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Information on EC 3.4.24.23 - matrilysin
for references in articles please use BRENDA:EC3.4.24.23
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.23 matrilysin
IUBMB Comments
Found in rat uterus; at 19 kDa, the smallest member of peptidase family M10 (interstitial collagenase family). Similar in specificity to stromelysin, but more active on azocoll
The enzyme appears in viruses and cellular organisms
- 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
Reaction Schemes
showCleavage 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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
matrilysin
matrilysin-1
Matrin
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-
-
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matrix metalloprotease-7
Matrix metalloproteinase 7
Matrix metalloproteinase pump 1
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-
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Matrix metalloproteinase-7
MMP
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-
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MMP 7
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-
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MMP-7
MMP7
Proteinase, metallo-, pump-1
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Proteinase, PUMP-1
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PUMP
Pump-1 protease
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-
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Putative (or punctuated) metalloproteinase-1
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-
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Putative metalloproteinase
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Uterine metalloendopeptidase
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Uterine metalloproteinase
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-
additional information
the enzyme belongs to the zinc-dependent endopeptidases
Matrix metalloproteinase 7
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-
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Matrix metalloproteinase 7
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Matrix metalloproteinase-7
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Matrix metalloproteinase-7
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Matrix metalloproteinase-7
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MMP-7
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638796, 649827, 651772, 651777, 651781, 651804, 652071, 652723, 706943, 707003, 707186, 707870, 707880, 707905, 707957, 707986, 708011, 708021, 708084, 708164, 708198, 708293, 708301, 708308, 708392, 708635, 708642, 708667, 708674, 708772, 709079, 709318, 709345, 709415, 709655, 709669, 709809, 710176, 710179, 710651, 710683, 710694, 717204, 717292, 717397, 717399, 717745, 717801, 718394, 754942, 755514
MMP-7
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PUMP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
141256-52-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxy-coumarin-4-yl)acetyl-Ala-Pro-Lys-2,4-dinitrophenol + H2O
?
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly + L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
Substrates: MOCAc-PLGL(Dpa)AR
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-L-Leu-[N3-2,4-dinitrophenyl-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
Substrates: MOCAc-PLGL(Dpa)AR
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
(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
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser + H2O
?
-
Substrates: optimized fluorogenic substrate
Products: -
Products: -
?
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg + H2O
?
-
Substrates: -
Products: -
Products: -
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
-
Substrates: -
Products: -
Products: -
?
7-amino-4-methylcoumaryl-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
7-methoxycoumarin-4acetyl-PLG + ?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
?
-
Substrates: -
Products: -
Products: -
?
alpha1-antitrypsin + H2O
?
-
Substrates: a single cleavage at the Phe352-Leu353 peptide bond, a locus within active-site loop produces 2 fragments of approximately 50000 MW and 4000 MW
Products: -
Products: -
?
alpha1PI + H2O
?
-
Substrates: protein, inhibitor of elastase, inactivation by cleavage of Pro357-Met358 peptide bond of its reactive centre
Products: -
Products: -
?
annexin II + H2O
?
-
Substrates: treatment of human colon cancer cell lines with active matrilysin releases a 35 kDa annexin II form, which lacked its N-terminal region, into the culture supernatant. The release of the 35 kDa annexin II by matrilysin is significantly enhanced in the presence of serotonin or heparin. Matrilysin hydrolyzes annexin II at the Lys9-Leu10 bond, thus dividing the protein into an N-terminal nonapeptide and the C-terminal 35 kDa fragment. The nonapeptide generated by matrilysin treatment might be anchored to the cell membrane, possibly by binding to intact annexin II, and interact with tissue-type plasminogen activator via its C-terminal lysine
Products: -
Products: -
?
C-type lectin domain family 3 member A + H2O
?
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Substrates: i.e. CLEC3A. MMP-7 cleaves the 20 kDa CLEC3A protein, dividing it to a 15 kDa COOH-terminal fragment and an NH2-terminal fragment with the basic sequence. The 15 kDa fragment no longer has heparin-binding activity. Treatment of the CLEC3A-expressing cells with MMP-7 releases the 15 kDa CLEC3A into the culture supernatant. The native 20 kDa CLEC3A promotes cell adhesion to laminin-332 and fibronectin substrates, but this activity is abrogated by the cleavage by MMP-7
Products: -
Products: -
?
Cy5.5-M7 peptide + H2O
?
-
Substrates: method development for in vivo detection and quantitation of MMP7 activity, in tumors induces in nude mice by injection of human SW480 colon cancer cells, using a specific near-infrared polymer-based proteolytic beacon, PB-M7NIR. PB-M7NIR is a pegylated polyamidoamine PAMAM-Generation 4 dendrimer core covalently coupled to a Cy5.5 labeled peptide representing a selective substrate that monitors MMP7 activity and AF750 as an internal reference to monitor relative substrate concentration. In vivo imaging of tumors expressing MMP7 has a median S/R ratio 2.2-fold higher than a bilateral control tumor, quantitative detection method with ability of substrate PB-M7NIR to effectively localize and assess MMP7 activity in the tumor microenvironment, development and evaluation, overview
Products: -
Products: -
?
dansyl-PLALWAR + H2O
?
-
Substrates: synthetic fluorescent peptide
Products: -
Products: -
?
Dinitrophenyl-Pro-Leu-Gly-Ile-Ala-Gly-Pro-D-Arg + H2O
?
-
Substrates: -
Products: -
Products: -
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
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Substrates: matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
Products: -
Products: -
?
entactin + H2O
peptide fragment ranging from 29000 to 115000 MW
-
Substrates: basement membrane protein which bridges laminin and type IV collagen, enzyme produces multiple but distict cleavages in entactin resulting in peptide fragments ranging from 29000 to 115000 MW, cleavage sites: Glu34-Leu35, Gly275-Leu276, Ala637-Leu638, Cys747-Ile748
Products: -
Products: -
?
fibronactin + H2O
fibronectin peptide fragments
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Substrates: -
Products: MWs of 30 to 175 kDa
Products: MWs of 30 to 175 kDa
?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
Substrates: -
Products: -
Products: -
?
Insulin B-chain + H2O
?
-
Substrates: cleavage at 2 points: Ala14-Leu15 and Tyr16-Leu17
Products: -
Products: -
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
Substrates: 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
Products: -
Products: -
?
laminin-5/laminin-332 + H2O
90 kDa beta3 chain fragment + ?
Substrates: i.e. LN5, specific proteolysis by MMP7 in the beta3 chain at Ala515-Ile516, overview
Products: -
Products: -
?
MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
MUC-1 + H2O
?
Substrates: i.e. transmembrane glycoprotein DF3/MUC-1, aberrantly overexpressed by breast and other types of carcinomas
Products: -
Products: -
?
neuropilin-1 + H2O
?
Substrates: i.e. component of the perlecan-semaphorin 3A-plexin A1-neuropilin-1 complex
Products: -
Products: -
?
Oxidized alpha1PI + H2O
?
-
Substrates: cleavage of Phe352-Leu353 bond
Products: -
Products: -
?
PB-M7vis + H2O
?
-
Substrates: 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
Products: -
Products: -
?
perlecan-semaphorin 3A-plexin A1-neuropilin-1 complex + H2O
?
Substrates: i.e. complex at the cell surface of prostate cancer cells
Products: -
Products: -
?
plexin A1 + H2O
?
Substrates: i.e. component of the perlecan-semaphorin 3A-plexin A1-neuropilin-1 complex
Products: -
Products: -
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
-
Substrates: -
Products: -
Products: -
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
-
Substrates: i.e. procryptdins
Products: -
Products: -
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
-
Substrates: -
Products: -
Products: -
?
Pro-matrix metalloproteinase 1 + H2O
?
-
Substrates: activation by specific cleavage at the Gln80-Phe81 bond
Products: -
Products: -
?
proADAM28s + H2O
ADAM28s + propeptide
-
Substrates: secreted form of a member of a disintegrin and metalloproteinase family. ProADAM28s is processed by enzyme to active 42 and 40 kDa forms lacking the propeptide
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
Substrates: MOCAc-PLGL(Dpa)AR, Lot 480429
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
Substrates: MOCAc-PLGL(Dpa)AR
Products: -
Products: -
?
casein + H2O
?
-
Substrates: non-specific substrate used in zymography
Products: -
Products: -
?
casein + H2O
?
-
Substrates: non-specific substrate used in zymography
Products: -
Products: -
?
connexin-43 + H2O
?
Substrates: cleavage site determination, overview
Products: -
Products: -
?
elastin + H2O
elastin peptides
-
Substrates: degradation
Products: in the range of 500-8000 Da
Products: in the range of 500-8000 Da
?
elastin + H2O
elastin peptides
-
Substrates: degradation. MMP-7 mainly cleaves in N- and C-terminal regions of elastin's precursor, which involves linkages in domains encoded by exons 2, 3, 5-7, 26, and 30-33. Only few cleavages occur in the central part of the precursor and no cleavages in regions in elastin that are involved in cross-linking. MMP-7 shows a strong preference for Leu in P1' and also accepts Val, Gly, and Pro at this position, whereas Ala is not preferred at P1', molecular modeling, overview. Not only the size of the amino acid residue in P1' but also the orientation of the neighboring P1 residue and, thus, the orientation of the peptide bond that is cleaved influences the cleavage preference of MMP-7, cleavage site specificity of MMP-7 in human skin elastin, overview
Products: in the range of 500-8000 Da
Products: in the range of 500-8000 Da
?
Fibronectin + H2O
?
-
Substrates: also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: digests the alpha2(I) chain of gelatin in preference to the alpha1(I) chain
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: cleaves the alpha2(I) chain of rat gelatin producing major cuts at Gly713-Ile714, Gly775-Leu776, Gly809-Ile810
Products: -
Products: -
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
Substrates: 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
Products: -
Products: -
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
Substrates: membrane-bound, biotinylated Kunitz-type inhibitor HAI-1
Products: -
Products: -
?
IGFBP-3 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
IGFBP-3 + H2O
?
-
Substrates: i.e. insulin-like growth factor binding protein 3, hydrolysis leads to four major fragments. Cleavage sites include K144-I145 and R95-L96
Products: -
Products: -
?
insulin-like growth factor binding protein-2 + H2O
?
Substrates: 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
Products: -
Products: -
?
insulin-like growth factor binding protein-2 + H2O
?
Substrates: degradation, three distinct cleavage sites
Products: -
Products: -
?
insulin-like growth factor binding protein-5 + H2O
?
Substrates: in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
Products: -
Products: -
?
insulin-like growth factor binding protein-5 + H2O
?
Substrates: -
Products: -
Products: -
?
laminin-332 + H2O
?
-
Substrates: -
Products: analysis of peptide fragment degradation products
Products: analysis of peptide fragment degradation products
?
N-cadherin + H2O
?
-
Substrates: recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
Products: -
Products: -
?
N-cadherin + H2O
?
-
Substrates: recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
Products: -
Products: -
?
N-cadherin + H2O
?
-
Substrates: recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
Products: -
Products: -
?
Notch-1 + H2O
?
Substrates: 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
Products: -
Products: -
?
Notch-1 + H2O
?
Substrates: 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
Products: -
Products: -
?
perlecan + H2O
?
Substrates: i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
Products: -
Products: -
?
perlecan + H2O
?
