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 (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.23 - matrilysin
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
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matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
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?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
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?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
membrane-bound, biotinylated Kunitz-type inhibitor HAI-1, cell-bound MMP-7 cleaves HAI-1 mainly between Gly451 and Leu452 and thereby releases the extracellular region as soluble HAI-1 (sHAI-1, comprising amino acids 141-249). The peptide bonds corresponding to Gly375-Phe376 and Glu378-Leu379 in HAI-1 are slightly susceptible to MMP-7 cleavage
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?
IGFBP-3 + H2O
?
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i.e. insulin-like growth factor binding protein 3, proteolysis by enzyme plays a crucial role in regulating IGF-I bioavailability, thereby promoting cell survival
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?
insulin-like growth factor binding protein-2 + H2O
?
MMP-7 generates IGF-IIand triggers its matricine action by degradation of the IGF-II/IGFBP-2 complex binding to heparan sulfate proteoglycan in the extracellular matrix, MMP-7 induces phosphorylation of the insulin-like growth factor type-1 receptor in colon cancer cells involving IGF-II but not IGFBP-2, overview
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?
insulin-like growth factor binding protein-5 + H2O
?
in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
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?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
i.e. LN5, composed of alpha3, beta3,and gamma2 chains, is an important component of epithelial basement membranes where it induces firm adhesion and hemidesmosome formation, LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, MMP7-processed LN5 significantly enhances cell motility, overview
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?
perlecan + H2O
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i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
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?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
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i.e. procryptdins
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?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
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i.e. pro-human neutrophil peptide-1, in a cell-based assay system
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?
syndecan-2 + H2O
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MMP-7 cleaves the N-terminal Leu149 residue in the extracellular domain of syndecan-2 to a product of about 45 kDa, MALDI-TOF MS analysis, overview
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?
Fibronectin + H2O
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also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
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?
N-cadherin + H2O
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recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
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?
N-cadherin + H2O
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recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
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?
N-cadherin + H2O
?
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recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
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?
Notch-1 + H2O
?
MMP-7 interacts with the Notch pathway and is required for Notch activation, which leads to dedifferentiation of acinar cells to the nestin-positive transitional cell and further into duct-like epithelia. Besides being necessary for acinar transdifferentiation, it MMP-7 activity is sufficient to induce the process, overview
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?
Notch-1 + H2O
?
MMP-7 interacts with the Notch pathway and is required for Notch activation, which leads to dedifferentiation of acinar cells to the nestin-positive transitional cell and further into duct-like epithelia. Besides being necessary for acinar transdifferentiation, it MMP-7 activity is sufficient to induce the process, overview
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?
additional information
?
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enzyme could play a role in inflammatory tissue damage by proteolytically inactivating alpha1PI
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?
additional information
?
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enzyme may play a role in degradation of extracellular matrix macromolecules in concert with matrix metalloproteinase-1, metalloproteinase-3, and metalloproteinase-9 under pathological conditions
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?
additional information
?
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enzyme in mesangial cells may contribute to the progression of injury during glomerular inflammatory states
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?
additional information
?
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enzyme is believed to take part in processes involving physiological and pathological degradations, such as development, differentiation, tissue morphogenesis, wound healing, ovulation, rheumatoid arthritis, and tumor invasion
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?
additional information
?
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releases TNFalphaand Fas-L from the cell surface, after which they modulate macrophage migration and cell apoptosis
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?
additional information
?
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enzyme influences the morphology of mature dendritic spines, and hence synaptic stability. In hippocampal neuron cultures, enzyme induces the transformation of mature, short mushroom-shaped spines into long, thin filopodia accompanied by dramaitc redistribution of F-actin from spine heads into thick, rope-like structures in the dendritic shaft
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?
additional information
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enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
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?
additional information
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correlation of matrilysin expression with disease severity in melanomas, the survival rate of matrilysin-positive patients is about 4fold higher compared to matrilysin-negative patients, overview
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?
additional information
?
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correlation of matrilysin expression with disease severity in melanomas, the survival rate of matrilysin-positive patients is about 4fold higher compared to matrilysin-negative patients, overview
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?
additional information
?
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expression of MMP-7 correlates with the malignant potential of various tumors and with patient survival, it influences tumor progression by regulating invasion and angiogenesis, overview
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?
additional information
?
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expression of MMP-7 correlates with the malignant potential of various tumors and with patient survival, it influences tumor progression by regulating invasion and angiogenesis, overview
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?
additional information
?
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matrilysin-1 modulates crucial biological events by processing many epithelial cell surface-associated effectors, MMP-7 binds to epithelial and Ishikawa cells via cholesterol sulfate, protamine, or heparin, cell binding mechanism, MMP-7 can directly interact with the cells, without proMMP-7 having to bind first to the cell surface for local activation, overview
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?
additional information
?
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matrilysin-1 modulates crucial biological events by processing many epithelial cell surface-associated effectors, MMP-7 binds to epithelial and Ishikawa cells via cholesterol sulfate, protamine, or heparin, cell binding mechanism, MMP-7 can directly interact with the cells, without proMMP-7 having to bind first to the cell surface for local activation, overview
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?
additional information
?
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matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
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?
additional information
?
