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Information on EC 3.4.24.23 - matrilysin and Organism(s) Homo sapiens and UniProt Accession P09237

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.23 matrilysin
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P09237 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Cleavage of Ala14-/-Leu and Tyr16-/-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I)
Synonyms
mmp-7, matrilysin, matrix metalloproteinase-7, matrix metalloproteinase 7, matrin, pump-1, matrix metallopeptidase 7, metalloproteinase-7, matrilysin-1, mmp 7, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
matrilysin
-
matrilysin 1
-
matrilysin-1
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Matrix metalloproteinase 7
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matrix-metalloproteinase-7
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cyclic matrix metalloproteinase
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human matrix metalloproteinase 7
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matrilysin
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matrilysin-1
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Matrin
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matrix metalloprotease-7
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Matrix metalloproteinase 7
Matrix metalloproteinase pump 1
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-
-
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Matrix metalloproteinase-7
metalloproteinase-7
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MMP
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-
-
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MMP 7
-
-
-
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Proteinase, metallo-, pump-1
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-
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Proteinase, PUMP-1
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-
-
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PUMP
-
-
-
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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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-
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Uterine metalloproteinase
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-
-
-
additional information
the enzyme belongs to the zinc-dependent endopeptidases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
141256-52-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
7-amino-4-methylcoumaryl-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
fluorescence-labeled substrate
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
?
fibronecin + H2O
?
show the reaction diagram
pericellular proteolysis
-
-
?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
show the reaction diagram
-
-
-
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
show the reaction diagram
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
insulin-like growth factor binding protein-5 + H2O
?
show the reaction diagram
kappa-casein + H2O
?
show the reaction diagram
-
-
-
?
laminin-332 + H2O
?
show the reaction diagram
pericellular proteolysis
-
-
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
show the reaction diagram
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
-
-
?
laminin-5/laminin-332 + H2O
90 kDa beta3 chain fragment + ?
show the reaction diagram
i.e. LN5, specific proteolysis by MMP7 in the beta3 chain at Ala515-Ile516, overview
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
perlecan + H2O
?
show the reaction diagram
(7-methoxy-coumarin-4-yl)acetyl-Ala-Pro-Lys-2,4-dinitrophenol + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg amide + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg amide + H2O
?
show the reaction diagram
-
-
-
-
?
(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
?
show the reaction diagram
(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
?
show the reaction diagram
-
MOCAc-PLGL(Dpa)AR
-
?
(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
?
show the reaction diagram
-
MOCAc-PLGL(Dpa)AR
-
?
(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
?
show the reaction diagram
-
-
-
-
?
(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
show the reaction diagram
-
-
-
-
?
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser + H2O
?
show the reaction diagram
-
optimized fluorogenic substrate
-
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
7-methoxycoumarin-4acetyl-PLG + ?
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
?
show the reaction diagram
-
-
-
?
aggrecan + H2O
?
show the reaction diagram
-
-
-
?
alpha1PI + H2O
?
show the reaction diagram
-
protein, inhibitor of elastase, inactivation by cleavage of Pro357-Met358 peptide bond of its reactive centre
-
-
?
annexin II + H2O
?
show the reaction diagram
-
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
-
-
?
Azocoll + H2O
?
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
C-type lectin domain family 3 member A + H2O
?
show the reaction diagram
-
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
-
-
?
cartilage + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
collagen type IV + H2O
?
show the reaction diagram
-
-
-
?
Cy5.5-M7 peptide + H2O
?
show the reaction diagram
-
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
-
-
?
dansyl-PLALWAR + H2O
?
show the reaction diagram
-
synthetic fluorescent peptide
-
?
decorin + H2O
transforming growth factor-beta + ?
show the reaction diagram
-
-
-
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
show the reaction diagram
-
matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
-
-
?
Elastin + H2O
?
show the reaction diagram
elastin + H2O
elastin peptides
show the reaction diagram
FasL + H2O
sFasL + ?
show the reaction diagram
-
human and murine FasL
-
?
fibrin + H2O
fibrin fragments + ?
show the reaction diagram
-
-
-
?
fibronactin + H2O
fibronectin peptide fragments
show the reaction diagram
-
-
MWs of 30 to 175 kDa
-
?
Fibronectin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln + H2O
?
show the reaction diagram
-
-
-
-
?
IGFBP-3 + H2O
?
show the reaction diagram
kappa-casein + H2O
?
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
Laminin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
laminin-332 + H2O
?
show the reaction diagram
N-cadherin + H2O
?
show the reaction diagram
osteopontin + H2O
?
show the reaction diagram
-
-
-
?
Oxidized alpha1PI + H2O
?
show the reaction diagram
-
cleavage of Phe352-Leu353 bond
-
-
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
show the reaction diagram
-
i.e. procryptdins
-
-
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
show the reaction diagram
Pro-matrix metalloproteinase 1 + H2O
?
show the reaction diagram
-
activation by specific cleavage at the Gln80-Phe81 bond
-
-
?
proADAM28s + H2O
ADAM28s + propeptide
show the reaction diagram
-
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
-
-
?
Proteoglycan + H2O
?
show the reaction diagram
syndecan-2 + H2O
?
show the reaction diagram
tumor-associated antigen 90K + H2O
?
show the reaction diagram
type IV basement membrane collagen + H2O
?
show the reaction diagram
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
show the reaction diagram
-
-
-
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
show the reaction diagram
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
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
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
-
-
?
insulin-like growth factor binding protein-5 + H2O
?
show the reaction diagram
in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
-
-
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
show the reaction diagram
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
-
-
?
perlecan + H2O
?
show the reaction diagram
i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
-
-
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
show the reaction diagram
-
matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
-
-
?
elastin + H2O
elastin peptides
show the reaction diagram
-
degradation
in the range of 500-8000 Da
-
?
fibronactin + H2O
fibronectin peptide fragments
show the reaction diagram
-
-
MWs of 30 to 175 kDa
-
?
Fibronectin + H2O
?
show the reaction diagram
-
also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
-
-
?