Substrates: high activity, the enzyme produces discrete perlecan fragments corresponding to an origin in immunoglobulin repeat region domain IV, the enzyme cleaves every subpart of recombinantly generated perlecan domain IV. Identification and characterization of perlecan Dm IV-3 sites of cleavage by enzyme MMP-7, overview
Products: -
Products: -
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
-
Substrates: i.e. pro-human neutrophil peptide-1, in a cell-based assay system
Products: -
Products: -
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
-
Substrates: i.e. pro-human neutrophil peptide-1
Products: -
Products: -
?
syndecan-2 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
syndecan-2 + H2O
?
-
Substrates: MMP-7 cleaves both recombinant syndecan-2 and an endogenously glycosylated syndecan-2 ectodomain in the N-terminus at Leu149 residue in vitro. MMP-7 cleaves the N-terminal Leu residue in the extracellular domain of syndecan-2
Products: -
Products: -
?
tumor-associated antigen 90K + H2O
?
-
Substrates: i.e. TAA90K or/Mac-2-binding protein. TAA90K binds to pro- and active MMP7, it also binds to extracellular matrix proteins, and it increases the extracellular level of active MMP7 secreted from HT-29 cancer cells. MMP-7-mediated cleavage of TAA90K does not affect its binding to MMP-7, laminin-1, collagen IV and galectin-3 but reduces its interaction with fibronectin and laminin-10, and lowers the levels of proMMP-7 in the HT-29 medium, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no action on: pro-matrix metalloproteinase 2 and 3
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity at subsite P1: tolerates small amino acids such as Gly and Ala, larger residues such as Met, Pro, Gln and Glu are also accomodated well
Products: -
Products: -
?
additional information
?
-
-
Substrates: at subsite P1': hydrophobic aliphatic residues preferred, strong preference for Leu
Products: -
Products: -
?
additional information
?
-
-
Substrates: activates pro-matrix metalloproteinase 9
Products: -
Products: -
?
additional information
?
-
-
Substrates: activates progelatinase A by removing the propeptide in a process that does not require any autolytic cleavage
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: releases TNFalphaand Fas-L from the cell surface, after which they modulate macrophage migration and cell apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme could play a role in inflammatory tissue damage by proteolytically inactivating alpha1PI
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme in mesangial cells may contribute to the progression of injury during glomerular inflammatory states
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 plays an important role in the development and progression of renal cancer
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 content is elevated in tumors copared to healthy mucosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 content is elevated in tumors copared to healthy mucosa
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP7 plays an essential role in cancer, innate immunity, and in inflammatory disorders
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the expression of MMP-7 in gliomas is not related to the invasive behaviour
Products: -
Products: -
?
additional information
?
-
-
Substrates: the expression of MMP-7 in gliomas is not related to the invasive behaviour
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 plays a role in tumor angiogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 plays a role in tumor angiogenesis
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 interacts with anionic, cationic and neutral lipid membranes, it interacts strongest with anionic membranes, overview
Products: -
Products: -
?
additional information
?
-
Substrates: usage of a MMP-7-specific substrate solution containing 7-dimethylaminocoumarin-4-acetate/6-([7-nitrobenz-2-oxa-1,3-diazol-4-yl]amino) hexanoic acid fluorescence
Products: -
Products: -
?
additional information
?
-
-
Substrates: usage of a MMP-7-specific substrate solution containing 7-dimethylaminocoumarin-4-acetate/6-([7-nitrobenz-2-oxa-1,3-diazol-4-yl]amino) hexanoic acid fluorescence
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrix metalloproteinases are zinc-dependent neutral endopeptidases
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 interacts with insulin-like growth factor binding protein 5, inhibitor of metalloproteinase-3, fibronectin 1, and TFPI
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 is capable of degrading many extracellular matrix proteins and cellular adhesions
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 participates in activation other members of the MMP family
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrilysins proteolyze a number of extracellular matrix/basement membrane components, including type IV collagens and proteoglycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 assay using DQ-gelatin fluorescent substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: binding of MMP-7 to EJ-1 cell surface
Products: -
Products: -
?
additional information
?
-
-
Substrates: immunohistochemic analysis of peptide fragment degradation products
Products: -
Products: -
?
additional information
?
-
-
Substrates: two substrate peptides present in human skin elastin: PGGLAG, residues 67-72, containing Leu at P1', and LGGAGQ, residues 754-759, containing Ala at P1', and two further peptides PGGAAG and PGGGAG are modeled and docked into the MMP-7 catalytic site. The binding site was defined on the zinc ion
Products: -
Products: -
?
additional information
?
-
Substrates: cholesterol sulfate modulates the substrate preference of the enzyme, thereby regulating its pericellular proteolytic action
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 is an endopeptidase that degrades a broad range of substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: rapid identification of highly active and selective substrates using bacteriophage peptide display libraries
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: potentially important role of the enzyme in disruption of basement membranes by tumor or inflammatory cells
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction, MMP-7 is implicated in post-MI remodeling, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 cleaves E-cadherin from lung epithelium
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 assay using DQ-gelatin fluorescent substrate
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 is an endopeptidase that degrades a broad range of substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 assay using DQ-gelatin fluorescent substrate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 cleaves E-cadherin from lung epithelium
Products: -
Products: -
?
additional information
?
-
-
Substrates: rat and human enzyme do not activate rat collagenase 3
Products: -
Products: -
?
additional information
?
-
-
Substrates: phenylazo-Pro-Leu-Gly-Pro-D-Arg
Products: -
Products: -
?
additional information
?
-
-
Substrates: maximum activation of human interstitial collagenase 1 (pro-matrix metalloproteinase 1) when added in presence of 4-aminophenylmercuric acetate by cleaving the Gln80-Phe81 bond
Products: -
Products: -
?
additional information
?
-
-
Substrates: collagens of type I, III or V
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
-
Substrates: matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
Products: -
Products: -
?
elastin + H2O
elastin peptides
-
Substrates: degradation
Products: in the range of 500-8000 Da
Products: in the range of 500-8000 Da
?
fibronactin + H2O
fibronectin peptide fragments
-
Substrates: -
Products: MWs of 30 to 175 kDa
Products: MWs of 30 to 175 kDa
?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
Substrates: -
Products: -
Products: -
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
Substrates: 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
Products: -
Products: -
?
IGFBP-3 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
insulin-like growth factor binding protein-2 + H2O
?
Substrates: 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
Products: -
Products: -
?
insulin-like growth factor binding protein-5 + H2O
?
Substrates: in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
Products: -
Products: -
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
Substrates: 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
Products: -
Products: -
?
perlecan + H2O
?
Substrates: i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
Products: -
Products: -
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
-
Substrates: -
Products: -
Products: -
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
-
Substrates: i.e. procryptdins
Products: -
Products: -
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
-
Substrates: -
Products: -
Products: -
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
-
Substrates: i.e. pro-human neutrophil peptide-1, in a cell-based assay system
Products: -
Products: -
?
syndecan-2 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
Fibronectin + H2O
?
-
Substrates: also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
Products: -
Products: -
?
N-cadherin + H2O
?
-
Substrates: recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
Products: -
Products: -
?
N-cadherin + H2O
?
-
Substrates: recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
Products: -
Products: -
?
N-cadherin + H2O
?
-
Substrates: recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
Products: -
Products: -
?
Notch-1 + H2O
?
Substrates: 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
Products: -
Products: -
?
Notch-1 + H2O
?
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: releases TNFalphaand Fas-L from the cell surface, after which they modulate macrophage migration and cell apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme could play a role in inflammatory tissue damage by proteolytically inactivating alpha1PI
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme in mesangial cells may contribute to the progression of injury during glomerular inflammatory states
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 plays an important role in the development and progression of renal cancer
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 content is elevated in tumors copared to healthy mucosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 content is elevated in tumors copared to healthy mucosa
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MMP7 plays an essential role in cancer, innate immunity, and in inflammatory disorders
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the expression of MMP-7 in gliomas is not related to the invasive behaviour
Products: -
Products: -
?
additional information
?
