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Information on EC 3.4.24.23 - matrilysin and Organism(s) Mus musculus and UniProt Accession Q10738
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- 3.4.24.23
- metalloproteinases
- mmp-2
- metastasis
- timp-1
- colorectal
- fibrosis
- collagen
- endothelial
- node
- gelatinase
- e-cadherin
-
clinicopathological
-
zymography
-
interstitial
- gastric
- epithelium
- tumour
- adenocarcinoma
- pulmonary
-
basement
- prostate
-
invasiveness
- tumorigenesis
- beta-catenin
- gelatin
- carcinogenesis
-
resect
- mt1-mmp
- cyclin
- c-myc
- adenoma
- plasminogen
-
transwell
- osteopontin
- metalloelastase
- stromelysin-1
- laminin-5
-
hemopexin-like
- pharmacology
- upa
- drug development
- alpha-defensins
- collagenase-3
- analysis
- medicine
- diagnostics
-
gelatinolytic
-
matrix-degrading
-
paneth
-
membrane-type
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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
mmp-7, matrilysin, matrix metalloproteinase-7, matrix metalloproteinase 7, matrin, pump-1, matrix metallopeptidase 7, metalloproteinase-7, matrilysin-1, mmp 7, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Matrin
-
-
-
-
Matrix metalloproteinase 7
Matrix metalloproteinase pump 1
-
-
-
-
Matrix metalloproteinase-7
MMP
-
-
-
-
MMP 7
-
-
-
-
Proteinase, metallo-, pump-1
-
-
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Proteinase, PUMP-1
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-
-
-
PUMP
-
-
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Pump-1 protease
-
-
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-
Putative (or punctuated) metalloproteinase-1
-
-
-
-
Putative metalloproteinase
-
-
-
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Uterine metalloendopeptidase
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-
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Uterine metalloproteinase
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-
-
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Matrix metalloproteinase 7
-
-
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Matrix metalloproteinase-7
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
141256-52-2
-
SUBSTRATE
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
PB-M7vis + H2O
?
-
fluorogenic substrate based on a polyamino amino dendrimer core of 14.2 kDa covalently coupled with an fluorescein-labeled peptide fluorescein(aminohexanoic acid)RPLALWRS(aminohexanoic acid)Cand with tetramethylrhodamine
-
-
?
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
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
MMP-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction, MMP-7 is implicated in post-MI remodeling, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
MMP-7 is an endopeptidase that degrades a broad range of substrates
-
-
?
additional information
?
-
-
MMP-7 cleaves E-cadherin from lung epithelium
-
-
?
additional information
?
-
-
MMP-7 assay using DQ-gelatin fluorescent substrate
-
-
?
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
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
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
MMP-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction, MMP-7 is implicated in post-MI remodeling, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
MMP-7 cleaves E-cadherin from lung epithelium
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tissue inhibitor of metalloproteinase
i.e. TIMP-1. TIMP-1 and matrilysin co-localize and co-immunoprecipitate in wounded primary airway epithelial cultures. TIMP-1-deficient cultures migrate faster, and epithelial cells spread to a greater extent compared with wild-type cultures. TIMP-1 also inhibits matrilysin-mediated cell migration and spreading in vitro. In vivo, TIMP-1 deficiency enhances airway re-epithelialization after naphthalene injury. TIMP-1 and matrilysin co-localize in airway epithelial cells adjacent to the wound edge
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BB-94
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[4-(N-hydroxyamino)-(2R)-isobutyl-(3S)-(thienylthiomethyl)-succinyl]-L-Phe-N-methylamine
sulindac
-
in sulindac-treated ApcMin/+ mice, a genetic model of human familial adenomatous polyposis, collagen genes, viz. Col1a2, Col5a2, Col6a2, and Col6a3, are upregulated, and matrilysin matrix metalloproteases-7 is downregulated. Mmp7 is found in hot spot areas within the tumors of ApcMin/+ mice treated with the vehicle, but is greatly diminished in those mice treated with sulindac
additional information
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
primary airway epithelial cell air-liquid interface culture. Tissue inhibitor of metalloproteinase TIMP-1 and matrilysin co-localize and co-immunoprecipitate in wounded primary airway epithelial cultures. TIMP-1-deficient cultures migrate faster, and epithelial cells spread to a greater extent compared with wild-type cultures. TIMP-1 also inhibits matrilysin-mediated cell migration and spreading in vitro. In vivo, TIMP-1 deficiency enhances airway re-epithelialization after naphthalene injury. TIMP-1 and matrilysin co-localize in airway epithelial cells adjacent to the wound edge
MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
additional information
-
pulmonary CD103+ dendritic cells are significantly increased in bleomycin-injured wild-type compared with Mmp7-/- mice, and CD103+ leukocytes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
MMP-7 is one of the smallest MMPs, and it is synthesized as an inactive zymogen
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
MMP-7 is a proteolytic enzyme that can modify the intestinal microbial replicative niche as well as affect tumorigenesis, and Helicobacter pylori stimulates expression of MMP-7 in gastric epithelial cells in vitro, that may serve to protect the gastric mucosa from pathophysiologic processes which promote carcinogenesis. Enhanced gastritis in Helicobacter pyloriinfected mmp-7-knockout mice is strongly linked to accelerated epithelial cellular turnover. However, more severe inflammation and heightened proliferation and apoptosis are not dependent on MMP-7-mediated bacterial eradication
physiological function
additional information
-
MMP-7 expression regulation, high expression of ADAM-12 observed under sustained agonist stimulation acts in a negative feedback loop to inhibit MMP-7 transcription, overview
malfunction
MMP-7-deficient mice show educed beta-catenin activation after lung injury or bleomycin treatment
malfunction
MMP-7 knockout mice experience higher mortality, elevated serum creatinine, and more severe histologic lesions after ischemic or toxic insults. Tubular apoptosis and interstitial inflammation are more prominent in MMP-7 knockout kidneys, accompanied by increased expression of FasL and other components of the extrinsic apoptotic pathway, as well as increased expression of pro-inflammatory chemokines. Ablation of MMP-7 promotes tubular cell apoptosis after acute kidney injury (AKI) augmenting renal inflammation, phenotype, overview. Exogenous MMP-7 ameliorates kidney injury in MMP-7 knockout mice after ischemia/reperfusion, mechanism underlying renal protection of MMP-7 in AKI. MMP-7 augmentes c-fos and PCNA expression induced by mitogens-rich serum in renal tubules ex vivo
physiological function
the enzyme functions to degrade extracellular matrix and other pericellular substrates including the adherens junction protein E-cadherin to promote wound healing and tissue remodeling. Matrilysin's catalytic activity regulates beta-catenin localization and signaling activation in lung epithelial cells, the enzyme activity releases beta-catenin from the cell membrane after which it is degraded in the cytosol. Matrilysin activity also increases beta-catenin translocation in the presence of a Wnt activating signal
physiological function
the primary function of MMP-7 is to break down the extracellular matrix by digesting casein, gelatins, fibronectin, and proteoglycan. MMP-7 is also capable of cleaving other substrates and plays a role in E-cadherin ectodomain shedding, tumor necrosis factor-alpha (TNF-alpha) release, and activation of other proteinases. Exogenous MMP-7 ameliorates kidney injury in MMP-7 knockout mice after ischemia/reperfusion. In vitro, MMP-7 protects tubular epithelial cells against apoptosis by directly degrading FasL. In isolated tubules ex vivo, MMP-7 promotes cell proliferation by degrading E-cadherin and thereby liberating beta-catenin, priming renal tubules for regeneration. Mechanism underlying renal protection of MMP-7 in acute kidney injury (AKI), overview
physiological function
-
matrilysin regulates pulmonary influx and localization of dendritic cells that express CD103, and E-cadherin cleavage may activate CD103+ dendritic cells to limit inflammation and inhibit fibrosis, overview. Matrilysin effects on CD103-E-cadherin interactions in lung injury, matrilysin expression is increased in lung injury, and it cleaves E-cadherin from injured lung epithelium, overview. Matrilysin regulates pulmonary neutrophil clearance in cronic lung injury, overview
physiological function
-
MMP-7 controls the transcription of the disintegrin and metalloproteinase-12, ADAM-12, the major metalloproteinase implicated in cardiac hypertrophy. Matrix metalloproteinase-7 and ADAM-12 form a novel signaling axis in a variety of cardiovascular processes, including hypertension and hypertrophy, overview. Induction of acute hypertension by vasoconstrictors, i.e. catecholamines, angiotensin II, and the nitric oxide synthase inhibitor NG-nitro-L-arginine methyl ester, require the posttranscriptional activation of vascular MMP-7. Sustained agonist stimulation regulates the development and progression of hypertension and hypertrophy processes through posttranscriptional, short-term and transcriptional, long-term mechanisms involving metalloproteinases such as MMP-7 and ADAM-12
physiological function
-
MMP-7 deletion improves survival after myocardial infarction
physiological function
-
MMP-7 mediates cleavage of N-cadherin and promotes vascular smooth muscle cell apoptosis, that can lead to thinning of the fibrous cap and plaque instability
