MMP between Asn37 and Leu38, generating an activated intermediate form that is further processed to the fully activated form by an intermolecular auto-cleavage when an intermediate form is present at a sufficiently high concentration at the cell surface, mechanism, overview. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
progelatinase A + H2O
?
-
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
-
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
-
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
cleaves at N37-L38 and N80-Y81
-
-
?
progelatinase A + H2O
?
21 kDa fragment
-
-
?
progelatinase A + H2O
?
-
-
-
-
?
proMMP-2 + H2O
?
-
-
-
-
?
proMMP-2 + H2O
?
-
activation
-
-
?
proMMP-2 + H2O
?
-
activation
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
activation
-
-
?
proMMP-2 + H2O
MMP-2 + pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + pro-peptide
-
-
-
-
?
syndecan-1 + H2O
?
-
-
-
-
?
syndecan-1 + H2O
?
-
-
-
?
syndecan-1 core protein + H2O
?
-
-
-
-
?
syndecan-1 core protein + H2O
?
cleaves preferably at G245-L246 peptide bond
-
-
?
transglutaminase + H2O
?
-
-
-
-
?
transglutaminase + H2O
?
tissue transglutaminase that binds fibronectin
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment
-
-
?
Type I collagen + H2O
?
-
type I collagen binds MT1-MMP via a hemopexin-like domain and is cleaved
-
-
?
type II collagen + H2O
?
-
-
-
-
?
type II collagen + H2O
?
-
-
-
?
type III collagen + H2O
?
-
-
-
-
?
type III collagen + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
-
-
-
?
Vitronectin + H2O
?
-
-
-
?
additional information
?
-
degrades extracellular matrix compounds
-
-
?
additional information
?
-
-
membrane type 1 matrix metalloproteinase activates progelatinase A, a type IV collagenase, on the cell surface of tumors. Membrane type 1-matrix metalloproteinase may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
enzyme activates gelatinase
-
-
?
additional information
?
-
-
enzyme activates gelatinase
-
-
?
additional information
?
-
role in extracellular matrix remodelling under physiological and pathological conditions
-
-
?
additional information
?
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
remodeling of the extracellular matrix
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
-
central role in tumor cell invasion
-
-
?
additional information
?
-
key protease in tumor cell invasion
-
-
?
additional information
?
-
-
the enzyme regulates extracellular matrix remodeling and is capable of cleaving a wide variety of transmembrane proteins. The enzymatic activity of MT1-MMP is regulated by endogenous inhibitors, TIMP, the tissue inhibitor of metalloproteinases
-
-
?
additional information
?
-
-
hydrolysis of triple helical substrates that, via addition of N-terminal alkyl chains, differ in their thermal stabilities, substitution of Cys(4-methoxybenzyl) for Leu in the P1' subsite is greatly favored by MMP-14, increase in substrate triple-helical thermal stability leads to the decreased ability of the enzyme to cleave such substrates
-
-
?
additional information
?
-
-
rat-tail tendon type I collagen not degraded by cdMT1-MMP at 37°C
-
-
?
additional information
?
-
-
MT1-MMP plays an important role in early cancer dissemination by converting epithelial cells to migratory mesenchymal-like cells
-
-
?
additional information
?
-
-
pro-alpha2 integrin subunit is not a substrate
-
-
?
additional information
?
-
-
enzyme regulation, transcription factor EGR1 is involved, overview
-
-
?
additional information
?
-
the enzyme performs autoproteolysis
-
-
?
additional information
?
-
-
membrane-type MMPs are membrane spanning binding sites that play an important role in the cell surface activation of MMPs such as MMP-2
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
overview of MT1-MMP-associating proteins by localization and MT1-MMP-associating membrane proteins by function. Some proteins, such as MT1-SP, EGFR, 5T4, DCP, and CD36L1, preferentially precipitate pro-MT1-MMP, other proteins, e.g. GA733-1, HAI-1, HAI-2, TF, THBD, and CD9, precipitate preferentially the active form of MT1-MMP indicating that these proteins may form a complex on the cell surface
-
-
?
additional information
?
-
-
membrane proteins were cleaved by MT1-MMP in a MMI270-sensitive manner
-
-
?
additional information
?
-
the enzyme does not degrade fibroblast growth factor-2 or fibroblast growth factor receptor-2
-
-
?
additional information
?
-
interaction analysis of MMP14 with proteins in HeLa cells identified by inactive catalytic domain capture yeast 2-hybrid analysis, overview. Detection of CCN5 as a MMP14 substrate by yeast 2-hybrid screening
-
-
?
additional information
?
-
CCN = cysteine rich protein 61/connective tissue growth factor/nephroblastoma overexpressed
-
-
?
additional information
?
-
modeling of enzyme-substrate interaction
-
-
?
additional information
?
-
-
modeling of enzyme-substrate interaction
-
-
?
additional information
?
-
-
healing process
-
-
?
additional information
?
-
-
in vivo growth of FaDu cells co-injected with murine fibroblasts is increased, while their progression is reduced in MT1-MMP-deficient fibroblasts, overview
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
MT1-MMP activates MMP-2
-
-
?
additional information
?
-
-
MT1-MMP is increased in myocardial ischemia and reperfusion, and contributes to myocardial dysfunction, upstream induction mechanism by release of endothelin and protein kinase C activation, microdialysis analysis, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CCN5 + H2O
?
UniProt ID O76076, CCN5 lacks the CTCK domain
-
-
?
fibroblast growth factor receptor-1 + H2O
?
-
-
-
?
fibroblast growth factor receptor-4 + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
growth differentiation factor-1 + H2O
?
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
kidney injury molecule-1 + H2O
?
the enzyme cleaves and sheds the substrate's ectodomain
-
-
?
Laminin-1 + H2O
?
-
-
-
?
laminin-5 + H2O
?
-
-
-
?
neuronal glial antigen 2 + H2O
?
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
pro-MMP-2 + H2O
?
-
MT-MMP1 activates MMP-2, EC 3.4.24.24
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
-
activation of MMP-2
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
pro-MMP-2 + H2O
MMP-2 + propeptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
proMMP-2 + H2O
MMP-2 + pro-peptide
stromal cell-derived factor 1 + H2O
?
-
-
-
?
syndecan-1 + H2O
?
-
-
-
?
transforming growth factor-beta + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
-
-
?
additional information
?
-
Collagen + H2O
?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
collagen I + H2O
?
-
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
the 66 kDa protein is cleaved to 58, 42, and 16 kDa fragments
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
MMP14 is essential for proMMP-2 activation: pro-MMP-2 activation by MMP14/TIMP complex is realized in an environment of low TIMP concentration
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP (TIMP)-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
activation
-
-
?
proMMP-2 + H2O
MMP-2 + pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + pro-peptide
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment
-
-
?
additional information
?
-
-
membrane type 1 matrix metalloproteinase activates progelatinase A, a type IV collagenase, on the cell surface of tumors. Membrane type 1-matrix metalloproteinase may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
enzyme activates gelatinase
-
-
?
additional information
?
-
-
enzyme activates gelatinase
-
-
?
additional information
?
-
role in extracellular matrix remodelling under physiological and pathological conditions
-
-
?
additional information
?
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
remodeling of the extracellular matrix
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
-
central role in tumor cell invasion
-
-
?
additional information
?
-
key protease in tumor cell invasion
-
-
?
additional information
?
-
-
the enzyme regulates extracellular matrix remodeling and is capable of cleaving a wide variety of transmembrane proteins. The enzymatic activity of MT1-MMP is regulated by endogenous inhibitors, TIMP, the tissue inhibitor of metalloproteinases
-
-
?
additional information
?
-
-
enzyme regulation, transcription factor EGR1 is involved, overview
-
-
?
additional information
?