-
-
Substrates: the expression of MMP-7 in gliomas is not related to the invasive behaviour
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-7 plays a role in tumor angiogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-7 plays a role in tumor angiogenesis
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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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Substrates: matrix metalloproteinases are zinc-dependent neutral endopeptidases
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additional information
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Substrates: 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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Substrates: 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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Substrates: MMP-7 interacts with insulin-like growth factor binding protein 5, inhibitor of metalloproteinase-3, fibronectin 1, and TFPI
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Substrates: MMP-7 is capable of degrading many extracellular matrix proteins and cellular adhesions
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Substrates: MMP-7 participates in activation other members of the MMP family
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Substrates: matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
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Substrates: matrilysins proteolyze a number of extracellular matrix/basement membrane components, including type IV collagens and proteoglycans
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Substrates: binding of MMP-7 to EJ-1 cell surface
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Substrates: 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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Substrates: 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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Substrates: potentially important role of the enzyme in disruption of basement membranes by tumor or inflammatory cells
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: MMP-7 cleaves E-cadherin from lung epithelium
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: MMP-7 cleaves E-cadherin from lung epithelium
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additional information
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Substrates: the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Na+
NaCl
-
wild-type and Y219F mutant MMP-7 activity is enhanced with increasing concentration of NaCl, activation by 550% and 850% at 4 M NaCl, respectively
Zinc
Zn2+
additional information
Ca2+
-
contains a zinc ion essential for enzyme activity as well as a second zinc ion necessary for enzyme stability
Zinc
-
contains 1 zinc atom per molecule which is essential for catalytic acivity
Zinc
-
two metal binding sites at which zinc is bound firmly and possibly a third site at which it is bound weakly
Zinc
-
two metal binding sites at which zinc is bound firmly and possibly a third site at which it is bound weakly
Zinc
-
2.36 (promatrilysin expressed in Escherichia coli), 2.13 (promatrilysin expressed in Chinese hamster ovary cells)
Zn2+
-
MMP-7 is a zinc metalloprotease. The stabilizing protein/zinc-bound water molecules might be the ionizable group responsible for pKe2 inb MMP-7
Zn2+
-
the inactive pre-proenzyme is cleaved to the pro-peptide, which is then activated when the propeptide residue Cys70 binds to the active site Zn2+
additional information
metal ions are required for the MMP-7-induced cell aggregation
additional information
-
promatrilysin and matrilysin do not contain significant amounts of Fe, Cu, Mn, or Ni
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin-3-gallate
-
inhibitory effect is increased on presence of 10 mM CaCl2, no interaction with Cl-
1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)-piperazine-2-carboxylic acid
-
-
3,9-di(4-methoxylphenyl)-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-di(4-methylphenyl)-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(2,3,4-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(2,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(2,4-dimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
3,9-dibenzyl-6,12-di(2,3,4-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-6,12-di(2,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-6,12-di(2,4-dimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-6,12-di(3,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-6,12-di(4-methoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-dibenzyl-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-diphenyl-6,12-di(4-fluoridephenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-diphenyl-6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-diphenyl-6,12-di(4-methoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-diphenyl-6,12-di(4-methylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3,9-diphenyl-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
3.9-diphenyl-6,12-di(3,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-di(2,3,4-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-di(2,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-di(2,4-dimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-di(3,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-di(4-methoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
andrographolide
-
a diterpenoid lactone isolated from a traditional herbal medicine Andrographis paniculata, downregulates MMP-7 in colorectal carcinoma LoVo cells leading to inhibition of cell migration and invasion, overview
BB-94
-
[4-(N-hydroxyamino)-(2R)-isobutyl-(3S)-(thienylthiomethyl)-succinyl]-L-Phe-N-methylamine
Brij-35
activates MMP-7 in a broad concentration range, but inhibits at high concentration
cardiolipin
associates with the enzyme at the cell surface and inhibits by 92%
diethyl 1-phenoxy-4-(4-propylphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(4-nitrophenyl)-1-phenoxy-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-[4-(5-methoxypentyl)phenyl]-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-[4-(5-methoxypentyl)phenyl]-1-phenoxy-1,4-dihydropyridine-3,5-dicarboxylate
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-(N-methyl-N-hexylaminocarbonyl)piperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)piperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-cyclohexanecarbonylpiperazine-2-carboxylate
-
-
methyl 4-[4-(4-bromophenyl)thiazol-2-yl]-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxylate
-
-
methyl-beta-cyclodextrin
inhibits release of the HAI-1 fragment by MMP-7-catalyzed cleavage
N-(2-[[(2S)-1-([(2S)-1-[(2S)-2-(2-amino-2-oxoethyl)pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino)-4-methyl-1-oxopentan-2-yl]-amino]-2-oxoethyl)-N2-[(4-chloro-3-trifluoromethyl)benzene-1-sulfonyl]-L-glutamine
compound shows low or negligible potency against MMP-1, -3, -8, -9, and -13 and is stable in human serum and liver microsomes
N-hydroxy-1-(4-bromophenyl)sulfonyl-4-(N-methyl-N-hexylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-bromophenyl)sulfonyl-4-(S)-(2-hydroxy-3-methyl-1-oxobutyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-bromophenyl)sulfonyl-4-[N-bis(2-methoxyethyl)aminocarbonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(1-oxohexyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(2-phenylethylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(3-ethoxy-1-propoxycarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(3-methoxyphenylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(3-pyridinylmethoxycarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-biphenylcarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-methyl-1,2,3-thiadiazole-5-carbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-morpholinylcarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(5-methyl-3-phenylisoxazole-4-carbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(isoxazole-5-carbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(n-hexylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-methyl-N-hexylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-methyl-N-phenylmethylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-methylpiperazine-1N-carbonyl)piperazine-2-carboxamide hydrochloride
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-propyl-N-cyclopropylmethyl aminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzylcarbamoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzyloxycarbonylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzylthiocarbamoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-cyclohexanecarbonylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-nicotinoylpiperazine-2-carboxamide hydrochloride
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-phenoxyacetylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-phenylmethylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-thiophenecarbonylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-[(3,5-dimethyl-4-isoxazolyl)sulfonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-[(hexahydro-1H-azepin-1-yl)carbonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-[2-amino-4-methyl-5-thiazolylsulfonyl]piperazine-2-carboxamide
-
-
N-hydroxy-4-[4-(4-bromophenyl)thiazol-2-yl]-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxamide
-
-
N-[3-[3,5-bis(hydroxymethyl)-1-phenoxy-1,4-dihydropyridin-4-yl]phenyl]acetamide
-
N-[4-chloro-3-(trifluoromethyl)benzene-1-sulfonyl]-L-gamma-glutamylglycyl-L-leucyl-L-valyl-L-alaninamide
compound shows low or negligible potency against MMP-1, -3, -8, -9, and -13 and is stable in human serum and liver microsomes
N-[4-chloro-3-(trifluoromethyl)benzene-1-sulfonyl]-L-gamma-glutamylglycyl-L-leucyl-L-valyl-L-prolinamide
compound shows low or negligible potency against MMP-1, -3, -8, -9, and -13
N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-(naphthalen-2-yl)-L-alanyl-N-(2-aminoethyl)-L-alaninamide
-
i.e. TAPI-1, a hydroxamate-based metalloproteinase inhibitor
Sulfatide
associates with the enzyme at the cell surface and inhibits by 80%
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
TAPI-1
a hydroxamate-based matrix metalloproteinase inhibitor, reduces the affinity of the enzyme for cholesterol sulfate and cardiolipin, but not for sulfatide, molecular mechanism by which TAPI-1 inhibits binding of MMP-7 to the lipids, overview
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
-
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucyl-[(1'',1'')-diphenyl]-methylamide
-
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucyl-[(1''R)-phenyl]-ethylamide
-
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucyl-[(1''S)-phenyl]-ethylamide
-
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucylmethylamide
-
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucylphenylamide
-
[4-(2,4-dimethoxyphenyl)-1-phenoxy-1,4-dihydropyridine-3,5-diyl]dimethanol
-
(-)-epicatechin-3-gallate
-
inhibition is un affected by presence of 10 mM CaCl2
(-)-gallocatechin-3-gallate
-
inhibitory effect is increased on presence of 10 mM CaCl2, no interaction with Cl-
batimastat
-
i.e. BB-94, BB-94 significantly reduces the amount of N-cadherin fragment produced in response to Fas-L
Cholesterol sulfate
non-competitive inhibition, decreases the enzyme's thermostability, inhibition mechanism, overview
Cholesterol sulfate
associates with the enzyme st the cell surface and modulates the substrate preference of the enzyme, 20% inhibition
TIMP-1
i.e. type 1 tissue inhibitor of MMPs, is elevated in colorectal tumor tissue compared to healthy mucosa
-
TIMP-1
expression and activity of MMP-7 in fetal membranes during premature rupture of membranes is increased, while the TIMP-1 level is reduced, immunohistochemic analysis, overview
-
TIMP-1
-
no apparent regulation of the expression of TIMP-1 by either tumor necrosis factor or enamel matrix derivative
-
TIMP-1
-
from gingival and dermal fibroblasts forms complexes with MMP-7 and inhibits its expression and activity
-
additional information
-
examination of inhibitor-enzyme complexes emphasizes the dominant role the zinc-coordination group plays in determining the relative potencies of their inhibitors
-
additional information
-
for lignans, dibenzylbutyryrolactone structure is essential for inhibitory effect
-
additional information
estrogen acidification of the luminal solution tends to alkalinize exocytotic vesicles and may lead to decreased activation of the MMP-7
-
additional information
-
estrogen acidification of the luminal solution tends to alkalinize exocytotic vesicles and may lead to decreased activation of the MMP-7
-
additional information
MMP-7 interacts with anionic, cationic and neutral lipid membranes, while the catalytic activity of the enzyme remains unaffected upon binding to neutral and negatively charged membranes, it is drastically impaired upon binding to the positively charged membranes, overview
-
additional information
angiogenesis and apoptosis do not influence MMP-7 expression in lung cancer cells, overview
-
additional information
-
angiogenesis and apoptosis do not influence MMP-7 expression in lung cancer cells, overview
-
additional information
inhibition of hyaluronan synthases HAS2 and HAS3 highly decreases MMP-7 expression and activity in SW620 cells
-
additional information
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
-
additional information
-
green tea catechins inhibit MMP-7 competitively and the galloyl group is essential, differences result from the B-ring, mechanism of inhibition
-
additional information
design, synthesis and biological evaluation of 3,9-diazatetraasteranes as matrilysin inhibitors, molceular docking and simulations, overview. Common interaction mechanism of 3,9-diazatetraasteranes with the catalytic site of matrilysin
