3.4.24.80: membrane-type matrix metalloproteinase-1
This is an abbreviated version!
For detailed information about membrane-type matrix metalloproteinase-1, go to the full flat file.
Word Map on EC 3.4.24.80
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3.4.24.80
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metalloproteinases
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mmp-2
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metastasis
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endothelial
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zymography
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angiogenesis
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gelatin
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gelatinase
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timps
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prommp-2
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mesenchymal
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invasiveness
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vessel
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basement
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integrins
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angiogenic
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fibrosarcoma
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matrigel
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transwell
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furin
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fibronectin
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zymogen
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gelatinolytic
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progelatinase
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ectodomain
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invadopodia
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hemopexin
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alphavbeta3
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proproteins
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mt-mmps
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collagen-rich
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anti-invasive
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matrix-degrading
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collagenolytic
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pro-matrix
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emmprin
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hemopexin-like
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membrane-tethered
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proenzyme
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convertase
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invasion-promoting
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analysis
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diagnostics
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cona-induced
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medicine
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drug development
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endoglin
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reck
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podosomes
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mmp-dependent
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cortactin
- 3.4.24.80
- metalloproteinases
- mmp-2
- metastasis
- endothelial
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zymography
- angiogenesis
- gelatin
- gelatinase
- timps
- prommp-2
- mesenchymal
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invasiveness
- vessel
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basement
- integrins
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angiogenic
- fibrosarcoma
- matrigel
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transwell
- furin
- fibronectin
- zymogen
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gelatinolytic
- progelatinase
- ectodomain
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invadopodia
- hemopexin
- alphavbeta3
- proproteins
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mt-mmps
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collagen-rich
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anti-invasive
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matrix-degrading
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collagenolytic
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pro-matrix
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emmprin
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hemopexin-like
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membrane-tethered
- proenzyme
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convertase
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invasion-promoting
- analysis
- diagnostics
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cona-induced
- medicine
- drug development
- endoglin
- reck
- podosomes
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mmp-dependent
- cortactin
Reaction
endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-/-Leu. Other bonds hydrolysed include Gly35-/-Ile in the propeptide of collagenase 3, and Asn341-/-Phe, Asp441-/-Leu and Gln354-/-Thr in the aggrecan interglobular domain =
Synonyms
ectMMP-14, gelatinase A, interstitial MT1-MMP, matrix metalloprotease 14, matrix metalloproteinase 14, matrix metalloproteinase MT 1, matrix metalloproteinase MT-MMP-1, matrix metalloproteinase MT1-MMP, matrix metalloproteinase-14, membrane type 1 matrix, membrane type 1 matrix metalloproteinase, membrane type 1 MMP, membrane type 1-matrix metalloproteinase, membrane type 1-MMP, membrane type I MMP, membrane type matrix metalloproteinase, membrane type MMP-1, membrane type MT1-MMP, membrane type-1 matrix metalloprotease, membrane type-1 matrix metalloprotease 1, membrane type-1 matrix metalloproteinase, membrane type-1 MMP, membrane type-I matrix metalloproteinase, membrane type-I MMP, membrane-anchored matrix metalloproteinase 14, membrane-type 1 matrix metalloproteinase, membrane-type 1 matrix metalloproteinase 1, membrane-type 1 MMP, membrane-type 1-matrix metalloproteinase, membrane-type I matrix metalloproteinase, membrane-type matrix metalloproteinase MT1-MMP, membrane-type matrix metalloproteinase-1, membrane-type metalloproteinase MT1-MMP, membrane-type MMP, metalloproteinase, MMP-14, MMP-2, MMP-8, MMP14, mmp14a, mmp14b, More, MT-MMP-1, MT-MMP1, MT1-MMP, MT1-MMP/MMP-14, MT1-MPP, MTI-MMP, pericellular collagenase, proteinase, matrix metallo-, sMT1-MMP
ECTree
3.4.24.80 membrane-type matrix metalloproteinase-1Advanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.24.80 - membrane-type matrix metalloproteinase-1
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(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
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(2R)-4-(acetylamino)-2-[(biphenyl-4-ylsulfonyl)amino]-N-hydroxybutanamide
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1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
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4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
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4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
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4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
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alpha1-PDX
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completely abats MT1-MMP-induced gelatin degradation by A375 cells
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alpha1-PIMT1
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alpha1-proteinase inhibitor-based inhibitor by incorporating the MT1-MMP propeptide sequence into the alpha1-PI reactive-site loop, inhibits proMT1-MMP activation
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alpha1-PIPDX
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alpha1-proteinase inhibitor-based inhibitor with furin consensus cleavage sequence inserted into the reactive-site loop, inhibits proMT1-MMP activation