IGFBP-3 + H2O
?
show the reaction diagram
-
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
-
-
?
laminin-332 + H2O
?
show the reaction diagram
-
pericellular substrate
-
-
?
N-cadherin + H2O
?
show the reaction diagram
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
show the reaction diagram
-
i.e. procryptdins
-
-
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
show the reaction diagram
-
i.e. pro-human neutrophil peptide-1, in a cell-based assay system
-
-
?
syndecan-2 + H2O
?
show the reaction diagram
-
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
-
-
?
tumor-associated antigen 90K + H2O
?
show the reaction diagram
-
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4-phenyl-1,4-dihydropyridine-3,5-diyl)dimethanol
-
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
-
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%
Cholesterol sulfate
diethyl 1-phenoxy-4-(4-propylphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(2-methoxyphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(2-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(3-methoxyphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(3-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(4-methylphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(4-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(4-nitrophenyl)-1-phenoxy-1,4-dihydropyridine-3,5-dicarboxylate
-
diethyl 4-(4-propylphenyl)-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
-
EDTA
inhibits MMP-7-induced cell aggregation
methyl-beta-cyclodextrin
inhibits release of the HAI-1 fragment by MMP-7-catalyzed cleavage
MMPI-II
a small synthetic inhibitor of 514 Da
N-[3-[3,5-bis(hydroxymethyl)-1,4-dihydropyridin-4-yl]phenyl]acetamide
-
N-[3-[3,5-bis(hydroxymethyl)-1-phenoxy-1,4-dihydropyridin-4-yl]phenyl]acetamide
-
Sulfatide
associates with the enzyme at the cell surface and inhibits by 80%
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
TIMP-1
-
tissue inhibitors of metalloproteinase 1
TIMP-1
-
[(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
-
[4-(3,4,5-trimethoxyphenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
[4-(4-methoxyphenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
[4-(4-nitrophenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
[4-(4-propylphenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
(-)-5-hydroxypluviatolide
-
50% inhibition at 0.05 mM
(-)-catechin-3-gallate
(-)-epicatechin-3-gallate
(-)-epigallo-3-catechin gallate
-
-
(-)-epigallocatechin-3-gallate
-
inhibitory effect is increased on presence of 10 mM CaCl2, no interaction with Cl-
(-)-gallocatechin-3-gallate
(-)-haplomyrfolin
-
50% inhibition at 0.1 mM
(-)-hinokinin
-
50% inhibition at 0.1 mM
(-)-thujaplicatin-d3
-
50% inhibition at 0.08 mM
1,10-phenanthroline
-
-
1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)-piperazine-2-carboxylic acid
-
-
1-butanol
-
-
2-butanol
-
-
2-methyl-1-propanol
-
-
2-methyl-2-butanol
-
-
2-Methyl-2-propanol
-
-
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
batimastat
-
i.e. BB-94, BB-94 significantly reduces the amount of N-cadherin fragment produced in response to Fas-L
dimethyl sulfoxide
-
competitive inhibition
fibronectin 1
-
fibronectin 1, interacts with MMP-7
-
GM6001
-
a broad-spectrum MMP inhibitor
green tea catechin
-
-
-
Hydroxamate
-
-
KB-R7785
-
-
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-acetylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-amidopiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-cyclohexanecarbonylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-methylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-methylsulfonylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxylate hydrochloride
-
-
methyl 4-[4-(4-bromophenyl)thiazol-2-yl]-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxylate
-
-
N-alkylpiperazine
-
-
N-hydroxy-1,4-bis(4-methoxyphenylsulfonyl)piperazine-2-carboxamide
-
-
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-hexyl)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-acetylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-amidopiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzoylpiperazine-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-furoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-methylpiperazine-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-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxamide
-
-
N-hydroxy-4-[4-(4-bromophenyl)thiazol-2-yl]-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxamide
-
-
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
o-phenanthroline
-
-
R-94138
-
-
Sulfodiimine
-
-
thiorphan
-
-
TIMP-1
-
TIMP-3
-
TIMP-4
-
tissue inhibitor of metalloproteinases-4
-
TIMP3
-
tissue inhibitor of metalloproteinase-3, interacts with MMP-7
-
Tissue inhibitor of metalloproteinase-1
-
-
-
Zincov
-
-
ZnCl2
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Brij-35
activates MMP-7 in a broad concentration range, but inhibits at high concentration
heparin
porcine intestinal heparin, increases activity by decreasing the Km value, increases the enzyme's thermostability
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
-
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%
-
plasmin
-
-
-
Trypsin
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
0.026
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser
-
-
0.065
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
-
-
0.0079 - 0.024
dansyl-PLALWAR
0.81
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln
-
-
2
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
-
-
2.3
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln
-
-
7.3
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln
-
-
4.2
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln
-
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
5
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser
-
-
3.5
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
-
-
0.00051 - 6.08
dansyl-PLALWAR
0.472
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln
-
-
0.222
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
-
-
1.17
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln
-
-
2.47
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln
-
-
1.92
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln
-
-
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
Cholesterol sulfate
pH 7.5, 25°C
0.000027 - 0.000053
MMPI-II
0.000009 - 0.000064
TIMP-2
-
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
0.00144
(-)-catechin-3-gallate
-
pH 7.5, 25°C
0.00047
(-)-epicatechin-3-gallate
-
pH 7.5, 25°C
0.00165
(-)-epigallo-3-catechin gallate
-
pH 7.5, 25°C
0.00106
(-)-gallocatechin-3-gallate
-
pH 7.5, 25°C
670
1-butanol
-
pH 7.5, 25°C
11700
2-butanol
-
pH 7.5, 25°C
660
2-methyl-1-propanol
-
pH 7.5, 25°C
780
2-methyl-2-butanol
-
pH 7.5, 25°C
820
2-Methyl-2-propanol
-
pH 7.5, 25°C
590
dimethyl sulfoxide
-
pH 7.5, 25°C
0.0105
R-94138
-
pH 7.5, 25°C
0.0112 - 0.015
thiorphan
additional information
additional information
inhibition kinetic analysis
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
Brij-35
Homo sapiens
pH 7.5, 25°C
0.0006
cardiolipin
Homo sapiens
pH 8.0, 25°C
0.0007
Sulfatide
Homo sapiens
pH not specified in the publication, 37°C
0.00001
batimastat
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
assay at
6.5
-
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
7 - 8.5
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
-
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
4.5 - 9.5
-
-
5 - 9
-
maximal activity range of wild-type enzyme, and mutants Y193F and Y216F
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
assay at