-
-
membrane-type MMPs are membrane spanning binding sites that play an important role in the cell surface activation of MMPs such as MMP-2
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
overview of MT1-MMP-associating proteins by localization and MT1-MMP-associating membrane proteins by function. Some proteins, such as MT1-SP, EGFR, 5T4, DCP, and CD36L1, preferentially precipitate pro-MT1-MMP, other proteins, e.g. GA733-1, HAI-1, HAI-2, TF, THBD, and CD9, precipitate preferentially the active form of MT1-MMP indicating that these proteins may form a complex on the cell surface
-
-
?
additional information
?
-
the enzyme does not degrade fibroblast growth factor-2 or fibroblast growth factor receptor-2
-
-
?
additional information
?
-
interaction analysis of MMP14 with proteins in HeLa cells identified by inactive catalytic domain capture yeast 2-hybrid analysis, overview. Detection of CCN5 as a MMP14 substrate by yeast 2-hybrid screening
-
-
?
additional information
?
-
-
healing process
-
-
?
additional information
?
-
-
in vivo growth of FaDu cells co-injected with murine fibroblasts is increased, while their progression is reduced in MT1-MMP-deficient fibroblasts, overview
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
MT1-MMP activates MMP-2
-
-
?
additional information
?
-
-
MT1-MMP is increased in myocardial ischemia and reperfusion, and contributes to myocardial dysfunction, upstream induction mechanism by release of endothelin and protein kinase C activation, microdialysis analysis, 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.
(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N-hydroxy-2-[[(4'-methoxybiphenyl-4-yl)sulfonyl](propan-2-yloxy)amino]butanamide
-
(2R)-4-(acetylamino)-2-[(biphenyl-4-ylsulfonyl)amino]-N-hydroxybutanamide
-
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
-
-
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
AB815
-
against hinge region of MT1-MMP
-
Acetohydroxamic acid
inhibition of Co2+-MT1-MMP
AG3340
-
inhibits MT1-MMP in a sub-nanomolar range
alpha1-PDX
-
completely abats MT1-MMP-induced gelatin degradation by A375 cells
-
alpha1-PIMT1
-
alpha1-proteinase inhibitor-based inhibitor by incorporating the MT1-MMP propeptide sequence into the alpha1-PI reactive-site loop, inhibits proMT1-MMP activation
-
alpha1-PIPDX
-
alpha1-proteinase inhibitor-based inhibitor with furin consensus cleavage sequence inserted into the reactive-site loop, inhibits proMT1-MMP activation
-
anti-membrane-type 1-MMP antibody
-
antibodies LEM-1 and LEM-2 inhibit endothelial cell invasion in a dose dependent manner
-
bone marrow stromal cell antigen 2
best-2, interaction with MT1-MMP via the cytoplasmic tails of both. Bst-2 inhibits the release of virus from infectious cells and this inhibition can be reversed by MT1-MMP. Bst-2 tetherin activity is blocked by MT1-MMP
-
CT1399
-
inhibits endothelial cell invasion
-
CT1847
-
inhibits endothelial cell invasion
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin inhibitor repressing activation of MMP-2
DX2400
human monoclonal antibody
-
EDTA
-
10 mM, non-specific inhibitor
epigallocatechin-3-gallate
-
-
genistein
-
markedly suppresses the VEGF mRNA induction in MT clones without affecting the VEGF expression in control clones
hemopexin
-
soluble hemopexin domain inhibits collagenolysis by preventing dimerization
-
herbimycin-A
-
strongly inhibits up-regulation effect of VEGF-A by MT1-MMP
MT1-MMP siRNA
-
collagen degrading activity is completely lost when MT1-MMP expressing cells are transfected with 100 nM MT1-MMP siRNA
-
N,N'-bis(4-[[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]amino]-4-oxobutyl)benzene-1,3-dicarboxamide
-
N,N'-bis[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]benzene-1,3-dicarboxamide
-
N,N'-bis[4-[(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)amino]-4-oxobutyl]benzene-1,3-dicarboxamide
-
N-(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)-N'-(2-[[4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]
modelling ofcompound 6 binding to dimeric MT1-MMP (catalytic domains)
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N4-hydroxyamino-2-isobutyl-3-(thienylthiomethyl) succinyl]-L-phenylalamine-methylamide
-
-
PD98059
-
inhibits MMP-2 processing in HT1080 cells
Rac1
-
inhibits both enzyme activity and dimerization
-
Rac1(N17Rac)
-
coexpression wit MT1-MMP cDNAs leads to complete inhibition of migration
-
RECK
membrane anchor type proteinase inhibitor
-
reversion-inducing cysteine rich protein
-
-
-
reversion-inducing-cysteine-rich protein
-
-
-
RO28-2653
-
reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
TAPI-1
-
inhibits the shedding of the MT1-MMP 18 kDa form
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-1 mutant forms
-
TIMP-1(T98L), TIMP-1(V4A), TIMP-1(P6V), TIMP-1(V4S), TIMP-1(P6S), TIMP-1(M66I), TIMP-1(P6A), TIMP-1(M66V), TIMP-1(M66A), TIMP-1(T2S), TIMP-1(M66L), TIMP-1(M66G), TIMP-1(V69L), TIMP-1(M66K), TIMP-1(V4A/P6V/T98L). TIMP-1 is inactive against MT1-MMP. TIMP-1 can be transformed into an active inhibitor against MT1-MMP by the mutation T98L. The resultant mutant displays inhibitory characteristics of a slow, tight binding inhibitor. The potency of the mutant can be further enhanced by the introduction of the mutations V4A and P6V
-
tissue inhibitor of matrix metalloproteinase-1
-
i.e. TIMP-1, recombinant, human
-
tissue inhibitor of matrix metalloproteinases-1
-
weak inhibitor
-
tissue inhibitor of matrix metalloproteinases-2
-
effective inhibitor
-
tissue inhibitor of matrix metalloproteinases-3
-
effective inhibitor
-
tissue inhibitor of metalloproteinase 2
-
-
Tissue inhibitor of metalloproteinase-1
-
TIMP-1
-
Tissue inhibitor of metalloproteinase-2
-
-
-
tissue inhibitor of metalloproteinases-2
-
tissue inhibitor of MMP-2
-
tissue inhibitor of MMP-3
-
i.e. TIMP-3
-
tissue inhibitor of MMP-4
-
i.e. TIMP-4
-
BB94
-
inhibits endothelial cell invasion
BB94
0.01 mM, dose dependent
BB94
-
supresses migration of HT1080 cells on type I collagen to 69%
BB94
-
reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
BB94
-
maturation of MT1-MMP normally occurs
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
DX-2400
enzyme activity is inhibited with 65.8 nM or 658 nM of the enzyme function-blocking antibody DX-2400
-
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
furin
concanavalin A-induced pro-matrix metalloproteinase 2 activation is inhibited in human uterine cervical fibroblasts, but not in rabbit dermal fibroblasts
-
furin
-
inhibits MT1-MMP partitioning at the plasma membrane
-
furin
-
concanavalin A-induced pro-matrix metalloproteinase 2 activation is inhibited in human uterine cervical fibroblasts, but not in rabbit dermal fibroblasts
-
GM6001
hydroxamate inhibitor, 0.001 mM, converts protease into a cell surface receptor for receptor of complement component 1q and promotes co-precipitation of the enzyme with the soluble receptor protein
GM6001
-
fully blocks proteolysis of PA83 by MT1-MMP, inhibits MT1-MMP-dependent activation of proMMP-2
GM6001
-
blocks MT1-MMP autolytic processing
GM6001
blocks conversion of active 50 kDa wild type MT1-MMP to a 37 kDa species, inhibits autolysis of both wild type and CHO-4 MT1-MMP in a dose-dependent manner and with a similar inhibitory profile
GM6001
-
pan-metalloprotease inhibitor inhibits degradation of apolipoprotein E
GM6001
-
a broad-spectrum metalloproteinase inhibitor
GM6001
-
broad-spectrum matrix metalloproteinase inhibitor, strong inhibition
GM6001
-
a broad-spectrum metalloproteinase inhibitor
ilomastat
inhibits processing to the mature form of the enzyme
marimastat
inhibits production of 18 kDa fragment during autocatalytic processing
marimastat
-
strong inhibition
testican 3
including its variant N-Tes
-
TIMP-2
-
inhibits endothelial cell invasion
-
TIMP-2
tissue inhibitor of metalloproteinases
-
TIMP-2
inhibits production of 18 kDa fragment during autocatalytic processing
-
TIMP-2
rapid binding to catalytic site of enzyme
-
TIMP-2
-
specificity of inhibitor binding of MT1-MMP, shedding of MT1-MMP ectodomain alters the balance of TIMP-2 between the cell surface and the pericellular space
-
TIMP-2
-
supresses migration of HT1080 cells on type I collagen to 62%
-
TIMP-2
-
blocks up-regulation of VEGF-A by MT1-MMP
-
TIMP-2
-
totally abolishes substrate degradation
-
TIMP-2
-
inhibitory interaction with the catalytically competent MT1-MMP active site, prevents autolytic processing
-
TIMP-2
under in vivo conditions primary inhibitor of MT1-MMP, increases endocytosis of wild type MT1-MMP
-
TIMP-2
-
potent inhibitor
-
TIMP-2
-
inhibits degradation of apolipoprotein E
-
TIMP-2
-
highly produced in brain microvessels
-
TIMP-2
-
natural inhibitor of MT1-MMP
-
TIMP-2
-
0.0002 mM, dose dependent
-
TIMP-3
-
inhibits endothelial cell invasion
-
TIMP-3
tissue inhibitor of metalloproteinases
-
TIMP-3
rapid binding to catalytic site of enzyme
-
TIMP-3
-
potent inhibitor
-
TIMP-3
-
during ischemia, loss of inhibitory control leading to increased MT1-MMP activity
-
TIMP-4
tissue inhibitor of metalloproteinases
-
TIMP-4
inhibits production of 18 kDa fragment during autocatalytic processing
-
TIMP-4
-