-
additional information
the internal four residues Ile29, Arg33, Arg51 and Trp55 of MMP-7 are important for binding of inhibitory acidic lipids, overview
-
additional information
nitro-based selective inhibitors against matrix metalloproteinase-7, overview. Kinetics and active-site-binding mode of the inhibitors, molecular docking. A reasonable adjustment of the P'3 side chains of the nitro-based MMP inhibitors could improve selectivity for the inhibition of MMP-7 over MMP-1 (EC 3.4.24.7)
-
additional information
-
two zinc and two calciums are required for inhibitor binding
-
additional information
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Brij-35
activates MMP-7 in a broad concentration range, but inhibits at high concentration
Cholesterol sulfate
-
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
-
treatment with Fas ligand, Fas-L, increases levels of active MMP-7 by 80%
-
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
-
heparin
porcine intestinal heparin, increases activity by decreasing the Km value, increases the enzyme's thermostability
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
-
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
-
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
-
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
-
additional information
infections with Helicobacter pylori increases MMP-7 expression in the stomach epithelium, overview
-
additional information
-
infections with Helicobacter pylori increases MMP-7 expression in the stomach epithelium, overview
-
additional information
angiogenesis and apoptosis do not influence MMP-7 expression in lung cancer cells, overview
-
additional information
-
angiogenesis and apoptosis do not influence MMP-7 expression in lung cancer cells, overview
-
additional information
-
cholesterol, dehydroepiandrosterone sulfate, and heparin do not affect MMP-7-catalyzed degradations of fibronactin and laminin-332
-
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
-
additional information
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, overview
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019 - 0.057
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
0.028
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-L-Leu-[N3-2,4-dinitrophenyl-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C
0.0511 - 0.211
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
0.019
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
pH 7.5, 25°C, with 0.05 mM heparin
0.057
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
pH 7.5, 25°C, without heparin
0.0511
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219C
0.0732
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219F
0.0736
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, wild-type enzyme
0.0788
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219A
0.0865
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219D
0.211
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219S
additional information
additional information
-
highly active and selective substrates produced by using bacteriophage peptide display libraries
-
additional information
additional information
-
Km-value decreases from 2.57 mg/ml to 2.29 mg/ml upon nitration of 4-5 Tyr residues of enzyme, pH 7.5, 25°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.61 - 6.43
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
1.61
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219C
3.53
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219A
5.41
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219S
6.18
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219F
6.35
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219D
6.43
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, wild-type enzyme
additional information
additional information
-
turnover of highly active and selective substrates produced by using bacteriophage peptide display libraries
-
additional information
additional information
-
kcat-value decreases from 337 mg/ml x M x s to 305 mg/ml x M x s upon nitration of 4-5 Tyr residues of enzyme, pH 7.5, 25°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26 - 87
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
26
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219S
32
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219C
45
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219A
74
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219D
84
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, mutant Y219F
87
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00001
N-(2-[[(2S)-1-([(2S)-1-[(2S)-2-(2-amino-2-oxoethyl)pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino)-4-methyl-1-oxopentan-2-yl]-amino]-2-oxoethyl)-N2-[(4-chloro-3-trifluoromethyl)benzene-1-sulfonyl]-L-glutamine
pH 7.5, temperature not specified in the publication
0.000016
N-[4-chloro-3-(trifluoromethyl)benzene-1-sulfonyl]-L-gamma-glutamylglycyl-L-leucyl-L-valyl-L-alaninamide
pH 7.5, temperature not specified in the publication
0.000019
N-[4-chloro-3-(trifluoromethyl)benzene-1-sulfonyl]-L-gamma-glutamylglycyl-L-leucyl-L-valyl-L-prolinamide
pH 7.5, temperature not specified in the publication
0.0000148
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucyl-[(1'',1'')-diphenyl]-methylamide
pH 7.5, 37°C, recombinant enzyme
0.0000089
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucyl-[(1''R)-phenyl]-ethylamide
pH 7.5, 37°C, recombinant enzyme
0.0000037
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucyl-[(1''S)-phenyl]-ethylamide
pH 7.5, 37°C, recombinant enzyme
0.000158
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucylmethylamide
pH 7.5, 37°C, recombinant enzyme
0.0000094
[(2'R,3'S)-2'-iso-butyl-3'-hydroxy-4'-nitro]butyryl-(S)-tert-leucylphenylamide
pH 7.5, 37°C, recombinant enzyme
additional information
additional information
inhibition kinetic analysis
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00001
batimastat
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
wound-healing activity of cut HT-29 cells, overview
additional information
quantitative determination of binding sites for MMP-7 on epithelial cells and Ishikawa cells, overview
additional information
-
quantitative determination of binding sites for MMP-7 on epithelial cells and Ishikawa cells, overview
additional information
quantitative MMP-7 expression anaylsis in glioma samples, overview
additional information
-
quantitative MMP-7 expression anaylsis in glioma samples, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
additional information
additional information
-
upon nitration of 4 or 5 Tyr residues, activity at pH 7 decreases significantly, while that at pH 7-10 is unchanged, leading to anomalous pH-dependence with an additional third pKa-value at 6.2-6.4
additional information
-
the pKe1 and pKe2 values of Y193F are 4.4 and 9.8, respectively, and those of Y216F are 4.3 and 9.8, respectively, both of which are the same as those of the wild-type enzyme with 4.2 and 9.7, respectively
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
-
4.5: about 40% of activity maximum, 8.5: about 65% of activity maximum, 2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
5.5 - 8.8
-
5.5: about 30% of activity maximum, 8.8: about 40% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
683312, 683329, 683331, 683334, 683345, 683362, 683399, 683413, 683475, 683497, 683563, 683843, 683847, 683864, 683933, 683945, 683946, 684022, 684052
SwissProt
brenda
-
707186, 707569, 707870, 707880, 707905, 707957, 707986, 707987, 708011, 708021, 708084, 708198, 708293, 708301, 708308, 708392, 708635, 708667, 708674, 708772, 709060
-
-
brenda
-
709079, 709318, 709345, 709415, 709655, 709669, 709760, 709977, 710176, 710179, 710360, 710536, 710651, 710683, 717204, 717292, 717397, 717399, 717745, 717801, 718394
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
expression in MCF-7 breast cancer cell. Overexpression of enzyme leads to increased invasion and gelatinase activation
-
-
brenda
expression in polarized MDCK cell and HCA-7 and Caco2 colon cancer cell lines
-
-
brenda
human
-
-
brenda
a His6-NH2 terminally tagged form of matrilysin expressed in Escherichia coli
-
-
brenda
enzyme is obtained by transfection of linearized PEE12 PUMP expression vector into NSO mouse myeloma cells
-
-
brenda
expression in Escherichia coli and Chinese hamster ovary cells, expression vector pGEX-2T
-
-
brenda
Sprague Dawley rats, spontaneously hypertensive rats and age-matched Wistar-Kyoto rats
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
brenda
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
brenda
MMP-7 activity is higher in amnion from premature rupture of membranes compared to cesarean delivery, overview
brenda
-
immunohistochemic detection of MMP7 expression in biliary tract cancer, semi-quantitative RT-PCR and real-time RT-PCR, overview
brenda
-
the matrix metalloproteinases MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 are highly expressed in the tumor-bone microenvironment, and, of these, MMP-7 and MMP-9 are found to be localized to bone-resorbing osteoclasts in human breast-to-bone metastases
brenda
early stage primary cancers, MMP-7 correlates with breast cancer development, overexpression of MMP-7 and ErbB4, overview
brenda
-
induction of enzyme expression by TNF-alpha and interleukin IL-1beta
brenda
MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
brenda
-
expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
brenda
-
low expression of MMP-7, which is induced by physiological processes such as wound healing, but also malignant transformation of epidermal cells
brenda
-
i.e. ELF, proMMP-7 protein is not detectable in any of the 3 HIV1- groups, including HIV1- smokers with early emphysema. In contrast, ELF pro-MMP-7 is readily detectable in the ELF of HIV1+ smokers with early emphysema
brenda
expression and activity of MMP-7 in fetal membranes during premature rupture of membranes, immunohistochemic analysis, overview
brenda
highly variable MMP-7 expression in the glioma population
brenda
MMP-7 expression analysis of 106 different samples, higher enzyme levels in squamous compared to adenocarcinomas, MMP-7 expression increases the cell proliferation and is correlated to Wnt1 expression,overview
brenda
high constitutive secretion of proMMP-7 in the EAC cell line, dependent on phosphatidylinositol (PI) 3-kinase, inhibited by PI 3-kinase inhibitor LY294002 but not by inhibitors of protein kinase C, or MAP kinase activation
brenda
-
strong expression of MMP-7 in epithelial dysplasia with a two-phase appearance: a clear demarcation of MMP-7-immunopositive (+) lower dysplastic/basaloid cells from non-positive upper keratinized cells
brenda
-
exclusive detection of active enzyme in conditioned medium of dissociated cells, detection of proenzyme only in conditioned medium of non-dissociated cells. Enzyme protein is greatly reduced by treatment with the epidermal growth factor receptor inhibitor AG1478 and the mitogen activated protein kinase kinase inhibitor U0126
brenda
-
MMP-7 expression analysis semiquantitatively by immunohistochemistry in prostate cancer. E1AF, an ets-oncogene family transcription factor, expression correlates with that of MMP-7
brenda
invasive prostate cancer cells, high enzyme expression level
brenda
-
induction of enzyme expression by TNF-alpha and interleukin IL-1beta
brenda
additional information
MMP-7 expression analysis, the expression level is increased compared to normal cells
brenda
-
carcinoma in situ, MMP-7+ cells are spread over the whole epithelial layer
brenda
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
brenda
-
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
-
brenda
MMP-7 overexpression in carcinomas compared to healthy tissue, mucosal, tubular, tubulovillous, or villous colonic adenoma subtypes, MMP-7 expression analysis, overview
brenda
MMP7 s generally not expressed by normal differentiated epithelial colon cells, but has been shown to be up-regulated in human colon adenomas and adenocarcinomas
brenda
-
more expression of cyclooxygenase 2 and matrix metalloproteinase 7 is correlated in colorectal cancer, analysis of COX-2 and MMP-7 RNA in feces from patients, overview
brenda
MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
brenda
MMP-7 is overexpressed in colorectal cancer
brenda
-
YAP is a critical regulatory factor in upregulating MMP-7 expression on the stiffer substrate in colorectal cancer
brenda
sprouting, of different cancers, the endothelial enzyme is associated with CD34 and/or CD105 expression
brenda
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
brenda
vaginal-cervical epithelial cells secrete constitutively MMP-7 into the luminal solution
brenda
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
brenda
-
expression of MMP-7 in the normal oral mucosal epithelium is restricted mainly to the parabasal layers
brenda
-
primary specimen, overexpression of MMP-7, realtime PCR, RT-PCR or Western blotting analysis
brenda
-
wild-type HCT-116 and oxaliplatin-resistant RHCT-116 p53 positive- and p53 negative cell lines
brenda
expression analysis in hearts after transplantation, overview
brenda
LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, distribution, overview
brenda
-
MMP-7 expression analysis in estrogen-dependently proliferating cells, overview
brenda
higher expression in epithelium compared to stroma, expression in proximal and distal convoluted tubules and collecting duct, and weakly in renal corpuscles and mesangial cells, podocytes, and Bowman's capsule of glomerules, overview
brenda
MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
brenda
MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
brenda
expression analysis in kidneys after transplantation, overview
brenda