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
-
37 - 55
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MMP-7 activity is higher in amnion from premature rupture of membranes compared to cesarean delivery, overview
Manually annotated by BRENDA team
primary tumors
Manually annotated by BRENDA team
early stage primary cancers, MMP-7 correlates with breast cancer development, overexpression of MMP-7 and ErbB4, overview
Manually annotated by BRENDA team
MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
Manually annotated by BRENDA team
sprouting, of different cancers, the endothelial enzyme is associated with CD34 and/or CD105 expression
Manually annotated by BRENDA team
expression and activity of MMP-7 in fetal membranes during premature rupture of membranes, immunohistochemic analysis, overview
Manually annotated by BRENDA team
highly variable MMP-7 expression in the glioma population
Manually annotated by BRENDA team
endometrial carcinoma-derived cell line
Manually annotated by BRENDA team
primary cutaneous and metastatic melanoma
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
invasive prostate cancer cells, high enzyme expression level
Manually annotated by BRENDA team
-
high MMP-7 expression level
Manually annotated by BRENDA team
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
Manually annotated by BRENDA team
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
Manually annotated by BRENDA team
-
immunohistochemic detection of MMP7 expression in biliary tract cancer, semi-quantitative RT-PCR and real-time RT-PCR, overview
Manually annotated by BRENDA team
-
from umbilical cord, MMP-7 quantification, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and interleukin IL-1beta
Manually annotated by BRENDA team
-
rectal carcinoma cell
Manually annotated by BRENDA team
-
overexpression of MMP-7
Manually annotated by BRENDA team
-
expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
Manually annotated by BRENDA team
-
low expression of MMP-7, which is induced by physiological processes such as wound healing, but also malignant transformation of epidermal cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
gingival
Manually annotated by BRENDA team
-
connective tissue
Manually annotated by BRENDA team
-
infiltrating
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
primary, monocyte-derived
Manually annotated by BRENDA team
-
frp, peripheral blood
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
MMP-7 expression analysis semiquantitatively by immunohistochemistry in prostate cancer. E1AF, an ets-oncogene family transcription factor, expression correlates with that of MMP-7
Manually annotated by BRENDA team
-
presence of enzyme in plasma of normal and azoospermic semen
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and interleukin IL-1beta
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme is expressed in the cytoplasm in colorectal cancer cells
Manually annotated by BRENDA team
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
-
Manually annotated by BRENDA team
-
wild-type MMP-7 Gly137 is distributed both in the membrane and cytosol fractions
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
-
the active-site tyrosyl residue, Tyr219, is conserved in all other MMPs
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP7_HUMAN
267
0
29677
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A15T
-
a naturally occuring polymorphism, not involved in liver cirrhosis
E198A
-
site-directed mutagenesis
E198C
-
site-directed mutagenesis
E198D
-
site-directed mutagenesis
E198Q
-
site-directed mutagenesis
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
R77H
-
a naturally occuring polymorphism, not involved in liver cirrhosis
V470M
-
a naturally occuring polymorphism, not involved in liver cirrhosis
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
purified enzyme with or without heparin and cholesterol sulfate, 10 min, 10-40% activity remaining, overview
70
purified enzyme, inactivation within 10 min
4
-
purified mutants are stable at
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
-
half of inactivation induced at 0.8 M
urea
-
half of inactivation induced at 2 M urea
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies, after solubilization and refolding, by gel filtration
recombinant solubilized and refolded enzyme from Escherichia coli strain BL21(DE3) inclusion bodies by ammonium sulfate fractionation and heparin affinity chromatography
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
-
recombinant His-tagged wild-type full-length, His-tagged deletion mutants, and His-tagged MMP-7 pro-domain by nickel affinity chromatography
-
recombinant wild-type and mutant matrilysins, after solubilization from Escherichia coli strain BL21 inclusion bodies, by cation exchange chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, overexpression in Escherichia coli strain BL21(DE3) in inclusion bodies
gene MMP7, quantitative real-time PCR enzyme expression analysis
gene MMP7, quantitative real-time PCR enzyme expression and analysis
overexpression of MMP-7 in Escherichia coli strain BL21(DE3)
quantitative real time PCR enzyme expression analysis
recombinant expression of the enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
semi- and quantitative MMP-7 expression analysis in SW620 cells
active MMP-7 lacking the propeptide expressed in Escherichia coli BL21(DE3)
-
catalytic domain expressed in Escherichia coli
-
expression analysis
-
expression in Escherichia coli
-
expression in Escherichia coli strain BL21(DE3) in inclusion bodies
-
expression of wild-type and mutant matrilysins in Escherichia coli strain BL21 in inclusion bodies
-
gene MMP7, enzyme expression analysis
-
MMP-7 genotyping
-
MMP-7 genotyping in healthy persons and liver cirrhosis patients, overview
-
MMP-7 genotyping, overview
-
prepromatrliysin cDNA expressed in Escherichia coli
-
quantitative real-time RT-PCR analysis of MMP-7 in different endometriosis samples
-
recombinant expression of wild-type full-length, and deletion mutants, as well as isolated MMP-7 pro-domain as His-tagged proteins
-
recombinant pro-matrilysin
-
wild-type and mutant matrylysin cDNA in plasmid pUN121 expressed in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inhibition of hyaluronan synthases HAS2 and HAS3 highly decreases MMP-7 expression and activity in SW620 cells
resveratrol inhibits MMP7 expression
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
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 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
-
IGF stimulates matrilysin expression in gastrointestinal cancer cell lines
-
infection by Mycobacterium tuberculosis upregulates MMP-7 expression
-
MMP-7 expression is induced in te epidermis by physiological processes such as wound healing, but also malignant transformation of epidermal 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
-
serum MMP-7 is increased in diabetic renal disease and diabetic diastolic dysfunction
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
drug development
matrilysin is an ideal biological target to developl inhibitors because it is overexpressed in malignant tumour cells
medicine
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
analysis
-
method to localize enzyme activity within tissues by selective degradation of crosslinked carboxymethylated transferrin on polyethylene films
diagnostics
drug development
-
andrographolide is a chemotherapeutic agent due to its ability of inhibiting tumor cell proliferation and inflammation by e.g. supprressing MMP-7
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Quantin, B.; Murphy, G.; Breathnach, R.
Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
Biochemistry
28
5327-5334
1989
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Netzel-Arnett, S.; Sang, Q.X.; Moore, W.G.I.; Navre, M.; Birkedal-Hansen, H.; van Wart, H.E.
Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin)
Biochemistry
32
6427-6432
1993
Homo sapiens
Manually annotated by BRENDA team
Zhang, Z.; Winyard, P.G.; Chidwick, K.; Murphy, G.; Wardell, M.; Carrell, R.W.; Blake, D.R.
Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin
Biochim. Biophys. Acta
1199
224-228
1994
Homo sapiens
Manually annotated by BRENDA team
Crabbe, T.; Smith, B.; O'Connell, J.; Docherty, A.
Human progelatinase A can be activated by matrilysin
FEBS Lett.
345
14-16
1994
Homo sapiens
Manually annotated by BRENDA team
Browner, M.F.; Smith, W.W.; Castelhano, A.L.
Matrilysin-inhibitor complexes: common themes among metalloproteases
Biochemistry
34
6602-6610
1995
Homo sapiens
Manually annotated by BRENDA team
Imai, K.; Yokohama, Y.; Nakanishi, I.; Ohuchi, E.; Fujii, Y.; Nakai, N.; Okada, Y.
Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
J. Biol. Chem.
270
6691-6697
1995
Homo sapiens
Manually annotated by BRENDA team
Welch, A.R.; Holman, C.M.; Browner, M.F.; Gehring, M.R.; Kan, C.C.; van Wart, H.E.
Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate
Arch. Biochem. Biophys.
324
59-64
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Crabbe, T.; Willenbrock, F.; Eaton, D.; Hynds, P.; Carne, A.F.; Murphy, G.; Docherty, A.J.P.
Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases
Biochemistry
31
8500-8507
1992
Homo sapiens
Manually annotated by BRENDA team
Marti, H.P.; McNeil, L.; Thomas, G.; Davies, M.; Lovett, D.H.
Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1
Biochem. J.
285
899-905
1992
Homo sapiens
Manually annotated by BRENDA team
Soler, D.; Nomizu, T.; Brown, W.E.; Shibata, Y.; Auld, D.S.
Matrilysin: expression, purification, and characterization
J. Protein Chem.
14
511-520
1995
Homo sapiens
Manually annotated by BRENDA team
Woessner, J.F.
Matrilysin
Methods Enzymol.
248
485-495
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Bini, A.; Wu, D.; Schnuer, J.; Kudryk, B.J.
Characterization of stromelysin 1 (MMP-3), matrilysin (MMP-7), and membrane type 1 matrix metalloproteinase (MT1-MMP) derived fibrin(ogen) fragments D-dimer and D-like monomer: NH2-terminal sequences of late-stage digest fragments
Biochemistry
38
13928-13936
1999
Homo sapiens
Manually annotated by BRENDA team
Vargo-Gogola, T.; Crawford, H.C.; Fingleton, B.; Matrisian, L.M.
Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand
Arch. Biochem. Biophys.
408
155-161
2002
Homo sapiens
Manually annotated by BRENDA team
Cha, J.; Auld, D.S.
Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
Biochemistry
36
16019-16024
1997
Homo sapiens
Manually annotated by BRENDA team
Windsor, L.J.; Steele, D.L.; LeBlanc, S.B.; Taylor, K.B.
Catalytic domain comparisons of human fibroblast-type collagenase, stromelysin-1, and matrilysin
Biochim. Biophys. Acta
1334
261-272
1997
Homo sapiens
Manually annotated by BRENDA team
Inouye, K.; Tanaka, H.; Oneda, H.
States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence
J. Biochem.
128
363-369
2000
Homo sapiens
Manually annotated by BRENDA team
Oneda, H.; Inouye, K.
Effects of dimethyl sulfoxide, temperature, and sodium chloride on the activity of human matrix metalloproteinase 7 (matrilysin)
J. Biochem.
128
785-791
2000
Homo sapiens
Manually annotated by BRENDA team
Oneda, H.; Inouye, K.
Interactions of human matrix metalloproteinase 7 (matrilysin) with the inhibitors thiorphan and R-94138
J. Biochem.
129
429-435
2001
Homo sapiens
Manually annotated by BRENDA team
Oneda, H.; Shiihara, M.; Inouye, K.
Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinase 7 (Matrilysin)
J. Biochem.
133
571-576
2003
Homo sapiens
Manually annotated by BRENDA team
Yu, W.H.; Woessner, J.F.Jr.
Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
J. Biol. Chem.
275
4183-4191
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Agnihotri, R.; Crawford, H.C.; Haro, H.; Matrisian, L.M.; Havrda, M.C.; Liaw, L.
Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin)
J. Biol. Chem.
276
28261-28267
2001
Homo sapiens
Manually annotated by BRENDA team
Cheng, M.; De, B.; Pikul, S.; Almstead, N.G.; Natchus, M.G.; Anastasio, M.V.; McPhail, S.J.; Snider, C.E.; Taiwo, Y.O.; Chen, L.; Dunaway, C.M.; Gu, F.; Dowty, M.E.; Mieling, G.E.; Janusz, M.J.; Wang-Weigand, S.
Design and synthesis of piperazine-based matrix metalloproteinase inhibitors
J. Med. Chem.
43
369-380
2000
Homo sapiens
Manually annotated by BRENDA team
Mochizuki, S.; Shimoda, M.; Shiomi, T.; Fujii, Y.; Okada, Y.
ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3
Biochem. Biophys. Res. Commun.