during ischemia, loss of inhibitory control leading to increased MT1-MMP activity
-
tissue inhibitor of metalloproteinases-2
-
-
-
tissue inhibitor of metalloproteinases-2
-
-
tissue inhibitor of MMP-2
-
MMP-2 activation involves tissue inhibitor of MMP-2, i.e. TIMP-2, as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. MT1-MMP auto-degradation is suppressed in the presence of TIMP-2, and MT1-MMP/TIMP-2 complex accumulates on cell surface. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
tissue inhibitor of MMP-2
-
MMP-2 activation involves tissue inhibitor of MMP-2, i.e. TIMP-2, as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. MT1-MMP auto-degradation is suppressed in the presence of TIMP-2, and MT1-MMP/TIMP-2 complex accumulates on cell surface. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
additional information
-
TIMP-1 does not inhibit endothelial cell invasion
-
additional information
no inhibitor: TIMP-1
-
additional information
no inhibitor: TIMP-1
-
additional information
-
no inhibitor: TIMP-1
-
additional information
no inhibitor: TIMP-1
-
additional information
-
mercaptosulfide and hydroxamate inhibitors
-
additional information
-
mercaptosulfide inhibitors, interacting exclusively at the enzyme active site, strong stereoselectivity at the P1' and zinc-binding groups, competitive and reverse inhibition
-
additional information
-
migration of HT1080 cells on type I collagen not supressed by TIMP-1
-
additional information
-
TIMP-1 does not block up-regulation of VEGF-A by MT1-MMP, aprotinin, Pefabloc SC, leupeptin and pepstatin A fail to modulate the VEGF expression, wortmannin, PD98059 nor SB203580 affect MT1-MMP-mediated VEGF induction
-
additional information
-
cells cotransfected with TIMP-1 cDNA along with MT1-MMP and pMMP-2 cDNAs result in partial inhibition of substrate degradation, down to the basal digestion level resulting from MT1-MMP alone, wortmannin and PD98059 do not interfer with MT1-MMP-induced cell migration, CDC42 (N17) and RhoA(N19) have no effect on MT1-MMP-dependent cell migration
-
additional information
-
not inhibited by tissue inhibitor of metalloproteinases-1
-
additional information
-
not inhibited by tissue inhibitor of metalloproteinase-1
-
additional information
-
not inhibited by TIMP-1
-
additional information
-
not inhibited by TIMP-1
-
additional information
-
not inhibited by TIMP-1
-
additional information
-
MT1-MMP is inhibited by endogenous inhibitors TIMP-2, -3, and -4, but not by TIMP-1. MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview
-
additional information
-
not inhibited by E-64 and aprotinin
-
additional information
design, synthesis, and biological evaluation of bifunctional inhibitors of membrane type 1 matrix metalloproteinase (MT1-MMP), overview
-
additional information
-
insensitive to TIMP-1
-
additional information
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview
-
additional information
-
synthesis of a series of phenyl piperidine a-sulfone hydroxamate derivatives, inhibitory potencies on different MMPs, overview. No inhibition by derivatives 1-cyclopropyl-N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]piperidine-4-carboxamide, 4-([4-[4-(2,4-dimethylphenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-[(4-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-([4-[4-(2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide, 4-([4-[4-(2-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-[(4-[4-[2-(trifluoromethyl)phenyl]piperidin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide, 4-([4-[4-(2-ethoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, 4-([4-[4-(4'-fluorobiphenyl-4-yl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, and 4-[(4-[4-[2-ethyl-5-(propan-2-yl)phenyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
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.
0.00344
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
pH 7.5, 37°C, mature and mutant enzyme
0.0151 - 0.0368
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
0.0003 - 0.32
collagen I alpha-1 chain
-
0.00065 - 0.12
collagen I alpha-2 chain
-
0.00086 - 0.17
collagen type I alpha-1 chain
-
0.00025 - 0.53
collagen type I alpha-2 chain
-
0.0006 - 0.0028
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
0.009 - 0.01
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
0.000034
type I collagen chain alpha-1
-
at 37°C
-
0.000035
type I collagen chain alpha-2
-
at 37°C
-
additional information
additional information
-
0.0151
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant wild-type membrane-bound enzyme
-
0.0186
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant soluble enzyme
-
0.0234
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the C-terminal domain
-
0.0368
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the HPX domain
-
0.0003
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.00077
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.0027
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.32
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.00065
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.0031
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.0079
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.12
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.00086
collagen type I alpha-1 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.045
collagen type I alpha-1 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.12
collagen type I alpha-1 chain
-
3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.17
collagen type I alpha-1 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.00025
collagen type I alpha-2 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.004
collagen type I alpha-2 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.14
collagen type I alpha-2 chain
-
3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.53
collagen type I alpha-2 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.0006
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 10°C, recombinant enzyme
0.0018
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 25°C, recombinant enzyme
0.0021
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 30°C, recombinant enzyme
0.0028
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 37°C, recombinant enzyme
0.009
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
pH 7.5, Tyr112-Gly284 fragment
0.01
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
pH 7.5, Tyr112-Gly288 fragment
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
increase in substrate triple-helical thermal stability is not detrimental to enzyme binding of substrate
-
additional information
additional information
steady-state kinetics and thermodynamics over a wide range of temperatures and pressures, stopped-flow fluorescence technique
-
additional information
additional information
-
steady-state kinetics and thermodynamics over a wide range of temperatures and pressures, stopped-flow fluorescence technique
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.14 - 0.84
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
0.019 - 1.1
collagen I alpha-1 chain
-
1.52 - 255.6
collagen I alpha-2 chain
-
0.3 - 10.41
collagen type I alpha-1 chain
-
0.0089 - 58.61
collagen type I alpha-2 chain
-
0.33 - 6.8
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
0.02 - 0.055
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
1.05
type I collagen chain alpha-1
-
at 37°C
-
0.99
type I collagen chain alpha-2
-
at 37°C
-
additional information
additional information
-
increase in substrate triple-helical thermal stability is detrimental to enzyme turnover of substrate
-
0.14
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant wild-type membrane-bound enzyme
-
0.2
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the HPX domain
-
0.21
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the C-terminal domain
-
0.84
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant soluble enzyme
-
0.019
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.47
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.68
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
1.1
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
1.52
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
5.79
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
9.89
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
255.6
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.3
collagen type I alpha-1 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.43
collagen type I alpha-1 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
4.56
collagen type I alpha-1 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
10.41
collagen type I alpha-1 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.0089
collagen type I alpha-2 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.014
collagen type I alpha-2 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
4.09
collagen type I alpha-2 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
58.61
collagen type I alpha-2 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
0.33
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 10°C, recombinant enzyme
