3.4.24.23: matrilysin
This is an abbreviated version!
For detailed information about matrilysin, go to the full flat file.
Word Map on EC 3.4.24.23
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3.4.24.23
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metalloproteinases
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mmp-2
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metastasis
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timp-1
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colorectal
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fibrosis
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collagen
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endothelial
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node
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gelatinase
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e-cadherin
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clinicopathological
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zymography
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interstitial
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gastric
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epithelium
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tumour
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adenocarcinoma
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pulmonary
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basement
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prostate
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invasiveness
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tumorigenesis
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beta-catenin
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gelatin
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carcinogenesis
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resect
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mt1-mmp
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cyclin
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c-myc
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adenoma
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plasminogen
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transwell
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osteopontin
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metalloelastase
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stromelysin-1
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laminin-5
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hemopexin-like
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pharmacology
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upa
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drug development
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alpha-defensins
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collagenase-3
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analysis
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medicine
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diagnostics
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gelatinolytic
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matrix-degrading
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paneth
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membrane-type
- 3.4.24.23
- metalloproteinases
- mmp-2
- metastasis
- timp-1
- colorectal
- fibrosis
- collagen
- endothelial
- node
- gelatinase
- e-cadherin
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clinicopathological
-
zymography
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interstitial
- gastric
- epithelium
- tumour
- adenocarcinoma
- pulmonary
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basement
- prostate
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invasiveness
- tumorigenesis
- beta-catenin
- gelatin
- carcinogenesis
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resect
- mt1-mmp
- cyclin
- c-myc
- adenoma
- plasminogen
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transwell
- osteopontin
- metalloelastase
- stromelysin-1
- laminin-5
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hemopexin-like
- pharmacology
- upa
- drug development
- alpha-defensins
- collagenase-3
- analysis
- medicine
- diagnostics
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gelatinolytic
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matrix-degrading
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paneth
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membrane-type
Reaction
Cleavage of Ala14-/-Leu and Tyr16-/-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I) =
Synonyms
cyclic matrix metalloproteinase, human matrix metalloproteinase 7, matrilysin, matrilysin 1, matrilysin-1, Matrin, matrix metallopeptidase 7, matrix metalloprotease-7, Matrix metalloproteinase 7, Matrix metalloproteinase pump 1, Matrix metalloproteinase-7, matrix-metalloproteinase-7, metalloproteinase-7, MMP, MMP 7, MMP-7, MMP7, More, Proteinase, metallo-, pump-1, Proteinase, PUMP-1, PUMP, PUMP-1, Pump-1 protease, Putative (or punctuated) metalloproteinase-1, Putative metalloproteinase, Uterine metalloendopeptidase, Uterine metalloproteinase
ECTree
3.4.24.23 matrilysinAdvanced search results
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results (Activating Compound
Activating Compound on EC 3.4.24.23 - matrilysin
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Brij-35
activates MMP-7 in a broad concentration range, but inhibits at high concentration
Cholesterol sulfate
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selectively alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin. Degradation of laminin-332 (laminin-5) catalyzed by MMP-7 is accelerated dramatically in the presence of cholesterol sulfate, whereas the sulfated lipid inhibits the degradation of casein catalyzed by the protease. Cholesterol sulfate facilitates the proteolyses by cross-linking MMP-7 to its substrates, mechanism, overview
Fas ligand
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treatment with Fas ligand, Fas-L, increases levels of active MMP-7 by 80%
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syndecan-2
enhances both expression and secretion of MMP-7, directly interacts with pro-MMP-7, and potentiates the enzymatic activity of pro-MMP-7 by activating its processing into the active MMP-7. Syndecan-2 functions as a docking receptor for pro-MMP-7 in colon cancer cells, overview
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heparin
porcine intestinal heparin, increases activity by decreasing the Km value, increases the enzyme's thermostability
additional information
angiogenesis and apoptosis do not influence MMP-7 expression in lung cancer cells, overview
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additional information
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angiogenesis and apoptosis do not influence MMP-7 expression in lung cancer cells, overview
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additional information
binding of matrilysin-1 to epithelial cells via cholesterol sulfate, protamine or heparin promotes its activity and renders the enzyme resistant to TIMP-2, overview
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additional information
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binding of matrilysin-1 to epithelial cells via cholesterol sulfate, protamine or heparin promotes its activity and renders the enzyme resistant to TIMP-2, overview
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additional information
estrogen stimulates activation of the pro-MMP-7 intracellularly in the Golgi apparatus and augments secretion of the activated MMP-7 form, steady-state levels of MMP-7 mRNA and protein are not affected by estrogen, monensin, but not tunicamycin and brefeldin-A, blocks estrogen effects, overview, estrogen increases co-immunoreactivity of MMP-7 with synaptosomal-associated protein of 25 kDa in apical membranes, bafilomycin A1 inhibits activation of MMP-7
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additional information
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estrogen stimulates activation of the pro-MMP-7 intracellularly in the Golgi apparatus and augments secretion of the activated MMP-7 form, steady-state levels of MMP-7 mRNA and protein are not affected by estrogen, monensin, but not tunicamycin and brefeldin-A, blocks estrogen effects, overview, estrogen increases co-immunoreactivity of MMP-7 with synaptosomal-associated protein of 25 kDa in apical membranes, bafilomycin A1 inhibits activation of MMP-7
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additional information
infections with Helicobacter pylori increases MMP-7 expression in the stomach epithelium, overview
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additional information
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infections with Helicobacter pylori increases MMP-7 expression in the stomach epithelium, overview
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additional information
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cholesterol, dehydroepiandrosterone sulfate, and heparin do not affect MMP-7-catalyzed degradations of fibronactin and laminin-332
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additional information
the enzyme bound to cell surface sulfatide or cholesterol sulfate cleaves specific cell surface proteins and releases similar fragments, whereas the cleavage is not stimulated by cell surface cardiolipin-bound enzyme
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additional information
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, overview
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additional information
enzyme expression is upregulated in kidneys that are MHC-incompatible allografts but are tolerated through induction by the administration of anti-donor class II antibodies, as part of the pivotal non-canonical wingless-type signaling pathway, overview
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