315
79-84
2004
Homo sapiens
Manually annotated by BRENDA team
Muta, Y.; Oneda, H.; Inouye, K.
Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues
Biochem. J.
386
263-270
2005
Homo sapiens
Manually annotated by BRENDA team
Muta, Y.; Oneda, H.; Inouye, K.
Inhibitory effects of alcohols on the activity of human matrix metalloproteinase 7 (matrilysin)
Biosci. Biotechnol. Biochem.
68
2649-2652
2004
Homo sapiens
Manually annotated by BRENDA team
Wang, F.; Reierstad, S.; Fishman, D.A.
Matrilysin over-expression in MCF-7 cells enhances cellular invasiveness and pro-gelatinase activation
Cancer Lett.
236
292-301
2006
Homo sapiens
Manually annotated by BRENDA team
Miyamoto, S.; Yano, K.; Sugimoto, S.; Ishii, G.; Hasebe, T.; Endoh, Y.; Kodama, K.; Goya, M.; Chiba, T.; Ochiai, A.
Matrix metalloproteinase-7 facilitates insulin-like growth factor bioavailability through its proteinase activity on insulin-like growth factor binding protein 3
Cancer Res.
64
665-671
2004
Homo sapiens
Manually annotated by BRENDA team
Harrell, P.C.; McCawley, L.J.; Fingleton, B.; McIntyre, J.O.; Matrisian, L.M.
Proliferative effects of apical, but not basal, matrix metalloproteinase-7 activity in polarized MDCK cells
Exp. Cell Res.
303
308-320
2005
Homo sapiens
Manually annotated by BRENDA team
Riccioli, A.; Dal Secco, V.; De Cesaris, P.; Starace, D.; Gandini, L.; Lenzi, A.; Dondero, F.; Padula, F.; Filippini, A.; Ziparo, E.
Presence of membrane and soluble forms of Fas ligand and of matrilysin (MMP-7) activity in normal and abnormal human semen
Hum. Reprod.
20
2814-2820
2005
Homo sapiens
Manually annotated by BRENDA team
Muta, Y.; Oyama, S.; Umezawa, T.; Shimada, M.; Inouye, K.
Inhibitory effects of lignans on the activity of human matrix metalloproteinase 7 (matrilysin)
J. Agric. Food Chem.
52
5888-5894
2004
Homo sapiens
Manually annotated by BRENDA team
Yamamoto, K.; Higashi, S.; Kioi, M.; Tsunezumi, J.; Honke, K.; Miyazaki, K.
Binding of active matrilysin to cell surface cholesterol sulfate is essential for its membrane-associated proteolytic action and induction of homotypic cell adhesion
J. Biol. Chem.
281
9170-9180
2006
Homo sapiens
Manually annotated by BRENDA team
Tan, X.; Egami, H.; Abe, M.; Nozawa, F.; Hirota, M.; Ogawa, M.
Involvement of MMP-7 in invasion of pancreatic cancer cells through activation of the EGFR mediated MEK-ERK signal transduction pathway
J. Clin. Pathol.
58
1242-1248
2005
Homo sapiens
Manually annotated by BRENDA team
Nemori, R.; Yamamoto, M.; Kataoka, F.; Hashimoto, G.; Arakatsu, H.; Shiomi, T.; Okada, Y.
Development of in situ zymography to localize active matrix metalloproteinase-7 (matrilysin-1)
J. Histochem. Cytochem.
53
1227-1234
2005
Homo sapiens
Manually annotated by BRENDA team
Bilousova, T.V.; Rusakov, D.A.; Ethell, D.W.; Ethell, I.M.
Matrix metalloproteinase-7 disrupts dendritic spines in hippocampal neurons through NMDA receptor activation
J. Neurochem.
97
44-56
2006
Homo sapiens
Manually annotated by BRENDA team
Shiomi, T.; Inoki, I.; Kataoka, F.; Ohtsuka, T.; Hashimoto, G.; Nemori, R.; Okada, Y.
Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151
Lab. Invest.
85
1489-1506
2005
Homo sapiens
Manually annotated by BRENDA team
Salmela, M.T.; Pender, S.L.; Karjalainen-Lindsberg, M.L.; Puolakkainen, P.; Macdonald, T.T.; Saarialho-Kere, U.
Collagenase-1 (MMP-1), matrilysin-1 (MMP-7), and stromelysin-2 (MMP-10) are expressed by migrating enterocytes during intestinal wound healing
Scand. J. Gastroenterol.
39
1095-1104
2004
Homo sapiens
Manually annotated by BRENDA team
Kawasaki, K.; Kawakami, T.; Watabe, H.; Itoh, F.; Mizoguchi, M.; Soma, Y.
Expression of matrilysin (matrix metalloproteinase-7) in primary cutaneous and metastatic melanoma
Br. J. Dermatol.
156
613-619
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Gershtein, E.S.; Korotkova, E.A.; Shcherbakov, A.M.; Prorokov, V.V.; Golovkov, D.A.; Kushlinskii, N.E.
Matrix metalloproteinases 7 and 9 and their types 1 and 4 tissue inhibitors in tumors and plasma of patients with colorectal cancer
Bull. Exp. Biol. Med.
143
459-462
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Remy, L.; Trespeuch, C.; Bachy, S.; Scoazec, J.Y.; Rousselle, P.
Matrilysin 1 influences colon carcinoma cell migration by cleavage of the laminin-5 beta3 chain
Cancer Res.
66
11228-11237
2006
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Lynch, C.C.; Vargo-Gogola, T.; Martin, M.D.; Fingleton, B.; Crawford, H.C.; Matrisian, L.M.
Matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor
Cancer Res.
67
6760-6767
2007
Homo sapiens (P09237), Mus musculus (Q10738), Mus musculus, Mus musculus C57BL/6 (Q10738)
Manually annotated by BRENDA team
Miyamoto, S.; Nakamura, M.; Yano, K.; Ishii, G.; Hasebe, T.; Endoh, Y.; Sangai, T.; Maeda, H.; Shi-Chuang, Z.; Chiba, T.; Ochiai, A.