-
HIV1- smokers with early emphysema have a trend toward increased relative alveolar matrilysin/MMP-7 gene expression compared with HIV1- healthy smokers and HIV1- healthy nonsmokers. HIV1+ smokers with early emphysema have significantly higher relative expression of alveolar mucosa MMP-7 than both HIV1- healthy smokers and HIV1- healthy nonsmokers. HIV1+ smokers with early emphysema have increased expression over and above the increase in HIV- smokers with early emphysema, overview
brenda
-
expression levels of fibulin-5 and MMP-7 are inversely correlated in lung tumors
brenda
esophageal, expression of proMMP-7 but not secretion in myofibroblasts
brenda
infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
brenda
Gallus gallus Hy-Line Brown
-
infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
-
brenda
higher expression of MMP-7 in RCC subtypes, i.e. chromophobe, renal papillary and oncocytomas, compared to benign epithelial neoplasias, overview
brenda
-
from patients from Canada and Finland. Average indices of MMP-7 in epithelial cells are higher than in myoepithelial cells, but a significant association to the disease does not exist
brenda
-
analysis of expression of MMP-7 by immunohistochemistry, overview
brenda
-
cancer patients have higher serum levels of MMP-3 and MMP-7 than those with duodenal ulcer and gastritis, overview
brenda
-
circulating MMP-7 serum concentration is significantly elevated in patients with distant metastasis of prostate cancer, overview
brenda
-
the serum MMP-7 level is significantly higher in the patients with cholangiocarcinoma compared to benign biliary tract disease patients
brenda
-
MMP-7 positivity is reduced from carcinoma cells but instead appears in stromal cells
brenda
stimulated by VEGF, no MMP-7 expression in unstimulated HUVEC
brenda
-
MMP-7 levels in eutopic and ectopic endometriose, overview. MMP-7 expression levels are significantly higher in the endometrial epithelial cells from women with deep infiltrating endometriosis compared with those isolated from the endometria of patients with only superficial peritoneal endometriosis, uterine myomas or normal endometrium, in the proliferative, late secretory and menstrual phases. MMP-7 protein expression is detected in the ectopic endometrial epithelial cells of samples of deep infiltrating endometriosis, of ovarian endometriosis, of black peritoneal lesions, and of red peritoneal lesions. MMP-7 protein expression in epithelial cells is significantly higher in red peritoneal lesions compared with that of deep infiltrating endometriosis, ovarian endometriosis and black peritoneal lesions, in all phases of the menstrual cycle, quantitative real-time RT-PCR and immunohistochemical analysis, overview
brenda
-
MMP7 expression during the menstrual cycle in the human endometrium and fallopian tube, overview. The level of MMP7 secretion is highest in the secretory phase, although the difference from the proliferative phase does not reach statistical significance, neither in the endometrium nor in the fallopian tube
brenda
additional information
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation. The MMP-7 mRNA expression is significantly higher on plastic than that on a gel substrate
brenda
additional information
-
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation. The MMP-7 mRNA expression is significantly higher on plastic than that on a gel substrate
brenda
additional information
Gallus gallus Hy-Line Brown
-
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation. The MMP-7 mRNA expression is significantly higher on plastic than that on a gel substrate
-
brenda
additional information
MMP-7 content is elevated in tumors compared to helathy mucosa
brenda
additional information
-
MMP-7 content is elevated in tumors compared to helathy mucosa
brenda
additional information
-
MMP-7 activity is significantly higher in atherosclerotic plaques than internal mammary arteries
brenda
additional information
-
MMP-7 expression analysis in healthy persons and liver cirrhosis patients, overview
brenda
additional information
-
MMP7 basal expression is higher in the oxaliplatin-resistant compared to the parental cell lines
brenda
additional information
-
matrilysin-1 is expressed in injured lung and in cancer but not in normal epithelia and cell line BEAS-2B
brenda
additional information
-
heparan sulfate proteoglycans, especially perlecan, are extracellular docking molecules for MMP-7
brenda
additional information
-
MMP-7 expression analysis in gingival tissue, overview
brenda
additional information
-
MMP-7 expression analysis in gastric cancer cell lines, overview
brenda
additional information
-
quantitative enzyme expression in ulcerative colitis patients and healthy humans, 35 samples, overview
brenda
additional information
in colon cancer in neoplastic cells but not in stromal cells, enzyme expression and immunohistochemic analysis, overview
brenda
additional information
profile of metalloproteinases expression changes during colorectal cancer development, expecially of MMP-7, MMP-9, MMP-1, and their inhibitor TIMP-1, overview
brenda
additional information
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profile of metalloproteinases expression changes during colorectal cancer development, expecially of MMP-7, MMP-9, MMP-1, and their inhibitor TIMP-1, overview
brenda
additional information
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MMP-7 is overexpressed in a variety of epithelial cancers, such as stomach, liver, pancreatic, and colon cancer
brenda
additional information
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pulmonary CD103+ dendritic cells are significantly increased in bleomycin-injured wild-type compared with Mmp7-/- mice, and CD103+ leukocytes
brenda
additional information
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pulmonary CD103+ dendritic cells are significantly increased in bleomycin-injured wild-type compared with Mmp7-/- mice, and CD103+ leukocytes
-
brenda
additional information
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no MMP-7 in gingival fibroblasts isolated and cultured from gingiva. Coculture of aorta fiboblasts with fibroblasts from gingiva lead to inhibition of the secreted MMP-7 and reduction of its level at least in part due to the formation of MMP-7/TIMP-1 complexes, after 21 days MMP-7 is completely inhibited, the effect is less with dermal fibroblasts, overview. siRNA TGF-beta1 inhibits the inhibition efficiency of GF on MMP-7
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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wild-type MMP-7 Gly137 is distributed both in the membrane and cytosol fractions
brenda
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
-
brenda
additional information
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the MMP-7 Asp137 genetic variant is preferentially localized to the cell surface plasma membrane
brenda
syndecan-2 functions as a cell surface docking receptor for pro-MMP-7, overview
brenda
extracellular MMP-7 binds to cell-surface cholesterol sulfate (CS) and acts as a membrane-associated protease
brenda
the enzyme is expressed in the cytoplasm in colorectal cancer cells
brenda
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secretion of enzyme both to basolateral and apical compartment. Enzyme protein is more abundant in basolateral compartment, but the activity is 2fold higher in apical compartment. Enzyme overexpression increases cell saturation density as a result of increased cell proliferation due to apical enzyme activity
-
brenda
plasma, MMP-7 levels correlate with the tumor development, overview
-
brenda
the enzyme is secreted via soluble N-ethylmaleimide sensitive fusion factor attachment protein receptor-facilitated exocytosis of MMP-7
-
brenda
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secretory MMP-7 has to be recruited onto the cell surface to hydrolyze biologically relevant molecules
-
brenda
MMP-7 is secreted, which is enhanced by syndecan-2
-
brenda
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MMP7 is secreted mostly from the endometrial epithelium cells where attachment occurs
-
brenda
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
brenda
MMP-7 interacts with anionic, cationic and neutral lipid membranes, it interacts strongest with anionic membranes, overview
brenda
fetal membranes at term from women with no labor, i.e. cesarean delivery, with labor, i.e. normal delivery, and with labor during premature rupture of membranes, expression and activity of MMP-7 in fetal membranes during premature rupture of membranes is increased, while the TIMP-1 level is reduced, immunohistochemic analysis, overview
brenda
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
brenda
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the MMP-7 Asp137 genetic variant is preferentially localized to the cell surface plasma membrane
brenda
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wild-type MMP-7 Gly137 is distributed both in the membrane and cytosol fractions
brenda
charge-triggered membrane insertion of matrix metalloproteinase-7. Binding to cholesterol sulfate partially embeds the protease in the bilayer, restricts its diffusion, and tips the active site away from the bilayer. Its insertion of hydrophobic residues organizes the lipids, pushing the head groups and sterol sulfate outward towards the enzyme's positive charge on the periphery of the enlarged interface. Fluorescence probing demonstrates a similar mode of binding to plasma membranes and internalized vesicles of colon cancer cells. Binding of bilayered micelles induces allosteric activation and conformational change in the auto-inhibitory peptide and the adjacent scissile site, illustrating a potential intermediate in the activation of the zymogen. Cholesterol sulfate reorients and inserts proMMP-7 into bicelles. Potential interactions of the II-III loop and interdomain linker with bilayer, NMR structure determination and analysis, overview
brenda
additional information
enzyme localization and comparison to other MMPs, immunohistochemic analysis
-
brenda
additional information
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enzyme localization and comparison to other MMPs, immunohistochemic analysis
-
brenda
additional information
Gallus gallus Hy-Line Brown
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enzyme localization and comparison to other MMPs, immunohistochemic analysis
-
-
brenda
additional information
estrogen stimulates activation of the pro-MMP-7 intracellularly and augmented secretion of the activated MMP-7 form, overview
-
brenda
additional information
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estrogen stimulates activation of the pro-MMP-7 intracellularly and augmented secretion of the activated MMP-7 form, overview
-
brenda
additional information
the enzyme potentially associates with the cell surface via sulfatide and cardiolipin when they are overexpressed on the cell surface, molecular interaction, overview
-
brenda
additional information
Expression of proMMP-7 but not secretion in myofibroblasts
-
brenda
additional information
MMP-7 is one of the smallest MMPs, and it is synthesized as an inactive zymogen
-
brenda
additional information
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TGF-1beta mediates the secretion of MMP-7, but TGF-1beta inhibits MMP-7 expression. The MMP-7 gene has three TGF-beta1 inhibitory element, TIE, sites
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the active-site tyrosyl residue, Tyr219, is conserved in all other MMPs
evolution
matrilysin is a member of the matrix metalloproteinase (MMP) gene family
evolution
the enzyme is a member of a zinc-dependent endopeptidases family (MMPs)
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
malfunction
-
transforming growth factor-B1 and matrix metalloproteinase-7 promoter variants induce risk for Helicobacter pylori-associated gastric precancerous lesions
malfunction
-
a nonsynonymous genetic variant D137 of matrix metalloproteinase-7 confers risk of liver cirrhosis, overview
malfunction
-
high MMP-7 expression is associated with a worse overall survival of patients with acinic cell carcinoma, while low MMP-7 expression is associated with worse disease-specific survival of patients with acinic cell carcinoma
malfunction
-
the enhanced metabolism of perlecan associated with MMP-7 plays an important role in the cell proliferation of oral epithelia in their malignant transformation process
malfunction
-
MMP-7 polymorphisms are involved in colorectal cancer progression, overview
malfunction
-
epigenetic silencing or knockdown of fibulin-5, a vascular ligand for integrin receptors and a suppressor of lung cancer invasion and metastasis, promotes lung cancer invasion and metastasis by activating MMP-7 expression through the ERK pathway, injection of fibulin-5-deficient and unmodified H-460 cells into nude mice, overview
malfunction
-
overexpression of MMP-7 enhances syndecan-2 shedding, whereas the opposite is true when MMP-7 levels are knocked-down using small inhibitory RNAs
malfunction
MMP-7-deficient mice show educed beta-catenin activation after lung injury or bleomycin treatment
malfunction
-
MMP-7 pro-domain mutants lacking the N-terminal linker of the pro-domain (DELTAN, residues 9-79), the C-terminal linker (DELTAC, residues 1-73), or both (DELTANC, residues 9-73) interact with GST-tagged extracellular domain of syndecan-2 (S2E) in pulldown assays
malfunction
resveratrol attenuates renal injury and fibrosis by inhibiting epithelial-mesenchymal transition (EMT) process which is attributed to the fact that the up-regulated shRNA interfering MMP7 and sirtuin 1 (SIRT1) by resveratrol deacetylates Smad4 and inhibits MMP7 expression. In developing renal fibrosis, tubular epithelial cells in the kidney undergo epithelial-mesenchymal transition (EMT). Resveratrol reverses human kidney 2 (HK-2) cell EMT, renal I/R injury, and renal fibrosis. MMP7 inhibition is responsible for RSV-induced EMT repression