2.1
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 25°C, recombinant enzyme
3.4
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 30°C, recombinant enzyme
6.8
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 37°C, recombinant enzyme
0.02
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
pH 7.5, Tyr112-Gly288 fragment
0.055
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
pH 7.5, Tyr112-Gly284 fragment
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.44 - 45.2
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
3.4 - 880
collagen I alpha-1 chain
-
730 - 3200
collagen I alpha-2 chain
-
2.5 - 360
collagen type I alpha-1 chain
-
3.5 - 350
collagen type I alpha-2 chain
-
550 - 2429
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
5.44
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the HPX domain
-
8.97
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the C-terminal domain
-
9.27
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant wild-type membrane-bound enzyme
-
45.2
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37°C, recombinant soluble enzyme
-
3.4
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
63
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
170
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
880
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
730
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
2100
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
2300
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
3200
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
2.5
collagen type I alpha-1 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
88
collagen type I alpha-1 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
100
collagen type I alpha-1 chain
-
O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
360
collagen type I alpha-1 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
3.5
collagen type I alpha-2 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
30
collagen type I alpha-2 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
110
collagen type I alpha-2 chain
-
O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
350
collagen type I alpha-2 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C
-
550
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 10°C, recombinant enzyme
1167
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 25°C, recombinant enzyme
1619
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 30°C, recombinant enzyme
2429
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 37°C, recombinant enzyme
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0.0000039
(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N-hydroxy-2-[[(4'-methoxybiphenyl-4-yl)sulfonyl](propan-2-yloxy)amino]butanamide
Homo sapiens
pH 7.5, 37°C
0.000034
(2R)-4-(acetylamino)-2-[(biphenyl-4-ylsulfonyl)amino]-N-hydroxybutanamide
Homo sapiens
pH 7.5, 37°C
0.01
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.000023
CGS-27023A
Homo sapiens
pH 7.5, 37°C
0.000041
N,N'-bis(4-[[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]amino]-4-oxobutyl)benzene-1,3-dicarboxamide
Homo sapiens
pH 7.5, 37°C
0.00008
N,N'-bis[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]benzene-1,3-dicarboxamide
Homo sapiens
pH 7.5, 37°C
0.000007
N,N'-bis[4-[(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)amino]-4-oxobutyl]benzene-1,3-dicarboxamide
Homo sapiens
pH 7.5, 37°C
0.000014
N-(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)-N'-(2-[[4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]
Homo sapiens
pH 7.5, 37°C
0.01
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.00286
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.00822
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
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evolution
membrane-type matrix metalloproteinase 1 (MT1-MMP, also MMP14) is a type I membrane protein belonging to the MT-MMP family
malfunction
-
increased levels of soluble MT1-1/MMP-14 in the serum of breast cancer patients may have implications in the pathogenesis of the disease
malfunction
-
loss of MMP14 activity increases steady-state vascular leakage, MMP14 activity impacts vascular leakage, mechanism, overview
malfunction
-
loss of MMP14 activity increases steady-state vascular leakage, MMP14 activity impacts vascular leakage, mechanism, overview
malfunction
-
MMP14 mediates tumor cell surface MHC class I chain-related molecule A shedding, suppression of MMP14 expression blocks MICA shedding, while overexpression of MMP14 enhances it. The regulation is independent of the activity of a disintegrin and metalloproteinases, overview
malfunction
-
MMP14 mediates tumor cell surface MHC class I chain-related molecule A shedding, suppression of MMP14 expression blocks MICA shedding, while overexpression of MMP14 enhances it. The regulation is independent of the activity of a disintegrin and metalloproteinases, overview
malfunction
-
membrane-type 1 matrix metalloproteinase knockdown in DU-145 cells decreases activity of reactive oxygen species 8-hydroxydeoxyguanosine
malfunction
MT1-MMP inhibition restores sensory axon regeneration and attenuates hypersensitivity caused by peripheral nerve injury
malfunction
a single mutation in the putative membrane interaction region of MT1-MMP (Ser466Pro) results in lower enzyme activation by bicelles
malfunction
Cartoon mice harbor the single point mutation S466P in the MT1-MMP hemopexin domain, a 200-amino acid segment. The S466P substitution generates a misfolded, temperature-sensitive mutant that is abnormally retained in the endoplasmic reticulum (ER). The MT1-MMPS466P mutation replicates the phenotypic status of Mt1-mmp-null animals as well as the functional characteristics of MT1-MMP-/- cells. The wild-type hemopexin domain does not play a required role in regulating MT1-MMP trafficking, as a hemopexin domain-deletion mutant is successfully mobilized to the cell surface and displays nearly normal collagenolytic activity. Cartoon mice exhibit a pattern of stunted growth, kyphosis, and rounded skulls, Cartoon mouse phenotype, detailed overview. Cartoon mouse fibroblasts are devoid of pericellular collagenolytic activity
malfunction
deletion of the MT1-MMP cytoplasmic tail enhances cell surface activity, with both kcat and KM values affected, while deletion of the hemopexin-like domain negatively impacts KM and increases kcat
malfunction
functional analysis of a hypomorphic allele shows that MMP14 catalytic activity is the prime determinant of the Winchester syndrome (WS) phenotype. The WS phenotype includes craniofacial malformations, kyphosis, short-stature, and reduced bone density owing to defective collagen remodeling
malfunction
membranous ossifying Weberian vertebral bodies in mmp14a/b KO fish are irregularly shaped, with clusters of multinucleated cells in their dorsal aspect. Mutant mmp14a/b KO fish have abnormal endochondral and membranous ossification, but collagen deposition is unaffected by mmp14a/b KO
malfunction
Mmp14-/- mice display defects in branching activity, phenotype, overview. Immunohistological assessments of Mmp14-/- mammary gland sections reveal no differences in the expression or organization of CK18, CK14, or alphaSMA from P0 through P10. MMP14 can activate MMP2 in vivo, a proteinase thought to mediate MMP14 function and to compensate partially for Mmp14 deficiency
metabolism
-
MMP-14 is involved in gene network of deregulated genes associated to cell cycle, overview
metabolism
-
MMP-14 is involved in the extracellular matrix metabolism
metabolism
-
type I collagen fibrils posttranslationally regulate perivascular MMP activity and TGFbeta bioavailability, which in turn regulate vascular homeostasis by altering vessel stability and leakage. Matrix metalloproteinase 14 and transforming growth factor beta 1 are involved in a pathway regulating vessel stability in tissues, the pathway mediates vessel stability and vascular response to tissue injury
metabolism
-
type I collagen fibrils posttranslationally regulate perivascular MMP activity and TGFbeta bioavailability, which in turn regulate vascular homeostasis by altering vessel stability and leakage. Matrix metalloproteinase 14 and transforming growth factor beta 1 are involved in a pathway regulating vessel stability in tissues, the pathway mediates vessel stability and vascular response to tissue injury
metabolism
an MT1-MMP/Notch1 signaling pathway supports melanoma cell growth
metabolism
cleavage of hepatocyte growth factor activator inhibitor-1 by membrane-type MMP-1 activates matriptase
metabolism
branching morphogenesis is thought to depend on the mobilization of the membrane-anchored matrix metalloproteinases MMP14 (MT1-MMP) and MMP15 (MT2-MMP), which drive epithelial cell invasion by remodeling the extracellular matrix and triggering associated signaling cascades. Different roles played by MMP14 or MMP15 in the mammary gland epithelial compartment and in development of mammary gland, overview. Whereas MMP14 promotes white fat-associated adipogenesis in the developing mammary gland, MMP15 serves as an endogenous suppressor of beige/brown fat production