Matrix metalloproteinase-7 triggers the matricrine action of insulin-like growth factor-II via proteinase activity on insulin-like growth factor binding protein 2 in the extracellular matrix
Cancer Sci.
98
685-691
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Berton, A.; Selvais, C.; Lemoine, P.; Henriet, P.; Courtoy, P.J.; Marbaix, E.; Emonard, H.
Binding of matrilysin-1 to human epithelial cells promotes its activity
Cell. Mol. Life Sci.
64
610-620
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Miyata, Y.; Iwata, T.; Ohba, K.; Kanda, S.; Nishikido, M.; Kanetake, H.
Expression of matrix metalloproteinase-7 on cancer cells and tissue endothelial cells in renal cell carcinoma: prognostic implications and clinical significance for invasion and metastasis
Clin. Cancer Res.
12
6998-7003
2006
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Kirimlioglu, H.; Kirimlioglu, V.; Yilmaz, S.; Sagir, V.; Coban, S.; Turkmen, E.; Hilmioglu, F.
Role of matrix metalloproteinase-7 in colorectal adenomas
Digest. Dis. Sci.
51
2068-2072
2006
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Gorodeski, G.I.
Estrogen decrease in tight junctional resistance involves matrix-metalloproteinase-7-mediated remodeling of occludin
Endocrinology
148
218-231
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Ganguly, B.; Banerjee, J.; Elegbede, A.I.; Klocke, D.J.; Mallik, S.; Srivastava, D.K.
Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes
FEBS Lett.
581
5723-5726
2007
Homo sapiens (P09237)
Manually annotated by BRENDA team
McCaig, C.; Duval, C.; Hemers, E.; Steele, I.; Pritchard, D.M.; Przemeck, S.; Dimaline, R.; Ahmed, S.; Bodger, K.; Kerrigan, D.D.; Wang, T.C.; Dockray, G.J.; Varro, A.
The role of matrix metalloproteinase-7 in redefining the gastric microenvironment in response to Helicobacter pylori
Gastroenterology
130
1754-1763
2006
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Patraki, E.; Cardillo, M.R.
Quantitative immunohistochemical analysis of matrilysin 1 (MMP-7) in various renal cell carcinoma subtypes
Int. J. Immunopathol. Pharmacol.
20
697-705
2008
Homo sapiens (P09237)
Manually annotated by BRENDA team
Liu, D.; Nakano, J.; Ishikawa, S.; Yokomise, H.; Ueno, M.; Kadota, K.; Urushihara, M.; Huang, C.L.
Overexpression of matrix metalloproteinase-7 (MMP-7) correlates with tumor proliferation, and a poor prognosis in non-small cell lung cancer
Lung Cancer
58
384-391
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Sier, C.F.; Hawinkels, L.J.; Zijlmans, H.J.; Zuidwijk, K.; de Jonge-Muller, E.S.; Ferreira, V.; Hanemaaijer, R.; Mulder-Stapel, A.A.; Kenter, G.G.; Verspaget, H.W.; Gorter, A.
Endothelium specific matrilysin (MMP-7) expression in human cancers
Matrix Biol.
27
267-271
2008
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Rome, C.; Arsaut, J.; Taris, C.; Couillaud, F.; Loiseau, H.
MMP-7 (matrilysin) expression in human brain tumors
Mol. Carcinog.
46
446-452
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Szklarczyk, A.; Conant, K.; Owens, D.F.; Ravin, R.; McKay, R.D.; Gerfen, C.
Matrix metalloproteinase-7 modulates synaptic vesicle recycling and induces atrophy of neuronal synapses
Neuroscience
149
87-98
2007
Homo sapiens (P09237)
Manually annotated by BRENDA team
Ito, T.K.; Ishii, G.; Chiba, H.; Ochiai, A.
The VEGF angiogenic switch of fibroblasts is regulated by MMP-7 from cancer cells
Oncogene
26
7194-7203
2007
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Ichikawa, Y.; Ishikawa, T.; Momiyama, N.; Kamiyama, M.; Sakurada, H.; Matsuyama, R.; Hasegawa, S.; Chishima, T.; Hamaguchi, Y.; Fujii, S.; Saito, S.; Kubota, K.; Hasegawa, S.; Ike, H.; Oki, S.; Shimada, H.
Matrilysin (MMP-7) degrades VE-cadherin and accelerates accumulation of beta-catenin in the nucleus of human umbilical vein endothelial cells
Oncol. Rep.
15
311-315
2006
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Ou, L.; Ma, J.; Zheng, X.; Chen, X.; Li, G.; Wu, H.
The expression and refolding of isotopically labeled recombinant matrilysin for NMR studies
Protein Expr. Purif.
47
367-373
2006
Homo sapiens (P09237)
Manually annotated by BRENDA team
Nishihara, S.; Someya, A.; Yonemoto, H.; Ota, A.; Itoh, S.; Nagaoka, I.; Takeda, S.
Evaluation of the expression and enzyme activity of matrix metalloproteinase-7 in fetal membranes during premature rupture of membranes at term in humans
Reprod. Sci.
15
156-165
2008
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Martinez-Fernandez, A.; Garcia-Albeniz, X.; Pineda, E.; Visa, L.; Gallego, R.; Codony-Servat, J.; Auge, J.M.; Longaron, R.; Gascon, P.; Lacy, A.; Castells, A.; Maurel, J.
Serum matrilysin levels predict outcome in curatively resected colorectal cancer patients
Ann. Surg. Oncol.
16
1412-1420
2009
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Yokoyama, Y.; Gruenebach, F.; Schmidt, S.M.; Heine, A.; Haentschel, M.; Stevanovic, S.; Rammensee, H.G.; Brossart, P.
Matrilysin (MMP-7) is a novel broadly expressed tumor antigen recognized by antigen-specific T cells
Clin. Cancer Res.
14
5503-5511
2008
Homo sapiens
Manually annotated by BRENDA team
Tsunezumi, J.; Yamamoto, K.; Higashi, S.; Miyazaki, K.
Matrilysin (matrix metalloprotease-7) cleaves membrane-bound annexin II and enhances binding of tissue-type plasminogen activator to cancer cell surfaces
FEBS J.