physiological function
-
MMP7 is required for cell migration. Lung injury promotes the expression of matrix metalloproteinase-7, which is required for neutrophil recruitment and re-epithelialization. MMP7 shedding of syndecan-1 facilitates re-epithelialization by affecting alpha2beta1 integrin activation. MMP7 releases syndecan-1 restrictions on wound closure, overview
physiological function
-
role of MMP7 in colon cancer progression, overview. MMP7 is required for tumor formation, but not for the invasion or fibrosis of the colon cancer whose SMAD4-dependent TGF-beta family signaling is blocked
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MMP7_MOUSE
264
0
29755
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
activation of pro-MMP-7 by proteolytic cleavage to mature MMP-7
proteolytic modification
MMP-7 is one of the smallest MMPs, and it is synthesized as an inactive zymogen. Upon activation, the N-terminal pro-region is removed through proteolysis, which results in the final active enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of MMP-7 knockout mice, which show higher content of pathogens in the small intestine two weeks after vaginal infection with Chlamydia trachomatis mouse pneumonitis as compared to wild-type C57BL/6 mice, because MMP-7 KO mice are deficient in active intestinal alpha-defensins, which play a role in regulating colonization of the gastrointestinal tract by Chlamydia, overview
additional information
-
construction of MMP-7 knockout mice, which show higher content of pathogens in the small intestine two weeks after vaginal infection with Chlamydia trachomatis mouse pneumonitis as compared to wild-type C57BL/6 mice, because MMP-7 KO mice are deficient in active intestinal alpha-defensins, which play a role in regulating colonization of the gastrointestinal tract by Chlamydia, overview
additional information
enzyme-deficient MMP7-/- mice show a lower mortality rate compared to wild-type mice in case of colon mucosal injury and inflammation, while neutrophil influx is similar in both cases, overview
additional information
MMP-7-deficient cells do not show activation of Notch-1, which can be restored by recombinant MMP-7, phenotype, overview
additional information
-
ApcMin/+ Mmp7-/- double-deficient mice demonstrate reciprocal relationships of Mmp7 expression and the levels of the collagens Col1a2, Col5a2, Col6a2, and Col6a3 in vivo
additional information
-
construction of MMP-7 null mice that show lower levels of full-length peroxiredoxin-1 and -2 and higher levels of the full-length peroxiredoxin-3, suggesting MMP-7 deletion may also indirectly regulate protein levels through nonenzymatic mechanisms. Null mice also show reduced fibronectin and tenascin-C fragment generation, which is restored by exogenous administration of MMP-7
additional information
-
introduction of an Mmp7 knockout mutation into the cis-Apc/Smad4 mutant mouse, a model of invasive colon cancer in which SMAD4-dependent TGF-beta family signaling is inactivated. Lack of MMP7 reduces the number and size of tumors in the cis-Apc/Smad4 mice
additional information
-
knockdown of MMP-7 by siRNA attenuates hypertension, inhibits ADAM-12 overexpression, and prevents cardiac hypertrophy. Resistance to acute hypertension in mice lacking active MMP-7
additional information
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is increased in epithelium by bacterial infection, inflammation, fibrosis, and in a lot of carcinomas
Helicobacter pylori stimulates expression of MMP-7 in gastric epithelial cells in vitro
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use of substrate PB-M7vis as a proteolytic beacon and optical molecular imaging contrast reagent for in vivo detection of enzyme activity
pharmacology
-
in sulindac-treated ApcMin/+ mice, a genetic model of human familial adenomatous polyposis, collagen genes, viz. Col1a2, Col5a2, Col6a2, and Col6a3, are upregulated, and matrilysin matrix metalloproteases-7 is downregulated. Mmp7 is found in hot spot areas within the tumors of ApcMin/+ mice treated with the vehicle, but is greatly diminished in those mice treated with sulindac
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McIntyre, J.O.; Fingleton, B.; Wells, K.S.; Piston, D.W.; Lynch, C.C.; Gautam, S.; Matrisian, L.M.
Development of a novel fluorogenic proteolytic beacon for in vivo detection and imaging of tumour-associated matrix metalloproteinase-7 activity
Biochem. J.
377
617-628
2004
Mus musculus
Lynch, C.C.; Vargo-Gogola, T.; Martin, M.D.; Fingleton, B.; Crawford, H.C.; Matrisian, L.M.
Matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor
Cancer Res.
67
6760-6767
2007
Homo sapiens (P09237), Mus musculus (Q10738), Mus musculus, Mus musculus C57BL/6 (Q10738)
Lindsey, M.L.; Escobar, G.P.; Mukherjee, R.; Goshorn, D.K.; Sheats, N.J.; Bruce, J.A.; Mains, I.M.; Hendrick, J.K.; Hewett, K.W.; Gourdie, R.G.; Matrisian, L.M.; Spinale, F.G.
Matrix metalloproteinase-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction
Circulation
113
2919-2928
2006
Mus musculus (Q10738)
Pal, S.; Schmidt, A.P.; Peterson, E.M.; Wilson, C.L.; de la Maza, L.M.