metabolism
CCN5 (WISP2) is processed in the variable region by MMP14 and MMP2, as well as by MMP1, 3, 7, 8, 9 and 15. CCN5 cleavage by proangiogenic MMPs results in removal of an angiogenic brake held by CCN5. CCN3 is processed most efficiently by MMP14, 2 and 1 from about 30 kDa to fragments of 20-25 kDa, and less efficiently by MMP8 and 9
metabolism
matrix metalloproteinases (MMP) are an important family of proteases which catalyze the degradation of extracellular matrix components
metabolism
MMP14 and MMP15 are involved in trophoblast invasion
physiological function
-
an essential role for MT1-MMP in the process of angiogenesis and bone growth. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities. MT1-MMP plays an essential role in angiogenesis, CD151 may contribute to endothelial homeostasis through the regulation of MT1-MMP. CD9, CD81, and TSPAN12 also associate with cell surface molecules including integrins. Tetraspanin-regulated cell surface localization of MT1-MMP increases the local concentration for focal proteolysis within the pericellular environment and leads to efficient extracellular matrix degradation and MMP-2 activation
physiological function
-
membrane-type 1 matrix metalloproteinase 1 is a potent modulator of the pericellular microenvironment and regulates cellular functions in physiological and pathological settings in mammals. MT1-MMP mediates its biological effects through cleavage of specific substrate proteins. Cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment
physiological function
-
MMP14 regulates TGFbeta bioactivity and vascular stability, MMP14 also regulates the bioavailability of several chemokines and growth factors. MMP14-mediated resistance to vascular and VEGF leakage is accompanied by decreased appearance of leakage sites in vessels with perivascular cell coverage
physiological function
-
podosomes mediate migration of dendritic cells through tissues by means of myosin-II-dependent protrusion coupled to MMP-14-dependent degradation and endocytosis. Degradation, protrusion and endocytosis in this system are dependent on the matrix metalloproteinase MMP-14
physiological function
-
tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities. MT1-MMP plays an essential role in angiogenesis, CD151 may contribute to endothelial homeostasis through the regulation of MT1-MMP. CD9, CD81, and TSPAN12 also associate with cell surface molecules including integrins. Tetraspanin-regulated cell surface localization of MT1-MMP increases the local concentration for focal proteolysis within the pericellular environment and leads to efficient extracellular matrix degradation and MMP-2 activation
physiological function
-
MT-MMP1 must form a homophilic ternary complex with TIMP-2 and pro-MMP-2 to activate MMP-2
physiological function
-
in endothelial cells, MMP-14 is the main endoglin shedding protease
physiological function
-
MT1-MMP coexpressed with heparin-binding epidermal growth factor in ovarian carcinoma cells potentiates the activity of heparin-binding epidermal growth factor to promote invasive tumor growth and spreading in vivo. MT1-MMP promotes heparin-binding epidermal growth factor-dependent proliferation of ovarian carcinoma cells
physiological function
-
oxidative stress and prostate cancer progression are elicited by membrane-type 1 matrix metalloproteinase
physiological function
-
the processing of heparin-binding epidermal growth factor by MT1-MMP converts the substrate into a heparin-independent growth factor with enhanced mitogenic activity, and thereby, expression of both proteins costimulates tumor cell growth in vitro and in vivo
physiological function
-
the processing of heparin-binding epidermal growth factor by MT1-MMP converts the substrate into a heparin-independent growth factor with enhanced mitogenic activity, and thereby, expression of both proteins costimulates tumor cell growth in vitro and in vivo
physiological function
activated hepatic stellate cells require membrane type 1 matrix metalloproteinase-cleaved collagen for their survival
physiological function
both neuronal glial antigen 2 shedding and axonal growth depend on the pericellular remodeling executed by MT1-MMP/MMP-14
physiological function
in tumor cells the enzyme downregulates fibroblast growth factor-2 signaling by reducing the amount of fibroblast growth factor-2 signaling bound to the cell surface with high and low affinity
physiological function
membrane type 1 matrix metalloproteinase-dependent activation of MMP-2 is required for optimal neurite outgrowth
physiological function
overexpression of MT1-MMP induces epithelial-to-mesenchymal transition and results in the acquisition of cancer stem cell-like properties in SCC-9 cells. Upon up-regulation of the enzyme, the cells undergo EMT, in which they presented a fibroblast-like phenotype and have a decreased expression of epithelial markers (E-cadherin, cytokeratin18 and beta-catenin) and an increased expression of mesenchymal markers (vimentin and fibronectin)
physiological function
the enzyme is critical to monocyte migration
physiological function
the enzyme promotes cancer cell invasion. The MT-LOOP-dependent enzyme localization to the cell adhesion complex promotes cellular invasion (the MT-LOOP is a region in the catalytic domain of MT1-MMP (163PYAYIREG170))
physiological function
the enzyme promotes Notch1 activation in melanoma cells
physiological function
the enzyme promotes tumor progression by circumventing the collagen-induced up-regulation of the pro-apoptotic tumor suppressor BIK. The enzyme contributes to the inactivation of the DDR1-BIK signalling axis through the cleavage of collagen fibres and/or the alteration of DDR1 receptor signalling unit, without triggering a drastic remodelling of the transcriptome of MCF-7 cells
physiological function
cell surface localization of MT1-MMP restricts substrate binding and protein-coupled motions (based on changes in both kcat and KM) for catalysis
physiological function
collagen degradation and proMMP-2 activation are major functions of MT1-MMP to promote cancer cell invasion. Both processes require MT1-MMP homodimerization on the cell surface
physiological function
enzyme MT1-MMP plays a crucial role in many physiological and pathological processes, especially in tumor invasion and metastasis
physiological function
heterotrimeric G proteins directly regulate membrane-localized MMP14/MT1-MMP, resulting in HB-EGF release and EGF receptor transactivation. Analysis of the membrane-delimited mechanism for EGF receptor transactivation. MMP14 is a heterotrimeric G protein-regulated effector
physiological function
heterotrimeric G proteins directly regulate membrane-localized MMP14/MT1-MMP, resulting in HB-EGF release and EGF receptor transactivation. Analysis of the membrane-delimited mechanism for EGFreceptor transactivation. MMP14 is a heterotrimeric G protein-regulated effector
physiological function
membrane type 1 matrix metalloproteinase (MT1-MMP) is a type I transmembrane cell-surface protease that has been implicated in numerous pathologies. The pericellular collagenase membrane-type 1 matrix metalloproteinase (MT1-MMP) and membrane-mimicking environments interplay in substrate binding and processing. MT1-MMP transiently associates with bicelles and cells through distinct residues in blades III and IV of its hemopexin-like domain, while binding of collagen-like triple helices occurs within blades I and II of this domain. MT1-MMP collagenolytic activity appears critical for transmigration of tumor cells, endothelial cells, and fibroblasts through collagen matrices, while post-myocardial infarction survival has been correlated to the collagenolytic potential of cardiac fibroblasts, where MT1-MMP is the dominant collagenase within myocardial tissues
physiological function
membrane type 1-matrix metalloproteinase (MT1-MMP or MMP-14) is involved in the degradation of extracellular matrix and tumor invasion. MT1-MMP is involved in the mediation of pericellular proteolysis of extracellular matrix components, essential for the physiological remodeling processes such as tissue repair, development, and morphogenesis. MT1-MMP is overexpressed in many cancer types and increases tumor cell growth, invasion, and metastasis by degrading extracellular matrix components and making paths through surrounding tissues
physiological function
membrane type-1 matrix metalloproteinase (MT1-MMP) plays a pivotal role in cellular growth and migration by activating proMMP-2 into active MMP2. MT1-MMP inhibits the tetherin activity of Bst-2 (bone marrow stromal cell antigen 2), a type II membrane protein, by interacting with Bst-2, not via downregulation of Bst-2. The cytoplasmic domains of both Bst-2 and MT1-MMP play critical roles within this interaction. Bst-2 inhibits MT1-MMP activity through their interaction resulting in a decrease of proMMP2 activation
physiological function