275
4810-4823
2008
Homo sapiens
Manually annotated by BRENDA team
Beeghly-Fadiel, A.; Shu, X.O.; Long, J.; Li, C.; Cai, Q.; Cai, H.; Gao, Y.T.; Zheng, W.
Genetic polymorphisms in the MMP-7 gene and breast cancer survival
Int. J. Cancer
124
208-214
2009
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Tsunezumi, J.; Higashi, S.; Miyazaki, K.
Matrilysin (MMP-7) cleaves C-type lectin domain family 3 member A (CLEC3A) on tumor cell surface and modulates its cell adhesion activity
J. Cell. Biochem.
106
693-702
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, H.; Huang, J.; Wu, B.; Zhou, Y.; Zhu, J.; Zhang, T.
Matrilysin inhibits proliferation and modulates sensitivity of lung cancer cells to FasL-mediated apoptosis
Med. Oncol.
25
419-430
2008
Homo sapiens
Manually annotated by BRENDA team
Liu, H.; Zhang, T.; Wu, B.; Huang, J.; Zhou, Y.; Zhu, J.
Chronic exposure to exogenous matrilysin induces chemoresistance and enhances Bcl-2 expression in A549 lung adenocarcinoma cells
Mol. Biol. Rep.
36
2099-2109
2008
Homo sapiens
Manually annotated by BRENDA team
Goswami, S.; Angkasekwinai, P.; Shan, M.; Greenlee, K.J.; Barranco, W.T.; Polikepahad, S.; Seryshev, A.; Song, L.Z.; Redding, D.; Singh, B.; Sur, S.; Woodruff, P.; Dong, C.; Corry, D.B.; Kheradmand, F.
Divergent functions for airway epithelial matrix metalloproteinase 7 and retinoic acid in experimental asthma
Nat. Immunol.
10
496-503
2009
Homo sapiens
Manually annotated by BRENDA team
Dilek, F.H.; Topak, N.; Aktepe, F.; Sahin, O.; Tuerel, K.S.; Sahin, D.A.; Dilek, O.N.
E-cadherin, beta-catenin adhesion complex and relation to matrilysin expression in pT3 rectosigmoid cancers
Pathol. Res. Pract.
204
809-815
2008
Homo sapiens
Manually annotated by BRENDA team
Dunn, K.M.; Lee, P.K.; Wilson, C.M.; Iida, J.; Wasiluk, K.R.; Hugger, M.; McCarthy, J.B.
Inhibition of hyaluronan synthases decreases matrix metalloproteinase-7 (MMP-7) expression and activity
Surgery
145
322-329
2009
Homo sapiens (P09237)
Manually annotated by BRENDA team
Gomes, E.G.; Juca, M.J.; de Menezes, H.L.; Nunes, B.L.; Costa, H.; Lima, F.d.e..O.; Matos, D.
Correlation between the immunohistochemical expressions of MMP-1, MMP-7 and VEGF and prognostic factors in colorectal adenocarcinoma
Acta Cir. Bras.
24
303-310
2009
Homo sapiens
Manually annotated by BRENDA team
Luukkaa, H.; Klemi, P.; Hirsimaeki, P.; Vahlberg, T.; Kivisaari, A.; Kaehaeri, V.M.; Grenman, R.
Matrix metalloproteinase (MMP)-7 in salivary gland cancer
Acta Oncol.
49
85-90
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, X.Y.; Demelash, A.; Kim, H.; Jensen-Taubman, S.; Dakir, e.l..H.; Ozbun, L.; Birrer, M.J.; Linnoila, R.I.
Matrilysin-1 mediates bronchiolization of alveoli, a potential premalignant change in lung cancer
Am. J. Pathol.
175
592-604
2009
Homo sapiens
Manually annotated by BRENDA team
Park, H.I.; Lee, S.; Ullah, A.; Cao, Q.; Sang, Q.X.
Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker
Anal. Biochem.
396
262-268
2010
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Maruta, S.; Sakai, H.; Kanda, S.; Hayashi, T.; Kanetake, H.; Miyata, Y.
E1AF expression is associated with extra-prostatic growth and matrix metalloproteinase-7 expression in prostate cancer
APMIS
117
791-796
2009
Homo sapiens
Manually annotated by BRENDA team
Ulmer, T.A.; Keeler, V.; Andre, S.; Gabius, H.J.; Loh, L.; Laferte, S.
The tumor-associated antigen 90K/Mac-2-binding protein secreted by human colon carcinoma cells enhances extracellular levels of promatrilysin and is a novel substrate of matrix metalloproteinases-2, -7 (matrilysin) and -9: Implications of proteolytic clea
Biochim. Biophys. Acta
1800
336-343
2010
Homo sapiens
Manually annotated by BRENDA team
Zhao, C.; Bu, X.; Zhang, N.; Wang, W.
Downregulation of SFRP5 expression and its inverse correlation with those of MMP-7 and MT1-MMP in gastric cancer
BMC Cancer
9
224
2009
Homo sapiens
Manually annotated by BRENDA team
Leelawat, K.; Sakchinabut, S.; Narong, S.; Wannaprasert, J.
Detection of serum MMP-7 and MMP-9 in cholangiocarcinoma patients: evaluation of diagnostic accuracy
BMC Gastroenterol.
9
30-38
2009
Homo sapiens
Manually annotated by BRENDA team
Hartmann-Petersen, S.; Tammi, R.H.; Tammi, M.I.; Kosma, V.M.
Depletion of cell surface CD44 in nonmelanoma skin tumours is associated with increased expression of matrix metalloproteinase 7
Br. J. Dermatol.
160
1251-1257
2009
Homo sapiens
Manually annotated by BRENDA team
Takai, T.; Kanaoka, S.; Yoshida, K.; Hamaya, Y.; Ikuma, M.; Miura, N.; Sugimura, H.; Kajimura, M.; Hishida, A.
Fecal cyclooxygenase 2 plus matrix metalloproteinase 7 mRNA assays as a marker for colorectal cancer screening
Cancer Epidemiol. Biomarkers Prev.