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MMP-7 alters the structure and function of presynaptic terminals without affecting neuronal survival, it induces long-lasting inhibition of synaptic vesicular recycling in rat neurons, chronic application results in synaptic atrophy, overview
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?
additional information
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MMP-7 content is elevated in tumors copared to healthy mucosa
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?
additional information
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MMP-7 content is elevated in tumors copared to healthy mucosa
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?
additional information
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MMP-7 elicits endothelial tube formation, which is abrogated by anti-VEGF antibody or connective tissue growth factor, cancer cell MMP-7 regulates the VEGF activity in colorectal tissue and VEGF angiogenic switch of fibroblasts, overview, suppression of MMP-7 in Capan-1 cells abrogates the tumor angiogenic activity of VA-13 fibroblasts, which is restored by suppression of CTGF in VA-13 fibroblasts
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?
additional information
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MMP-7 elicits endothelial tube formation, which is abrogated by anti-VEGF antibody or connective tissue growth factor, cancer cell MMP-7 regulates the VEGF activity in colorectal tissue and VEGF angiogenic switch of fibroblasts, overview, suppression of MMP-7 in Capan-1 cells abrogates the tumor angiogenic activity of VA-13 fibroblasts, which is restored by suppression of CTGF in VA-13 fibroblasts
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?
additional information
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MMP-7 is a strong proteolytic factor secreted from the cancer cell itself and it induces tumor angiogenesis, MMP-7 plays important roles in colon cancer invasion
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?
additional information
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MMP-7 is a strong proteolytic factor secreted from the cancer cell itself and it induces tumor angiogenesis, MMP-7 plays important roles in colon cancer invasion
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?
additional information
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MMP-7 is involved in signaling between epithelial cells and a key stromal cell type, the myofibroblast, via insulin-like growth factor binding protein-5 cleavage and IGF-II release, overview
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?
additional information
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MMP-7 is involved in signaling between epithelial cells and a key stromal cell type, the myofibroblast, via insulin-like growth factor binding protein-5 cleavage and IGF-II release, overview
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?
additional information
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MMP-7 plays a role in tumor angiogenesis
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?
additional information
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MMP-7 plays an important role in the development and progression of renal cancer
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?
additional information
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MMP7 plays an essential role in cancer, innate immunity, and in inflammatory disorders
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?
additional information
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the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
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additional information
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the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
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?
additional information
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the expression of MMP-7 in gliomas is not related to the invasive behaviour
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?
additional information
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the expression of MMP-7 in gliomas is not related to the invasive behaviour
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?
additional information
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chronic exposure to crescenting level of exogenous matrilysin does not significantly alter the growth rates of A-549 cells. A certain range of matrilysin might protect tumor cells from cisplatin-mediated death. The underlying mechanism may be due to the Bcl-2 overexpression and imbalance in the ratio of Bcl-2/Bax
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?
additional information
?
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treatment with matrilysin inhibits cell growth in a dose- and time-dependent manner by arresting in G0/G1 phase of the cell cycle and inducing apoptosis on A-549 cells. Although it directly promoted apoptosis at high concentrations, a certain range of matrilysin might protect tumor cells from FasL-mediated death. The mechanism may be due to the imbalance in the susceptibility of surface membrane-bound Fas receptor and ligand to proteolysis activity of matrilysin
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?
additional information
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matrilysins proteolyze a number of extracellular matrix/basement membrane components, including type IV collagens and proteoglycans
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?
additional information
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matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
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?
additional information
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matrix metalloproteinases are zinc-dependent neutral endopeptidases
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?
additional information
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MMP-7 interacts with insulin-like growth factor binding protein 5, inhibitor of metalloproteinase-3, fibronectin 1, and TFPI
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?
additional information
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MMP-7 is capable of degrading many extracellular matrix proteins and cellular adhesions
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?
additional information
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MMP-7 participates in activation other members of the MMP family
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?
additional information
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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, MMP-7 causes extracellular shedding of syndecan-2, overview
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?
additional information
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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, MMP-7 causes extracellular shedding of syndecan-2, overview
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?
additional information
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MMP-7 and syndecan-2 interaction analysis, mutational and NMR spectrometric analysis, overview. Interaction between the extracellular domain of syndecan-2 and the pro-domain of MMP-7
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?
additional information
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apart from its activity against extracellular matrix, the enzyme provides a mechanism for the regulation of leukocyte elastase activity through its capacity to degrade alpha1-antitrypsin
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?
additional information
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potentially important role of the enzyme in disruption of basement membranes by tumor or inflammatory cells
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?
additional information
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matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
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?
additional information
?
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matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
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?
additional information
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MMP-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction, MMP-7 is implicated in post-MI remodeling, overview
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?
additional information
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MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
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?
additional information
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MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
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additional information
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MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, enzyme-deficient mice show a much lower mortality rate compared to wild-type mice, overview
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?
additional information
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MMP-7 cleaves E-cadherin from lung epithelium
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additional information
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MMP-7 cleaves E-cadherin from lung epithelium
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additional information
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matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
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?
additional information
?
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MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
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?
additional information
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MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, enzyme-deficient mice show a much lower mortality rate compared to wild-type mice, overview
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?
additional information
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the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
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