membrane type-1 MMP (MT1-MMP) is elevated during thoracic aortic aneurysm (TAA) development in mouse models, and plays an important role in the activation of MMP-2 and the release of matrix bound TGF-beta. Enzyme MT1-MMP is subject to protein kinase C (PKC)-mediated regulation via reversible phosphorylation, which alters intracellular trafficking and activity with TAA. MT1-MMP abundance increases in aortas from both TAA groups. Active MMP-2 is increased only in large TAAs. Abundance of phosphorylated MT1-MMP and activated-PKC-delta is enhanced in small versus large TAAs. Phosphorylation of MT1-MMP mediates its activity through directing cellular localization, shifting its role from MMP-2 activation to intracellular signaling
physiological function
metalloproteinase MMP14 (MT1-MMP) drives epithelial cell invasion by remodeling the extracellular matrix and triggering associated signaling cascades. It plays a role in mammary gland development. Transcriptome profiling reveals a key role for MMP14 and MMP15 in regulating mammary gland adipocyte differentiation. MMP14 promotes the generation of white fat depots crucial for energy storage. MMP14-dependent regulation of branching morphogenesis, overview. MMP14 can activate MMP2 in vivo, a proteinase thought to mediate MMP14 function and to compensate partially for Mmp14 deficiency. Early mammary gland branching proceeds independently of MMP14, MMP14-independent epithelial cell sorting, proliferation, senescence and extracellular matrix organization, overview
physiological function
MMP14 is a regulator of angiogenesis, it cleaves CCN5 and abrogates the angiostatic activity. CCN5 is an angiogenesis inhibitor that is inactivated by MMP14 cleavage. Proteolytic processing of CCN3 by MMP14
physiological function
the cell-surface collagen degradation by MT1-MMP involves DDR2-mediated collagen signaling
physiological function
-
heterotrimeric G proteins directly regulate membrane-localized MMP14/MT1-MMP, resulting in HB-EGF release and EGF receptor transactivation. Analysis of the membrane-delimited mechanism for EGF receptor transactivation. MMP14 is a heterotrimeric G protein-regulated effector
-
additional information
a small conformational change is detected at 37°C, which is responsible for the change in activity observed at the same temperature. Pressure decreases the enzymatic activity until complete inactivation occurs at 2 kbar. The inactivation is associated with changes in the rate-limiting step of the reaction caused by additional hydration of the active site upon compression and/or minor conformational changes in the active site region
additional information
-
a small conformational change is detected at 37°C, which is responsible for the change in activity observed at the same temperature. Pressure decreases the enzymatic activity until complete inactivation occurs at 2 kbar. The inactivation is associated with changes in the rate-limiting step of the reaction caused by additional hydration of the active site upon compression and/or minor conformational changes in the active site region
additional information
an initial structural framework defines the role(s) of cell membranes in modulating proteolysis. Examination of simultaneous membrane interaction and triple-helix binding reveals a possible regulation of proteolysis due to steric effects of the membrane. Activity analysis of MT1-MMP in membrane-like environments, Interaction of the isolated 15N MT1-MMP HPX domain with bilayers, with a collagen-like triple helical peptide (THP) alone or in the presence of bicelles, or with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), interaction of 15N sMT1-MMP with bicelles, NMR spectroscopic analysis, modelling, overview
additional information
DDRs are receptor tyrosine kinases (RTKs) in which phosphorylation of their cytoplasmic domain is induced by binding to collagen at their ectodomain. Discoidin domain receptor 2 (DDR2) mediates type I collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts. Knocking down DDR2, but not the beta1 integrin subunit, a common subunit for all collagen-binding integrins, inhibits the collagen-induced MT1-MMP-dependent activation of pro-MMP-2 and upregulation of MT1-MMP at the gene and protein levels. This DDR2-mediated mechanism is only present in non-transformed mesenchymal cells, as collagen-induced MT1-MMP activation in HT-1080 fibrosarcoma cells and MT1-MMP function in MDA-MB231 breast cancer cells are not affected by DDR kinase inhibition
additional information
-
DDRs are receptor tyrosine kinases (RTKs) in which phosphorylation of their cytoplasmic domain is induced by binding to collagen at their ectodomain. Discoidin domain receptor 2 (DDR2) mediates type I collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts. Knocking down DDR2, but not the beta1 integrin subunit, a common subunit for all collagen-binding integrins, inhibits the collagen-induced MT1-MMP-dependent activation of pro-MMP-2 and upregulation of MT1-MMP at the gene and protein levels. This DDR2-mediated mechanism is only present in non-transformed mesenchymal cells, as collagen-induced MT1-MMP activation in HT-1080 fibrosarcoma cells and MT1-MMP function in MDA-MB231 breast cancer cells are not affected by DDR kinase inhibition
additional information
solvent water interactions within the active site of the membrane type I matrix metalloproteinase, crystal structure analysis, quantum mechanics/molecular mechanics geometries and modelling, structure modelling, overview
additional information
the catalytic domain comprises residues Tyr112-Gly284
additional information
visualization of membrane-bound, active MT1-MMP is achieved by fluorescence resonance energy transfer (FRET) imaging of surface-anchored sensors. An initial MT1-MMP sensor was created using the Cys-Pro-Lys-Glu-Ser-Cys-Asn-Leu-Phe-Val-Leu-Lys-Asp sequence, derived from the MT1-MMP cleavage site in proMMP-2. The C-terminus plays a required role in regulating proteolytic activity at the cell surface
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C127S
site-directed mutagenesis, no significant difference in activity is observed for the mutant C127S and the wild-type MT1-MMP
C574A
inefficient in stimulating cell adhesion, migration and invasion, mutation negatively affects cell adhesion
C574S
-
substitution in the cytoplasmic domain, reduction of pro-MMP2 activation, no up-regulation of VEGF expression
K110A
processing of the enzyme is blocked
K44A
-
dominant negative dynamin mutation controlled by a separate cytomegalovirus promoter MT1/K44A, leading to increased substrate digestion that is contributed by enhanced cell migration resulting from the accumulation of MT1-MMP ant the plasma membrane
K581R
-
ubiquitination-deficient mutant
L571A/L572A
mutation leads to reduced internalization of enzyme
L571A/L572A/L578A/L579A
mutation leads to reduced internalization of enzyme
L571A/L572A/Y573A
mutation leads to reduced internalization of enzyme, no effect on cell motility
L578A/L579A
mutation leads to reduced internalization of enzyme
MT1F-DELTACat
-
catalytic domain-deletion mutant
R108A
processing of the enzyme is blocked
R111A
processing of the enzyme is blocked
R111H
site-directed mutagenesis, MMP14 R111H enzyme is processed normally in human MRC-5V1 cells and is trafficked to the cell surface, the mutation partially impairs the catalytic activity of MMP14, thus MMP14 R111H retains partial gelatinolytic and pro-MMP2 hydrolyzing activity. The mutant demonstrates significantly reduced migratory behavior when compared with wild-type MMP14
R89A
can activate matrix metalloproteinase 2
R92C
site-directed mutagenesis, the mutation impairs cell surface localization. The mutant demonstrates significantly reduced migratory behavior when compared with wild-type MMP14
T17R
site-directed mutagenesis, the mutation impairs cell surface localization, MMP14 T17R distributed throughout the cytoplasm. The mutant demonstrates significantly reduced migratory behavior when compared with wild-type MMP14
T567A
-
substitution in the cytoplasmic domain, pro-MMP2-activating capacity not affected, similar VEGF upregulation
V582A
internalization of enzyme is not affected
Y112F
normal enzyme processing
Y573A/L571A/L572A/L578A/L579A
mutation leads to reduced internalization of enzyme
E240A
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catalytically inactive
S466P
naturally occuring mutation causing the Cartoon phenotype, Cartoon mice harbor the single point mutation in the MT1-MMP hemopexin domain, a 200-amino acid segment that is thought to play a critical role in regulating MT1-MMP collagenolytic activity
E240A
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inactive
E240A
catalytically inactive
E240A
polypeptide can not be refolded
E240A
catalytically inactive, inefficient in stimulating cell migration and invasion
E240A
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catalytically inert
E240A
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expressed on transfected cell surface but fails to activate pMMP-2
E240A
loss of MT1-MMP activity
E240A
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substitution in the active site, unable to activate exogenous pro-MMP2, fails to induce VEGF mRNA expression
E240A
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a catalytically inactive MT1-MMP mutant
E240A
inactive MMP14 mutant
E240A