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
malfunction
myofibroblasts exhibit increased migration and invasion in response to conditioned media from OE33 cells that is reduced by MMP-7 knockdown and immunoneutralization
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
-
malfunction
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MMP-7-deficient mice show educed beta-catenin activation after lung injury or bleomycin treatment
-
metabolism
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matrix metalloproteinase-7 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. The induction is not inhibited by p-aminosalicyclic acid, an agent used to treat drug-resistant tuberculosis. The p38 MAPK pathway regulates the divergence between MMPs and TIMP-1
metabolism
-
yes-associated protein (YAP), EGFR, integrin-alpha2beta1 and MRLC produce a positive feedback loop that enhances MMP-7 expression. Stiff substrates enhance colorectal cancer cell viability by upregulating MMP-7 expression through a positive feedback loop
metabolism
-
syndecans mediate the interaction between the ECM and the cell. Syndecan-2 regulates MMP-7 gene expression in colon cancer cells. The expression of a syndecan-2 mutant in which Tyr51 is changed to Ala diminishes the interaction between the syndecan-2 extracellular domain and the pro-domain of MMP-7. HT-29 colon adenocarcinoma cells expressing the interaction-defective mutant exhibit reductions in the cell-surface localization of MMP-7, the processing of pro-MMP-7 into active MMP-7, the MMP-7-mediated extracellular domain shedding of both syndecan-2 and E-cadherin, and syndecan-2-mediated anchorage-independent growth. Tyr51 of the syndecan-2 extracellular domain mediates its interaction with and a and activating processing of pro-MMP-7 and regulates MMP-7-dependent syndecan-2 functions. Syndecan-2 induces extracellular release of E-cadherin and supports the acquisition of a fibroblast-like morphology by regulation of MMP-7 in a colon cancer cell line
metabolism
MMP-7-induced cancer cell aggregation is an important mechanism in cancer metastasis, and the soluble fragment of hepatocyte growth factor activator inhibitor type 1 (sHAI-1) is an essential component of MMP-7-induced stimulation of cancer metastasis
metabolism
possible metabolism of MMP-7 by myofibroblasts studied by proteomic analysis indicates degradation via extensive endopeptidase, followed by amino- and carboxpeptidase, cleavages
physiological function
-
osteoclast-derived MMP-7 significantly contributes to tumor growth and tumor-induced osteolysis, overview. Solubilization of RANKL by MMP-7 is a potential mechanism through which MMP-7 mediates mammary tumor-induced osteolysis, mechanism, overview. MMP-7 is capable of processing a number of nonmatrix molecules to soluble active forms that have profound effects on cell-cell communication, such as RANKL, a crucial mediator of osteoclast precursor recruitment and maturation
physiological function
-
MMP-7 is a potential factor in the cascade affecting the malignant potential of extracellular matrix
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
-
MMP-7 mediates cleavage of N-cadherin and promotes vascular smooth muscle cell apoptosis, that can lead to thinning of the fibrous cap and atherosclerotic plaque instability
physiological function
-
serum MMP-7 is increased in diabetic renal disease and diabetic diastolic dysfunction. Total MMP-7 is increased in patients with diastolic dysfunction and those with macroalbuminuria
physiological function
-
Helicobacter pylori infection upregulates the expression of matrix metalloproteinases, involved in chronic inflammation, ulceration, and cancer development
physiological function
-
increased expression of ets-oncogene family transcription factor E1AF is involved in tumor aggression of prostate cancer influenced by regulation of MMP-7
physiological function
-
MMP-7 tissue expression and serum concentration is associated with cancer progression and metastasis, elevated serum matrix metalloproteinase 7 levels predict poor prognosis after radical prostatectomy
physiological function
-
matrix metalloproteinases are extracellular proteolytic enzymes involved in tumor progression
physiological function
-
MMP-7 is a key regulator of cisplatin resistance in cells of head and neck squamous cell carcinomas, overview
physiological function
-
matrilysins, i.e. MMP-7 or matrilysin-1, and MMP-26 or matrilysin-2, are involved in cell proliferation, apoptosis, invasion, and metastasis. Matrilysins have a role in the process of tissue remodeling and growth in ameloblastomas and adenomatoid odontogenic tumors, but it does not relate to the their distinct patterns of aggressiveness
physiological function
-
associated expression of metalloproteinase-1, metalloproteinase-7 and VEGF in colorectal adenocarcinoma is related to the incidence of disease recurrence
physiological function
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MMP7 is a metalloproteinase with prometastatic function related to early tumor development, metastatic potential, and clinical outcome in cancer. MMP7 is related to the acquisition of oxaliplatin-resistance in cancer cell lines and its inhibition restores drug sensitivity by increasing Fas receptor
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
-
MMP-7 is overexpressed in many malignancies, and plays a role in tumour progression. Association between MMP-7 tissue expression and poor prognosis for patients with gastric cancer
physiological function
-
LNgamma2 and LNbeta3, in conjunction with MMP7, play a key role in the progression of biliary tract cancer. MMP7 is positivity correlated with LNgamma2 or LNbeta3 expression but not with clinicopathological characteristics
physiological function
-
matrilysin-1 promotes migration and proliferation of airway epithelial cells in vitro, and matrilysin-1 may play an important role in the bronchiolization of alveoli by promoting proliferation, migration, and attenuation of apoptosis involving multiple genes in the MAP kinase pathway in vivo. Matrilysin-1 inhibits apoptosis in vitro, mechanism, 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 , ong-term mechanisms involving metalloproteinases such as MMP-7 and ADAM-12
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
-
matrix metalloproteinase-7 polymorphism is a risk factor for endometrial cancer susceptibility, overview
physiological function
-
expressions of matrix metalloproteinase-2, matrix metalloproteinase-7, and E-cadherin correlate with pY1349 hepatocyte growth factor receptor/c-Met expression MMP-7 is involved in the role of pY1349 hepatocyte growth factor receptor/c-Met in tumor development, overview
physiological function
-
MMP-7 deletion improves survival after myocardial infarction
physiological function
-
epithelial MMP7 is expressed during asthma and is required for the maximum activity of interleukin 25 in promoting the differentiation of T helper type 2 cells. MMP7 coordinates allergic lung inflammation by activating interleukin 25 while simultaneously inhibiting retinoid-dependent development of regulatory T cells
physiological function
-
expression of MMP7 is increased in human colorectal carcinomas, and correlates with malignant progression, 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
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
physiological function
-
matrix metalloproteinase-7 degrades the extracellular matrix and is implicated in tuberculosis-driven tissue destruction, signaling pathways regulating macrophage MMP-7 in human pulmonary tuberculosis, overview
physiological function
-
periodontal disease is characterized by increased expression and activity of matrix metalloproteinases and insufficient expression/activity of their inhibitors, tissue inhibitors of matrix metalloproteinases, TIMPs. This altered MMP-TIMP balance results in progressive destruction of gingival and periodontal extracellular matrix
physiological function
-
matrilysin is important for neutrophil migration into the lung in animal models of lung inflammation
physiological function
-
the cell surface heparan sulfate proteoglycan syndecan-2 regulates the activation of matrix metalloproteinase-7 as a docking receptor. MMP-7 directly mediates shedding of syndecan-2 from colon cancer cells
physiological function
-
binding of MMP-7 to cell surface cholesterol sulfate is essential for the cell membrane-associated proteolytic action of MMP-7 thereby ECM, thereby. 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
physiological function
-
MMP-7 expression in inflammatory and endothelial cells indicates a role of MMP-7 for both colitis associated neoangiogenesis and inflammatory changes, analysis of the regulation patterns of MMP-7, overview
physiological function
the enzyme is responsible for aggressive malignant phenotypes and poor prognoses implicated in many cancers
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
matrix metalloproteinases take part in tumor invasion and metastasis through modification of the biological functions of various cell surface proteins and degradation of extracellular matrix proteins. Acidic lipids differentially regulate pericellular proteolysis by MMP-7 through allosteric alteration of the substrate-binding site and their inherent affinities for MMP-7 substrates, overview
physiological function
a long C-terminal portion of perlecan domain IV, DmIV-3, induces a strong clustering phenotype in the metastatic PCa cell lines, PC-3 and C4-2. MMP-7 digestion of Dm IV-3 reverses the clustering effect into one favoring cell dispersion, pro-metastasis effects of MMP-7 on prostate cancer cells
physiological function
the enzyme plays an important role in tumor microenvironment, it decreases the susceptibility to 5-fluorouracil in colon cancer cells
physiological function
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
physiological function
-
stiff substrates (like plastic) enhance colorectal cancer cell viability by upregulating MMP-7 expression through a positive feedback loop, in contrast to soft substrates (e.g. collagen type I). Yes-associated protein (YAP) activity increases MMP-7 expression on stiffer substrates
physiological function
-
the extracellular matrix (ECM) is the three-dimensional network that structurally and functionally integrates cells into tissues. Through its diversity in composition and physical nature, the ECM can perform many functions, such as providing support, separate tissues, and regulating intercellular communication. the matrix metalloproteinases (MMPs) perform important protease functions in extracellular matrix (ECM) degradation and remodeling. Matrix metalloproteinase-7 (MMP-7) plays a role in cancer progression. MMP-7 is overexpressed in a variety of epithelial cancers, such as stomach, liver, pancreatic, and colon cancer. Increased MMP-7 regulates cancer progression and invasion through regulating the proteolytic degradation of ECM molecules (e.g., elastin, type IV collagen, fibronectin, vitronectin, aggrecan, and proteoglycan), and non-ECM molecules (e.g., beta4 integrin, E-cadherin, FasL, proHB-EGF, and TNFalpha precursor). Syndecan-2 in association with MMP-7 regulates colon cancer activities. The N-terminal syndecan-2 extracellular domain directly interacts with the MMP-7 pro-domain, mutational analysis, overview
physiological function
matrix metalloproteinase 7 (MMP7) is reported to reduce E-cadherin and induce EMT by upregulation of beta-catenin/lymphoid enhancer-binding factor 1 (LEF1) signaling
physiological function
matrix metalloproteinase-7 (MMP-7) plays important roles in tumor progression and metastasis. Treatment of human colon carcinoma cells with active MMP-7 in vitro induces cell aggregation by cleaving cell-surface proteins. MMP-7 binds to colon cancer cells via cell surface-bound cholesterol sulfate and induces significant cell aggregation by cleaving cell-surface protein(s). These aggregated cells exhibit a dramatically enhanced metastatic potential. MMP-7 induces homotypic tumor cell aggregation via proteolytic cleavage of the membrane-bound 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). sHAI-1 can induce cancer cell aggregation. MMP-7-catalyzed generation of sHAI-1 requires cholesterol sulfate (CS). Binding of MMP-7 to CS is important for cleavage of HAI-1 localized in raft region. The MMP-7-induced cell aggregation of colon carcinoma cells consists of two steps, initial loose cell aggregation is secondly converted to tight cell aggregation. Region of HAI-1 corresponding to amino acid residues 141-249 is essential for cell aggregation-inducing activity of MMP-7
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
matrix metalloproteinase-7 (MMP-7) sheds signaling proteins from cell surfaces to activate bacterial killing, wound healing, and tumorigenesis, mechanism targeting soluble MMP-7 to membranes. MMP-7 regulates the remodeling of female reproductive organs by proteolytic activation of heparin-binding epidermal growth factor precursor (pro-HB-EGF) to activate its ErbB4 receptor in uterine and mammary epithelia and tumor cells
physiological function
increased expression of MMP-7 in the progression to cancer. MMP-7 expression increases at the invasive front in esophageal adenocarcinoma (EAC), which may be partly attributable to activation of phosphatidylinositol 3-kinase. Secreted MMP-7 may modify the tumor microenvironment by stimulating stromal cell migration and invasion
physiological function
compared to wild-type mice, Mmp7-/- mice have significantly less inflammation in the colon upon dextran sulfate sodium insult. Dextran sulfate sodium-induced alterations in junction proteins are mitigated in Mmp7-/- mice