Role of matrix metalloproteinase-7 in the modulation of a Chlamydia trachomatis infection
Immunology
117
213-219
2006
Mus musculus (Q10738), Mus musculus, Mus musculus C57BL/6 (Q10738)
Swee, M.; Wilson, C.L.; Wang, Y.; McGuire, J.K.; Parks, W.C.
Matrix metalloproteinase-7 (matrilysin) controls neutrophil egress by generating chemokine gradients
J. Leukoc. Biol.
83
1404-1412
2008
Mus musculus (Q10738), Mus musculus C57BL/6 (Q10738)
Sawey, E.T.; Johnson, J.A.; Crawford, H.C.
Matrix metalloproteinase 7 controls pancreatic acinar cell transdifferentiation by activating the Notch signaling pathway
Proc. Natl. Acad. Sci. USA
104
19327-19332
2007
Mus musculus (Q10738), Mus musculus C57/BL6J (Q10738)
Chen, P.; McGuire, J.K.; Hackman, R.C.; Kim, K.H.; Black, R.A.; Poindexter, K.; Yan, W.; Liu, P.; Chen, A.J.; Parks, W.C.; Madtes, D.K.
Tissue inhibitor of metalloproteinase-1 moderates airway re-epithelialization by regulating matrilysin activity
Am. J. Pathol.
172
1256-1270
2008
Mus musculus (Q10738), Mus musculus
Guillen-Ahlers, H.; Buechler, S.A.; Suckow, M.A.; Castellino, F.J.; Ploplis, V.A.
Sulindac treatment alters collagen and matrilysin expression in adenomas of ApcMin/+ mice
Carcinogenesis
29
1421-1427
2008
Mus musculus
Manicone, A.M.; Huizar, I.; McGuire, J.K.
Matrilysin (matrix metalloproteinase-7) regulates anti-inflammatory and antifibrotic pulmonary dendritic cells that express CD103 (alphaEbeta7-integrin)
Am. J. Pathol.
175
2319-2331
2009
Mus musculus, Mus musculus C57BL/6
Ogden, S.R.; Noto, J.M.; Allen, S.S.; Patel, D.A.; Romero-Gallo, J.; Washington, M.K.; Fingleton, B.; Israel, D.A.; Lewis, N.D.; Wilson, K.T.; Chaturvedi, R.; Zhao, Z.; Shyr, Y.; Peek, R.M.
Matrix metalloproteinase-7 and premalignant host responses in Helicobacter pylori-infected mice
Cancer Res.
70
30-35
2010
Mus musculus, Mus musculus C57BL/6
Williams, H.; Johnson, J.L.; Jackson, C.L.; White, S.J.; George, S.J.
MMP-7 mediates cleavage of N-cadherin and promotes smooth muscle cell apoptosis
Cardiovasc. Res.
87
137-146
2010
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Wang, X.; Chow, F.L.; Oka, T.; Hao, L.; Lopez-Campistrous, A.; Kelly, S.; Cooper, S.; Odenbach, J.; Finegan, B.A.; Schulz, R.; Kassiri, Z.; Lopaschuk, G.D.; Fernandez-Patron, C.
Matrix metalloproteinase-7 and ADAM-12 (a disintegrin and metalloproteinase-12) define a signaling axis in agonist-induced hypertension and cardiac hypertrophy
Circulation
119
2480-2489
2009
Mus musculus, Rattus norvegicus
Chiao, Y.A.; Zamilpa, R.; Lopez, E.F.; Dai, Q.; Escobar, G.P.; Hakala, K.; Weintraub, S.T.; Lindsey, M.L.
In vivo matrix metalloproteinase-7 substrates identified in the left ventricle post-myocardial infarction using proteomics
J. Proteome Res.
9
2649-2657
2010
Mus musculus
Kitamura, T.; Biyajima, K.; Aoki, M.; Oshima, M.; Taketo, M.
Matrix metalloproteinase 7 is required for tumor formation, but dispensable for invasion and fibrosis in SMAD4-deficient intestinal adenocarcinomas
Lab. Invest.
89
98-105
2009
Homo sapiens, Mus musculus
Chen, P.; Abacherli, L.E.; Nadler, S.T.; Wang, Y.; Li, Q.; Parks, W.C.
MMP7 shedding of syndecan-1 facilitates re-epithelialization by affecting alpha2beta1 integrin activation
PLoS ONE
4
e6565
2009
Mus musculus
Rims, C.; McGuire, J.
Matrilysin (MMP-7) catalytic activity regulates beta-catenin localization and signaling activation in lung epithelial cells
Exp. Lung Res.
40
126-136
2014
Mus musculus (Q10738), Mus musculus C57BL/6 (Q10738)
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