site-directed mutagenesis, inactive enzyme mutant
S466P
site-directed mutagenesis
S466P
site-directed mutagenesis, the mutation impairs cell surface localization
S577A
internalization of enzyme is not affected, enhanced cell motility
S577A
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substitution in the cytoplasmic domain, pro-MMP2-activating capacity not affected, similar VEGF upregulation
Y573A
mutation leads to reduced internalization of enzyme
Y573A
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the mutant displays significant reduction of ubiquitination
additional information
generation of a mmp14a/b knockout zebrafish model, phenotype, overview
additional information
generation of a mmp14a/b knockout zebrafish model, phenotype, overview
additional information
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generation of a mmp14a/b knockout zebrafish model, phenotype, overview
additional information
catalytic domain: TM1 MMPcat, DELTA269-550 and deletion of transmembrane and cytoplasmic domain: DELTA TM MT1 MMP, DELTA501-559
additional information
mutant defective in catalytic domain, deletion of transmembrane/cytoplasmic domain, deletion of hemopexin domain abolishes enzyme activity, whereas substitution of transmembrane/cytoplasmic membrane with Il-2 receptor does not affect it
additional information
truncation mutant MT1DELTAC with more robust pro-MMP-2 activation and cell surface expression than wild type enzyme, mutant is resistant to increased cell surface expression after concanavalin A treatment
additional information
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catalytic inactive mutant (E/A) of MT1-MMP
additional information
deletions delta Cat or point mutations CHO-1 and CHO-4, which preserve a relative electrophoretic mobility shift following desialylation similar to the wild type protein, moreover mutant CHO-4 is insensitive to sialidase A treatment, CHO-3 and CHO-4 mtuants are unable to effectively catalyze pro-MMP-2 activation
additional information
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deletions delta Cat or point mutations CHO-1 and CHO-4, which preserve a relative electrophoretic mobility shift following desialylation similar to the wild type protein, moreover mutant CHO-4 is insensitive to sialidase A treatment, CHO-3 and CHO-4 mtuants are unable to effectively catalyze pro-MMP-2 activation
additional information
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MMP-14delta279-523, linker and C-terminal hemopexin-like domain deleted, does not undergo rapid autoproteolysis, relatively small differences to wild type
additional information
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mutant Sol.MT, fails to activate pMMP-2, mutant MTdeltaC, pMMP-2 activation as compared with wild type, neither cell type-dependent nor extracellular matrix component-dependent
additional information
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partial deletion of the catalytic domain deltacd or the cytoplasmic tail delta577 of MT1-MMP, unable to activate exogenous pro-MMP2, no up-regulation of VEGF expression
additional information
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specific amino acid substitutions at the Val524-Ile525 site have no effect on shedding of the 50 kDa species, whereas deletion of the entire stem region deltastem-MT1, which lacks Pro509-Gly535, completely abrogates shedding of the 50 kDa species
additional information
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transcription factor EGR1 gene silencing by siRNA blocks collagen-induced MT1-MMP expression and collagen invasion, integrin signaling through a SRC kinase-dependent pathway is necessary for EGR1 induction, overview
additional information
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suppression of MMP14 expression in human MCF-7 breast cells blocks MHC class I chain-related molecule A, MICA, shedding, while overexpression of MMP14 enhances it, overview
additional information
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construction of truncation mutant MT1EADELTATM lacking the pro-peptide and the transmembrane and cytoplasmic domains. Mutant MT1EADELTATM shows different mobility in reducing and non-reducing PAGE compared to the wild-type enzyme, the disulfide bond in the PEX domain is correctly folded, there is no intermolecular disulfide bond formation, and the complex with TIMP-2 is also correctly formed. A PEX-domain-deleted MT1-MMP mutant is no longer able to activate proMMP-2, but retains some proteolytic activity and forms the ternery complex with proMMP-2 and TIMP-2. A MT1-MMP mutant lacking the catalytic domain is catalytically inactive and inhibits the dimerization and complex formation of the enzyme, overview
additional information
deletion of the MT1-MMP cytoplasmic tail or deletion of the hemopexin-like domain
additional information
specific enzyme knockout by MT1-MMP siRNA
additional information
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specific enzyme knockout by MT1-MMP siRNA
additional information
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enzyme-deficient fibroblasts show impaired invasion of type I collagen matrices, MT1-MMP null fibroblasts fail to penetrate the matrix
additional information
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a MT1-MMP-deficient mouse produces only a faint level of active MMP-2. MT1-MMP-null mice have severe defects in skeletal development and angiogenesis and die within several weeks after birth, phenotype, overview
additional information
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construction of MMP14 null B6 mice
additional information
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generation of mutant Cola1(I)r/r mice, phenotype, overview. The mouse model of age-related dermal fibrosis, where MMP14 activity and TGFbeta bioavailability are chronically elevated, or in mice that ectopically express TGFbeta in the epidermis, cutaneous vessels are resistant to acute vessel leakage. Inhibition of ALK5 further enhances vascular leakage into the interstitium and facilitated increases delivery of high molecular weight compounds into premalignant tissue and tumors. Steady-state leakage of capillaries in back skin is also higher in MMP14 null mice versus age-matched heterozygous and wild-type littermates, overview
additional information
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suppression of MMP14 expression in mouse MyC-CaP prostate cancer cells blocks MHC class I chain-related molecule A, MICA, shedding, while overexpression of MMP14 enhances it, overview
additional information
MMP14 enzyme knockout in mammary gland epithelial cells
additional information
siRNA-mediated knockout of MMP14 in NIH3T3 cells
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18 kDa inactive fragment ranging from Tyr 112 to Ala 255, 21 kDa fragment ranging from Tyr 122 to Gly 284 and truncated form lacking the cytosolic domain
C-terminal truncated form containing the hemopexin-like domain
catalytic and hinge domain
catalytic and hinge domains of MMP-14 (Tyr112-Ile318), containing an N-terminal methionine and C-terminal hexa-histidines (chMMP-14) expressed as inclusion body in Escherichia coli
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catalytic domain of MT1-MMP expressed in Escherichia coli, MT1-MMP cDNAs cloned into vector pcDNA3-zeo
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cloned into a pcDNA3.0 expression vector
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cloned into pSG5 vector, expression in COS-1 cells
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cloned intop pCR-Blunt II TOPO vector
expressed in adenovirus
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expressed in breast adenocarcinoma cells
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells and COS-7 cells
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expressed in lentivirus
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expressed in LNCaP cells
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expressed in mouse bone marrow-derived stromal cells
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expressed in polarized human cancer cell lines A375, 451Lu, and HT-1080
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expressed in prostate cancer LNCaP cells
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expression in non-malignant monkey kidney epithelial BS-C-1 and CV-1 cells by co-infecting the cells with the vTF7-3 and vTF-MT1 vaccinia viruses
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gene MMP14, quantitative RT-PCR enzyme expression analysis
gene MMP14, recombinant coexpression of MMP14 with CCN5 in MCF-7 and CHO-K1 cells
gene MMP14, recombinant expression in Escherichia coli strain BL21(DE3)
gene MMP14, recombinant expression of C-terminally His-tagged wild-type and mutant Co2+-MT1-MMPs and apoenzymes in Escherichia coli strain BL21(DE3), the plasmid contains the catalytic domain of human MT1-MMP together with the hinge linker to the hemopexin-like domain (residues 112-292). Interaction of the His-tag with the protein cleft, modelling, overview