physiological function
MMP7 significantly elevates the migration rate of Schwann cells but does not affect the proliferation rate of Schwann cells. An increased level of MMP7 contributes to Schwann cell migration and myelin sheaths formation after peripheral nerve injury. Treatment with MMP7 induces genetic changes in Schwann cells, 34 genes are differentially expressed
physiological function
in a vitro model system for acquired drug resistance, MMP7 overexpression potentiates the drug efflux activity and MMP7 knockdown decreases the drug efflux activity of tumor cells. MMP7 overexpression does not correlate with the acquired stemness or epithelial to mesenchymal transition of drug-resistant cells. MMP7 overexpressing cells exhibit altered homing properties, which is inhibited by treatment with HSP90 inhibitor 17AAG
physiological function
MMP-7 disrupts cadherin-based cohesion of microtumors
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
-
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
-
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
Gallus gallus Hy-Line Brown
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potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
-
additional information
-
secretory MMP-7 has to be recruited onto the cell surface to hydrolyze biologically relevant molecules, MMP-7 docks to the cell surface membrane via CD44 heparan sulfate proteoglycan, cholesterol sulfate, and CD151 binding
additional information
-
MMP7 is secreted mostly from the endometrial epithelium cells where attachment occurs and is suggested to be important in the implantation process
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
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
additional information
-
SFRP5, i.e. Secreted Frizzled-Related Protein 5, a negative regulator in Wnt signaling, expression downregulation is correlated with higher expression of MMP-7 in gastric cancer, overview
additional information
-
MMP-7 expression in squamous cell carcinoma is inversely correlated with that of the hyaluronan receptor CD44, overview
additional information
-
one active-site tyrosyl residue is Tyr219, but Tyr219 is not the ionizable group responsible for pKe2. Tyr219 is not critical for catalytic activity, but is involved in the broad pH-dependence of the activity. Tyr193 and Tyr216 are neither critical for catalytic activity nor involved in the broad pH-dependence of the activity. There are no lysine and arginine residues in the active site of MMP-7
additional information
-
human matrilysin-1 is one of the most potent elastases besides macrophage elastase in the family of matrix metalloproteinases
additional information
-
the inactive pre-proenzyme is cleaved to the pro-peptide, which is then activated when the propeptide residue Cys70 binds to the active site Zn2+
additional information
the enzyme potentially associates with the cell surface via sulfatide and cardiolipin when they are overexpressed on the cell surface, molecular interaction, overview. The internal four residues Ile29, Arg33, Arg51 and Trp55 of MMP-7 are important for binding of inhibitory acidic lipids, overview
additional information
determination of NMR structures of the proMMP-7 zymogen free in solution and bound to membrane mimics, as well as by probing with a membrane-responsive fluor. Binding of plasma membranes and internalization, and bicelle-induced removal of auto-inhibitory conformation, overview
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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_RAT
267
0
29885
Swiss-Prot
other Location (Reliability: 5)
MMP7_FELCA
262
0
29263
Swiss-Prot
other Location (Reliability: 3)
MMP7_MOUSE
264
0
29755
Swiss-Prot
Mitochondrion (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
28000
additional information
-
human enzyme expressed in COS cells as a latent form which undergoes autocleavage in presence of 4-aminophenylmercuric acetate to a 21000 MW and a 19000 MW active forms
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme binds to cholesterol sulfate on cell surface. Treatment of colon cancer cells with beta-cyclodextrin significantly reduces both enzyme binding to cell surface and enzyme-dependent proteolysis and cell aggregation
additional information
bipolar distribution of the electrostatic surface potentials on the crystallographic structure of MMP-7, overview
additional information
MMP7 structure anaylsis by dynamic light scattering, MALDI-TOF mass spectrometry, and NMR
additional information
-
MMP-7 consists of of two domains, a pro-peptide domain and a catalytic domain
additional information
MMP-7 possesses hydrophobic surface areas around the catalytic site, PDB code 2DDY
additional information
-
MMP-7 possesses hydrophobic surface areas around the catalytic site, PDB code 2DDY
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
colocalization and interaction of pro-enzyme with C-terminal extracellular loop of CD151. Enzyme is captured and activated on cell membranes through the interaction with CD151
proteolytic modification
Pro-MM-7 is proteolytically activated prior to secretion
proteolytic modification
syndecan-2 potentiates the enzymatic activity of pro-MMP-7 by activating its processing into the active MMP-7
proteolytic modification
-
proMMP7 needs to be activated to the mature active MMP7
proteolytic modification
-
promatrilysin shows autolytic activation, promatrilysin activation is regulated by sulfated glycosaminoglycans, overview. Presence of chondroitin-4,6-sulfate markedly accelerates activation of promatrilysin. Chondroitin-4,6-sulfate and heparin also markedly accelerates the ability of active wild-type matrilysin to cleave inactive promatrilysin
proteolytic modification
-
the inactive pre-proenzyme is cleaved to the pro-peptide, which is then activated when the propeptide residue Cys70 binds to the active site Zn2+
proteolytic modification
the enzyme is matured by proteolytic cleavage, the mature MMP-7 comprises Tyr78-Lys250
proteolytic modification
-
Tyr51 of the syndecan-2 extracellular domain mediates its interaction with and a and activating processing of pro-MMP-7 and regulates MMP-7-dependent syndecan-2 functions
proteolytic modification
binding of bilayered micelles induces allosteric activation and conformational change in the auto-inhibitory peptide and the adjacent scissile site, illustrating a potential intermediate in the activation of the zymogen
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in complex with compound N-(2-[[(2S)-1-([(2S)-1-[(2S)-2-(2-amino-2-oxoethyl)pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino)-4-methyl-1-oxopentan-2-yl]-amino]-2-oxoethyl)-N2-[(4-chloro-3-trifluoromethyl)benzene-1-sulfonyl]-L-glutamine. The 4-chloro-3-(trifluoromethyl)benzene moiety occupies the S1' pocket, and the sulfonamide can form hydrogen bonds with the nitrogen atom of Leu176 and the carbonyl group of Ala177
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G137D
-
a naturally occuring polymorphism, the Asp137 genetic variant of MMP-7 is susceptible to liver cirrhosis, MMP-7 D137 shows an increased level in its distribution to the plasma membrane of HSCs and an enhanced ability on cell migration, overview. It converts to its active form in specific microdomains
Y193F
-
site-directed mutagenesis, the mutant shows no pH-dependence shift, as does mutants Y219X
Y216F
-
site-directed mutagenesis, the mutant shows no pH-dependence shift, as does mutants Y219X
Y219A
-
site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219C
-
site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219D
-
site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219F
-
site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219S
-
site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
additional information
additional information
-
induction of specific natural killer cells using monocyte-derived dendritic cells electroporated with MMP-7-mRNA. The induced CTLs elicit an antigen-specific and HLA-restricted cytolytic activity against tumor cells endogenously expressing the MMP-7 protein. MMP-7-specific natural killer cells could be induced using peripheral blood mononuclear cells from a patient with acute lymphoblastic leukemia capable of recognizing the autologous leukemic blasts while sparing nonmalignant cells
additional information
-
host MMP-7 contributes to mammary tumor growth in the bone microenvironment after injection of human tumor cells into tibias of mice
additional information
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
additional information
-
genotype and allele frequencies of transforming growth factor-B1, TGF-B1, and MMP-7 polymorphisms do not differ between patients with Helicobacter pylori-associated gastric precancerous lesions and control persons, overview. But CagA-positive patients carrying MMP-7 -181 G allele have a risk for lymphoid follicle formation. Thus, the present study reveal significant association of functional MMP-7 and TGF-B1 gene variants toward susceptibility to Helicobacter pylori-induced precancerous gastric lesions
additional information
-
MMP-7 polymorphisms increase the risk for endometrial cancer in women over 50. The frequencies of MMP-7 -181 G/G and A/G genotypes are found to be significantly higher in cancer patients compared with healthy controls
additional information
-
a form of MMP-7 containing an Glu to Gln mutation in the catalytic domain is catalytically inactive
additional information
-
allergen-challenged Mmp7-/- mice show less airway hyperreactivity and production of allergic inflammatory cytokines and higher expression of retinal dehydrogenase 1. Inhibition of retinal dehydrogenase 1 restores the asthma phenotype of Mmp7-/- mice and inhibits the responses of lung regulatory T cells, whereas exogenous administration of retinoic acid attenuates the asthma phenotype, overview
additional information
-
determination of MMP-7 181A/G polymorphisms involved in colorectal cancer, the MMP-3 5A allele is involved in the progression of adenoma to cancer, overview
additional information
-
overexpression of MMP-7, and knocked-down using small inhibitory RNAs
additional information
-
MMP-7 tethered to cancer cell surface via cholesterol sulfate degrades fibronectin and laminin-332 coated on a culture plate
additional information
-
generation of MMP-7 pro-domain mutants lacking the N-terminal linker of the pro-domain (DELTAN, residues 9-79), the C-terminal linker (DELTAC, residues 1-73), or both (DELTANC, residues 9-73), secondary structure homology modeling analysis. Mutant DELTANC retains the triple alpha-helical structure
additional information
generation of mutant MMP-7(29,33,51,55/M2)DELTAC3, a variant of MMP-7 lacking affinity for cell surface cholesterol sulfate (CS)
additional information
MMP-7 siRNA-mediated knockdown and immunoneutralization of MMP-7 in OE33 cells causes increased migration and invasion in response to conditioned media of myofibroblasts
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
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
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
-
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
-
MMP-7-deficient cells do not show activation of Notch-1, which can be restored by recombinant MMP-7, phenotype, overview
-
additional information
-
MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, 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 gene knockout or knockdown of MMP-7 by RNA interference, results in attenuation of hypertension and stops development of cardiac hypertrophy in spontaneously hypertensive rats, and in decreased levels of myocardial ADAM-12 mRNA
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
purified enzyme with or without heparin and cholesterol sulfate, 10 min, 10-40% activity remaining, overview
69 - 76
-
50% of the activity is lost upon incubation at 69°C for 10 min, activity decreases to zero as temperature is raised to 76°C
additional information
additional information
in thermal incubation of the enzyme at 50-70°C, heparin increases the relative activity (the ratio of kcat/Km of MMP-7 with incubation to that without it), while cholesterol sulfate decreases the relative activity
additional information
-
in thermal incubation of the enzyme at 50-70°C, heparin increases the relative activity (the ratio of kcat/Km of MMP-7 with incubation to that without it), while cholesterol sulfate decreases the relative activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion protein of glutathione S-transferase and human promatrilysin expressed in Escherichia coli, further activation to matrilysin
-
inactive zymogen is activated: by 4-aminophenylmercuric acetate, yielding an intermediate form of 21000 MW and an active species of 19000 MW, by stromelysin 1 in a single-step mechanism
-
latent precursor purified from transfected mouse myeloma cell conditioned medium, activation by 4-aminophenylmercuric acetate, trypsin and incubation at elevated temperatures
-
recombinant enzyme
recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies, after solubilization and refolding, by gel filtration
recombinant His-tagged wild-type full-length, His-tagged deletion mutants, and His-tagged MMP-7 pro-domain by nickel affinity chromatography
-
recombinant solubilized and refolded enzyme from Escherichia coli strain BL21(DE3) inclusion bodies by ammonium sulfate fractionation and heparin affinity chromatography
recombinant wild-type and mutant matrilysins, after solubilization from Escherichia coli strain BL21 inclusion bodies, by cation exchange chromatography and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, overexpression in Escherichia coli strain BL21(DE3) in inclusion bodies
expression of wild-type and mutant matrilysins in Escherichia coli strain BL21 in inclusion bodies
-