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anti-membrane-type 1-MMP antibody
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antibodies LEM-1 and LEM-2 inhibit endothelial cell invasion in a dose dependent manner
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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
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decanoyl-Arg-Val-Lys-Arg-chloromethylketone
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furin inhibitor repressing activation of MMP-2
genistein
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markedly suppresses the VEGF mRNA induction in MT clones without affecting the VEGF expression in control clones
hemopexin
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soluble hemopexin domain inhibits collagenolysis by preventing dimerization
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MT1-MMP siRNA
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collagen degrading activity is completely lost when MT1-MMP expressing cells are transfected with 100 nM MT1-MMP siRNA
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N,N'-bis(4-[[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]amino]-4-oxobutyl)benzene-1,3-dicarboxamide
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N,N'-bis[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]benzene-1,3-dicarboxamide
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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
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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
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N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
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N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
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N4-hydroxyamino-2-isobutyl-3-(thienylthiomethyl) succinyl]-L-phenylalamine-methylamide
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Rac1(N17Rac)
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coexpression wit MT1-MMP cDNAs leads to complete inhibition of migration
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RO28-2653
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reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
TIMP-1
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TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
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TIMP-1 mutant forms
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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
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tissue inhibitor of matrix metalloproteinase-1
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i.e. TIMP-1, recombinant, human
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BB94
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reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
DX-2400
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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
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DX-2400
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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
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DX-2400
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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
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DX-2400
enzyme activity is inhibited with 65.8 nM or 658 nM of the enzyme function-blocking antibody DX-2400
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DX-2400
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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
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furin
concanavalin A-induced pro-matrix metalloproteinase 2 activation is inhibited in human uterine cervical fibroblasts, but not in rabbit dermal fibroblasts
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furin
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concanavalin A-induced pro-matrix metalloproteinase 2 activation is inhibited in human uterine cervical fibroblasts, but not in rabbit dermal fibroblasts
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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
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fully blocks proteolysis of PA83 by MT1-MMP, inhibits MT1-MMP-dependent activation of proMMP-2
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
marimastat
inhibits production of 18 kDa fragment during autocatalytic processing
TIMP-2
inhibits production of 18 kDa fragment during autocatalytic processing
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TIMP-2
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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
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TIMP-2
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inhibitory interaction with the catalytically competent MT1-MMP active site, prevents autolytic processing
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TIMP-2
under in vivo conditions primary inhibitor of MT1-MMP, increases endocytosis of wild type MT1-MMP
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TIMP-3
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during ischemia, loss of inhibitory control leading to increased MT1-MMP activity
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TIMP-4
inhibits production of 18 kDa fragment during autocatalytic processing
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TIMP-4
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during ischemia, loss of inhibitory control leading to increased MT1-MMP activity
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tissue inhibitor of MMP-2
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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
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tissue inhibitor of MMP-2
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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
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additional information
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mercaptosulfide inhibitors, interacting exclusively at the enzyme active site, strong stereoselectivity at the P1' and zinc-binding groups, competitive and reverse inhibition
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additional information
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migration of HT1080 cells on type I collagen not supressed by TIMP-1
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additional information
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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
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additional information
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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
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additional information
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not inhibited by tissue inhibitor of metalloproteinases-1
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additional information
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not inhibited by tissue inhibitor of metalloproteinase-1
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additional information
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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
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additional information
design, synthesis, and biological evaluation of bifunctional inhibitors of membrane type 1 matrix metalloproteinase (MT1-MMP), overview
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additional information
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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
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additional information
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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
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