gene MMP14, recombinant expression of N-terminally HA3-tagged and C-terminally EGFP-tagged wild-type and mutant R111H enzymes in in MRC-5V1 immortalized human fetal lung fibroblasts, in which mutant protein localization is unlikely to be affected by dimerization with endogenous MMP14
gene MMP14, recombinant expression of wild-type and mutant enzymes in COS-1 cells
gene MMP14, recombinant expression of wild-type enzyme, a soluble enzyme form, and different enzyme MT1-MMP domain constructs in MCF-7 cells, overview
gene MMP14, transient recombinant overexpression of MT1-MMP in HT-1080 cells, quantitative expression analysis
gene mmp14a, recombinant expression of C-terminally HA-tagged enzyme in in MRC-5V1 immortalized human fetal lung fibroblasts, in which mutant protein localization is unlikely to be affected by dimerization with endogenous MMP14
gene mmp14b, recombinant expression of C-terminally HA-tagged enzyme in in MRC-5V1 immortalized human fetal lung fibroblasts, in which mutant protein localization is unlikely to be affected by dimerization with endogenous MMP14
MT1-MMP cDNA subcloned between the HindIII and EcoRI sites of pCDNA3.1 Zeo+ mammalian expression vector, annealed olignucleotides coding for huMT1-MMP signal sequence cloned upstream of ECFP in the NheI-AgeI sites of the pEGFP-C1 vector, amplified residues 283-582 of huMT1-MMP cloned into the BgIII-EcoRI sites of huMT1SSc1 in-frame with EGFP
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MT1-MMP expression in both the epithelial and stromal elements of head and neck squamous cell carcinoma cell line, low enzyme activity
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MT1-MMP, lacking the C-terminal transmembrane and cytoplasmic domains, expression in Pichia pastoris
recombinant cdMT1-MMP expressed in Escherichia coli, recombinant deltaTM-MT1-MMP expressed in Pichia pastoris
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recombinant expression of the truncation mutant MT1EADELTATM in Escherichia coli, expression of the PEX-domain-deleted MT1-MMP mutant
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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS in inclusion bodies
stable expression of FLAG-tagged MT1-MMP in A-431 cells, co-expression with Myc-tagged MT1-MMP
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the catalytic domain (Tyr112-Val335) is expressed in Escherichia coli BL21 cells
truncated forms, mutations and wild type
two truncated forms: CAT domain and CAT/PEX domain
wild-type and various mutants: deletion of catalytic domain, deletion of POX domain, deletion of cytoplasmic tail, deletion of 8, 8 or 12 amino acids at C-terminus, all deletions except catalytic and PEX domain reduced internalization of the protein
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expressed in COS-7 cells
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analysis
screening, identification, and characterization of affinity peptides, AF7p and Cy5.5-HS7, specific to MT1-MMP and application in tumor imaging, overview. Feasibility of using the subtraction biopanning strategy to screen the affinity peptide targeting MT-loop regions and HS7 is a superior probe for noninvasively imaging MT1-MMP expression in MT1-MMP-positive tumor models. Usage of HS7 in early diagnosis of tumors and in peptide-mediated drugs
diagnostics
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MMP-14 can be a biomarker in early development of mesothelioma tumours, overview
drug development
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MMP-14 is an effective therapeutic target in therapy of mesothelioma tumours
drug development
dimeric MT1-MMP inhibitors might be further developed and exploited as an alternative tool to reduce cancer cell invasion
medicine
the understanding of the regulatory mechanisms that control the activity of the key proteinase in tumor cell invasion, is essential for the design of potent and safe anti-cancer therapies
medicine
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complex reciprocal effects of ERK1/2 and p38 MAPK in the regulation of MT1-MMP activity, which may complicate the use of MAPK-specific inhibitors as therapeutic agents to down-regulate the biologic effects of TGF-beta1 on pericellular collagen degradation and tumor invasion
medicine
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endothelial cell invasion of collagen I gels is MT1-MMP dependent
medicine
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full enzymatic activity of MT1-MMP is required for a specific up-regulation of VEGF-A through an activation of Src tyrosine kinase pathways
medicine
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mechanistic association between MT1-MMP levels and post-I/R remodeling, multiple targets for the interruption of augmented MT1-MMP activity and abundance with I/R
medicine
MT1-MMP and MMP gelatinase A function together in the extracellular matrix degradation or remodeling associated with metamorphosis, MT1-MMP has additional MMP gelatinase A independent roles in the development of adult longitudinal muscle in the intestine
medicine
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MT1-MMP initiates substrate degradation and enhances cell migration, hemopexin-like domain and a nonenzymatic component of the catalytic domain of MT1-MMP are essential for MT1-MMP-mediated cell migration, Rac1 participates in the MT1-MMP signal transduction pathway
medicine
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MT1-MMP is involved in cell migration and collagen-induced mitogen-activated protein kinase-extracellular signal-related kinase activation, collagen-induced mitogen-activated protein kinase-extracellular signal-related kinase activation inhances MT1-MMP activity, hemopexin-like domain of MT1-MMP inhibits collagen-induced mitogen-activated protein kinase-extracellular signal-related kinase activation and migration
medicine
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MT1-MMP proteolysis of protective antigen markers makes the MT1-MMP-expressing aggressive invasive cells resistant to the cytotoxic effect of bipartite PA/FP59 toxin, synthetic inhibitors of MMPs are likely to increase the therapeutic anti-cancer effect of anthrax toxin, unique role of furin in the activation of protective antigen markers
medicine
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MT1-MMP proteolysis of T cell CD44 regulates adhesion and subsequent transmigration and homing of T cells into the pancreas, inhibition of T cell MT1-MMP is key to delaying the onset of diabetes
medicine
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some mercaptosulfide inhibitors effectively inhibit activation of proMMP-2 by endogenous MT1-MMP produced by HT1080 human fibrosarcoma cells, block fibronectin degradation by prostate cancer LNCaP cells stably transfected with MT1-MPP
medicine
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MT1-MMP is involved in keratinocyte growth factor receptor expression and epithelial cell proliferation after acute airway injury
medicine
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therapeutic target in angiogenesis-related disease
medicine
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considering the important role of apolipoproteinE for lipid metabolism and atherosclerosis protection, MMP-14 might play an essential role for the development of hyperlipidemia and atherosclerosis as a result of degradation of apolipoprotein E
medicine
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the relationship between serum MT1-MMP and bone mineral density as well as bone metabolic markers in 206 Chinese postmenopausal women aged 43-80 years is investigated by Western analysis and ELISA. Multiple linear stepwise regression analysis shows that MT1-MMP is not a determinant factor for bone mineral density. Significant positive correlations between MT1-MMP and serum alkaline phosphatase, N-telopeptides of type I collagen are found, and remain significant after adjustment for age and body-mass index. Moreover, serum MT1-MMP, BAP, and NTX decreased in response to alendronate therapy MT1-MMP and bone turnover markers are correlated, and serum MT1-MMP levels may rise with increase in bone turnover
additional information
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association of MT1-MMP with different membrane subdomains may be crucial in the control of its different activities like cell migration, invasion or MT1-MMP-dependent signaling pathways
additional information
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degradomics method that efficiently identifies substrates of MMP-14
additional information
glycolysation of MT1-MMP may protect against autolysis and thus stabilize ative MT1-MMP
additional information
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glycolysation of MT1-MMP may protect against autolysis and thus stabilize ative MT1-MMP
additional information
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MMP-2 and MT1-MMP are cooperative dynamic components of a cell surface proteolytic axis involved in regulating the cellular signaling environment and pericellular collagen homeostasis