MMP7 gene, DNA and amino acid sequence determination and analysis, genotyping, sequence comparison and phylogenetic analysis, overview
-
quantitative real-time RT-PCR analysis of MMP-7 in different endometriosis samples
-
recombinant expression of the enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
recombinant expression of wild-type full-length, and deletion mutants, as well as isolated MMP-7 pro-domain as His-tagged proteins
-
wild-type and mutant matrylysin cDNA in plasmid pUN121 expressed in Escherichia coli BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
1,25-dihydroxyvitamin D3, i.e. 1, 25(OH)2D3, significantly reduces the MMP-7 and MMP-9 and increases the TIMP-1 inhibitor level in Mycobacterium tuberculosis antigen stimulated and unstimulated mononuclear cell cultures of pulmonary tunerculosis patients as compared to healthy persons
-
andrographolide diminishes the activity and the mRNA and protein levels of MMP-7, but not MMP-2 or MMP-9. The downregulation of MMP-7 appears to be via the inactivation of activator protein-1, AP-1, overview
-
dominant negative insulin-like growth factor-I receptor, i.e. IGF-IR/dn, suppresses MMP-7 expression in invasive subcutaneous tumors. IGF-stimulated secretion of matrilysin and IGF-IR/dn blocks IGF-mediated matrilysin induction in three gastrointestinal cancers, overview
-
expression of MMP-7 is associated with tumour N stage and neural invasion in gastric cancer. Expression of MMP-7 or TIMP-1 alone cannot serve as an indicator of patient prognosis. Coexpression of MMP-7 and TIMP-1 is an independent predictive factor of overall survival in patients with gastric cancer
expression of MMP-7 is downregulated by tamoxifen and 5-fluorouracil in combination in HT-29 cells
-
fibulin-5 downregulates MMP-7, suppression of fibulin-5, as well as deletion of its RGD motif, induces MMP-7 expression in lung. Suppression of MMP-7 expression by fibulin-5 is mediated by an integrin-binding RGD motif via the extracellular signal-regulated kinase pathway
-
Helicobacter pylori infection upregulates the expression of matrix metalloproteinases, involved in chronic inflammation, ulceration, and cancer development
-
Helicobacter pylori stimulates expression of MMP-7 in gastric epithelial cells in vitro
inhibition of hyaluronan synthases HAS2 and HAS3 highly decreases MMP-7 expression and activity in SW620 cells
MMP-7 expression is induced in te epidermis by physiological processes such as wound healing, but also malignant transformation of epidermal cells
-
MMP-7 is highly expressed in patients with ulcerative colitis. IL-1b, IL-4, IL-13, TNFalpha, or lipopolysaccharide enhance MMP-7 expression in human colonic epithelial cells
MMP7 is upregulated by oxaliplatin in colon cancer cell lines. FasL expression is also upregulated by oxaliplatin treatment but decreased in the plasma membrane of resistant cells
-
Mycobacterium tuberculosis infection and its antigen cause an increase in MMP-7 expression in mononuclear cell cultures of pulmonary tunerculosis patients as compared to healthy persons untreated with 1,25-dihydroxyvitamin D3
-
no apparent regulation of the expression of MMP-7 by either tumor necrosis factor or enamel matrix derivative
-
possibly SFRP5 downregulation upregulates MMP-7 via the noncanonical Wnt pathway, overview
-
ROS and MMP-7 levels are upregulated in human pharyngeal epithelial cells following acid exposure. ERK/c-Jun signaling regulates the expression of MMP-7 and the degradation of E-cadherin
serum MMP-7 is increased in diabetic renal disease and diabetic diastolic dysfunction
-
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
the enzyme expression is increased in epithelium by bacterial infection, inflammation, fibrosis, and in a lot of carcinomas
TIMP-1 from gingival and dermal fibroblasts forms complexes with MMP-7 and inhibits its expression and activity. TGF-1beta mediates the secretion of MMP-7, but TGF-1beta inhibits MMP-7 expression. The MMP-7 gene has three TGF-beta1 inhibitory element, TIE, sites
-
YAP, EGFR, integrin-alpha2beta1 and MRLC produce a positive feedback loop that enhances MMP-7 expression. Stiff substrates enhance colorectal cancer cell viability by upregulating MMP-7 expression through a positive feedback loop
-
yes-associated protein (YAP) knockdown decreases MMP-7 expression. Treatment with inhibitors of epidermal growth factor receptor (EGFR) and myosin regulatory light chain (MRLC) and integrin-alpha2 or integrin-beta1 knockdown downregulate MMP-7 expression
-
Helicobacter pylori stimulates expression of MMP-7 in gastric epithelial cells in vitro
-
Helicobacter pylori stimulates expression of MMP-7 in gastric epithelial cells in vitro
-
-
the enzyme expression is increased in epithelium by bacterial infection, inflammation, fibrosis, and in a lot of carcinomas
the enzyme expression is increased in epithelium by bacterial infection, inflammation, fibrosis, and in a lot of carcinomas
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies through solubilization by 8 M urea, followed by anion exchange chromatography and dilution to 6 M urea, refolding in 6 M urea, 20 mM Tris-HCl, 10 mM CaCl2, and 100 mM NaCl, pH 7.5, after refolding dialysis in the same buffer with 10 mM ZnCl2, ultrafiltration, overview
recombinant enzyme, solubilization from Escherichia coli strain BL21(DE3) inclusion bodies by 6 M guanidine HCl, and refolded with 1 M L-arginine
recombinant MMP-7 from Escherichia coli strain BL21(DE3) inclusion bodies, solubilization and refolding at 1 M L-arginine
-
recombinant wild-type and mutant matrilysins from Escherichia coli strain BL21 inclusion bodies dialyzed in 8 M urea containing 50 mM Tris, pH 7.4, 50 mM NaCl, 10 mM CaCl2, 0.1 mM zinc acetate, 0.05% Brij-35, 0.02% NaN3, and 0.01% Triton X-100, followed by gel filtration
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
drug development
medicine
pharmacology
analysis
-
method to localize enzyme activity within tissues by selective degradation of crosslinked carboxymethylated transferrin on polyethylene films
analysis
-
use of substrate PB-M7vis as a proteolytic beacon and optical molecular imaging contrast reagent for in vivo detection of enzyme activity
diagnostics
-
elevated MMP-7 levels correlate with lymph node invasion and can be predictive for a shorter survival of cancer patients of 2-5 years, elevations of MMP-7 serum levels in the Helicobacter pylori-infected gastric cancer patients can serve as potential biomarker to correlate with poor survival
diagnostics
-
preoperative circulating MMP-7 levels in serum samples of patients with clinically localized prostate cancer have prognostic value, elevated serum matrix metalloproteinase 7 levels predict poor prognosis after radical prostatectomy, overview
diagnostics
-
clinical utility of circulating MMP-7, CC chemokine ligand 18, and CC chemokine ligand 11 as markers for diagnosis of epithelial ovarian cancer, detection method validation, overview
diagnostics
-
MMP-7 is a potential biomarker of intrinsic cisplatin sensitivity, ICS, which cisplatin treatment outcome in cancer therapy for advanced head and neck squamous cell carcinomas, overview
diagnostics
-
associated expression of metalloproteinase-1, metalloproteinase-7 and VEGF in colorectal adenocarcinoma is related to the incidence of disease recurrence
diagnostics
-
MMP-7 overexpression is an independent prognostic marker in gastric cancer
diagnostics
-
high MMP-7 expression is associated with a worse overall survival of patients with acinic cell carcinoma, while low MMP-7 expression is associated with worse disease-specific survival of patients with acinic cell carcinoma
diagnostics
-
MMP-7 immunohistochemistry may be a valuable aid for identification of the cell proliferation center in oral carcinoma in situ and dysplasia
diagnostics
-
the serum MMP-7 can be a diagnostic marker for cholangiocarcinoma, since its level is significantly higher in the patients with cholangiocarcinoma compared to benign biliary tract disease patients. The detection of the serum MMP-7 level is reasonably accurate in differentiating cholangiocarcinoma from benign biliary tract disease patients
diagnostics
-
usefulness of the combination of fecal cyclooxygenase 2, COX-2, mRNA and MMP-7 mRNA assays as a marker of colorectal cancer, evaluation of the feces screening method, overview
diagnostics
the enzyme is a potential marker for diagnosis of colorectal cancer
diagnostics
matrix metalloproteinase 7 is a useful marker for 5-fluorouracil-based adjuvant chemotherapy in stage II and stage III colorectal cancer patients
diagnostics
the enzyme MMP-7 may be a prognostic factor for disease-free survival in men with rectal cancer without distant metastasis
diagnostics
matrix metalloproteinase-7 (MMP-7) is an early and valuable biomarker for predicting severe acute kidney injury (AKI) and poor outcomes in patients after cardiac surgery
drug development
-
andrographolide is a chemotherapeutic agent due to its ability of inhibiting tumor cell proliferation and inflammation by e.g. supprressing MMP-7
drug development
matrilysin is an ideal biological target to developl inhibitors because it is overexpressed in malignant tumour cells
medicine
-
matrilysin is overexpressed in cancer cells of variuos organs including prostate, colorectum, brain, and stomach, important role in tumor invasion and metastasis
medicine
-
developing and searching for effective inhibitors of matrilysin for cancer diagnosis and therapy
medicine
-
overexpression of enzyme correlates with breast cancer in vitro invasiveness, enzyme may promote invasion by increasing the secretion and activation of matrix metalloproteinases proMMP-2 and pro-MMP-9
medicine
-
enzyme is involved in cell dissociation and the subsequent invasion of pancreatic cancer cells. It induces the disruption of tight junction structure and forms a positive feedback loop with activation of the epidermal growth factor receptor mediated MEK-ERK signalling pathway
medicine
MMP-7 promotes tolerance of incompatibel allografts and may help in development of strategies to improve long-term graft outcome in transplantation
medicine
serum matrilysin level predicts recurrence in curatively resected colorectal cancer patients. Patients with matrilysin level higher than the median 4.3 ng/ml are more likely to relapse. Median time to progression in relapsed patients is 8 months if matrilysin is above 4.3 ng/ml and 18 months if matrilysin is below 4.3 ng/ml. Node-negative patients with low matrilysin level have a predicted probability of relapse-free survival at 4 years of 88%; if the matrilysin level is higher than the median value, this probability is 77%
medicine
-
induction of specific natural killer cells using monocyte-derived dendritic cells electroporated with MMP-7-mRNA. The induced CTLs elicit an antigen-specific and HLA-restricted cytolytic activity against tumor cells endogenously expressing the MMP-7 protein. MMP-7-specific natural killer cells could be induced using peripheral blood mononuclear cells from a patient with acute lymphoblastic leukemia capable of recognizing the autologous leukemic blasts while sparing nonmalignant cells
medicine
MMP-7 genetic polymorphisms are significant determinants of survival among Chinese women with breast cancer
medicine
-
among patients with pT3 rectosigmoid cancer, fortyfive percent of the rectosigmoid cancers show strong expression of MMP-7. Membranous or cytoplasmic beta-catenin expression is significantly related to E-cadherin and MMP-7 expression. No significant association is seen between E-cadherin, beta-catenin, or MMP-7 expression and some clinicopathologic features
medicine
MMP-7 is highly expressed in patients with ulcerative colitis. IL-1b, IL-4, IL-13, TNFalpha, or lipopolysaccharide enhance MMP-7 expression in human colonic epithelial cells
medicine
Newcastle disease virus infection in oral cancer cells results in migration inhibition by a reduction in levels of MMP-7. Overexpression of MMP-7 reverses the inhibitory effect of Newcastle disease virus mediated migration. Newcastle disease virus dysregulates Wnt/beta-catenin by down-regulation of p-Akt and p-GSK3beta leading to degradation of beta-catenin. The infection leads to a reduction in cytoplasmic and nuclear levels of beta-catenin
medicine
expression of MMP-7 is associated with tumour N stage and neural invasion in gastric cancer. Expression of MMP-7 or TIMP-1 alone cannot serve as an indicator of patient prognosis. Coexpression of MMP-7 and TIMP-1 is an independent predictive factor of overall survival in patients with gastric cancer
medicine
in gefitinib-resistant cancer stem cells, MMP-7 mediates the shedding of transmembrane glycoprotein MUC-1 to release a cryptic oncogenic nucleolar shuttle, MUC-1 C-ter, which can mediate the nucleolar translocation of p53
medicine
digestion of the perlecan-semaphorin 3A-plexin A1-neuropilin-1 complex of prostate cancer cells with MMP-7 destabilizes cell-cell junctions in microtumors. MMP-7 is involved in prostat cancer cell transition to a dyscohesive, migratory phenotype
medicine
subjects with an reflux symptom index score of 13 or higher shows a significant increase of pepsin and MMP-7 activity in saliva. The sensitivity and specificity of MMP-7 for predicting the possibility of an reflux symptome index of 13 or more is higher than that of pepsin
medicine
degradation of E-cadherin after human mucosal cells are exposed to acid is caused by an increase in the expression of MMP-7 via the ROS/ERK/c-Jun pathway, a mechanism associated with the development of laryngopharyngeal reflux disease
pharmacology
MMP-7 is an important target for antimetastasis therapy of colorectal cancer because it is a strong proteolytic factor secreted from the cancer cell itself and it induces tumor angiogenesis
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
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