18
1888-1893
2009
Homo sapiens
Manually annotated by BRENDA team
Yue, W.; Sun, Q.; Landreneau, R.; Wu, C.; Siegfried, J.M.; Yu, J.; Zhang, L.
Fibulin-5 suppresses lung cancer invasion by inhibiting matrix metalloproteinase-7 expression
Cancer Res.
69
6339-6346
2009
Homo sapiens
Manually annotated by BRENDA team
Thiolloy, S.; Halpern, J.; Holt, G.E.; Schwartz, H.S.; Mundy, G.R.; Matrisian, L.M.; Lynch, C.C.
Osteoclast-derived matrix metalloproteinase-7, but not matrix metalloproteinase-9, contributes to tumor-induced osteolysis
Cancer Res.
69
6747-6755
2009
Homo sapiens
Manually annotated by BRENDA team
Adachi, Y.; Li, R.; Yamamoto, H.; Min, Y.; Piao, W.; Wang, Y.; Imsumran, A.; Li, H.; Arimura, Y.; Lee, C.T.; Imai, K.; Carbone, D.P.; Shinomura, Y.
Insulin-like growth factor-I receptor blockade reduces the invasiveness of gastrointestinal cancers via blocking production of matrilysin
Carcinogenesis
30
1305-1313
2009
Homo sapiens
Manually annotated by BRENDA team
Williams, H.; Johnson, J.L.; Jackson, C.L.; White, S.J.; George, S.J.
MMP-7 mediates cleavage of N-cadherin and promotes smooth muscle cell apoptosis
Cardiovasc. Res.
87
137-146
2010
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Manually annotated by BRENDA team
Shi, M.D.; Lin, H.H.; Chiang, T.A.; Tsai, L.Y.; Tsai, S.M.; Lee, Y.C.; Chen, J.H.
Andrographolide could inhibit human colorectal carcinoma Lovo cells migration and invasion via down-regulation of MMP-7 expression
Chem. Biol. Interact.
180
344-352
2009
Homo sapiens
Manually annotated by BRENDA team
Yi, Y.C.; Chou, P.T.; Chen, L.Y.; Kuo, W.H.; Ho, E.S.; Han, C.P.; Yang, S.F.
Matrix metalloproteinase-7 (MMP-7) polymorphism is a risk factor for endometrial cancer susceptibility
Clin. Chem. Lab. Med.
48
337-344
2010
Homo sapiens
Manually annotated by BRENDA team
Anand, S.P.; Selvaraj, P.
Effect of 1, 25 dihydroxyvitamin D(3) on matrix metalloproteinases MMP-7, MMP-9 and the inhibitor TIMP-1 in pulmonary tuberculosis
Clin. Immunol.
133
126-131
2009
Homo sapiens
Manually annotated by BRENDA team
Ban, C.R.; Twigg, S.M.; Franjic, B.; Brooks, B.A.; Celermajer, D.; Yue, D.K.; McLennan, S.V.
Serum MMP-7 is increased in diabetic renal disease and diabetic diastolic dysfunction
Diabetes Res. Clin. Pract.
87
335-341
2010
Homo sapiens
Manually annotated by BRENDA team
Yeh, Y.C.; Sheu, B.S.; Cheng, H.C.; Wang, Y.L.; Yang, H.B.; Wu, J.J.
Elevated serum matrix metalloproteinase-3 and -7 in H. pylori-related gastric cancer can be biomarkers correlating with a poor survival
Digest. Dis. Sci.
55
1649-1657
2010
Homo sapiens
Manually annotated by BRENDA team
Achyut, B.R.; Ghoshal, U.C.; Moorchung, N.; Mittal, B.
Transforming growth factor-B1 and matrix metalloproteinase-7 promoter variants induce risk for Helicobacter pylori-associated gastric precancerous lesions
DNA Cell Biol.
28
295-301
2009
Homo sapiens
Manually annotated by BRENDA team
Galewska, Z.; Romanowicz, L.; Jaworski, S.; Ba?kowski, E.
Matrix metalloproteinases, MMP-7 and MMP-26, in plasma and serum of control and preeclamptic umbilical cord blood
Eur. J. Obstet. Gynecol. Reprod. Biol.
150
152-156
2010
Homo sapiens
Manually annotated by BRENDA team
Luukkaa, H.; Klemi, P.; Leivo, I.; Maekitie, A.A.; Irish, J.; Gilbert, R.; Perez-Ordonez, B.; Hirsimaeki, P.; Vahlberg, T.; Kivisaari, A.; Kaehaeri, V.M.; Grenman, R.
Expression of matrix metalloproteinase-1, -7, -9, -13, Ki-67, and HER-2 in epithelial-myoepithelial salivary gland cancer
Head Neck
32
1019-1027
2009
Homo sapiens
Manually annotated by BRENDA team
Hung, T.M.; Chang, S.C.; Yu, W.H.; Wang, Y.W.; Huang, C.; Lu, S.C.; Lee, P.H.; Chang, M.F.
A novel nonsynonymous variant of matrix metalloproteinase-7 confers risk of liver cirrhosis
Hepatology
50
1184-1193
2009
Homo sapiens
Manually annotated by BRENDA team
Miyata, Y.; Sagara, Y.; Kanda, S.; Hayashi, T.; Kanetake, H.
Phosphorylated hepatocyte growth factor receptor/c-Met is associated with tumor growth and prognosis in patients with bladder cancer: correlation with matrix metalloproteinase-2 and -7 and E-cadherin
Hum. Pathol.
40
496-504
2009
Homo sapiens
Manually annotated by BRENDA team
Matsuzaki, S.; Maleysson, E.; Darcha, C.
Analysis of matrix metalloproteinase-7 expression in eutopic and ectopic endometrium samples from patients with different forms of endometriosis
Hum. Reprod.
25
742-750
2010
Homo sapiens
Manually annotated by BRENDA team
Szarvas, T.; Becker, M.; Vom Dorp, F.; Meschede, J.; Scherag, A.; Bankfalvi, A.; Reis, H.; Schmid, K.W.; Romics, I.; Ruebben, H.; Erguen, S.
Elevated serum matrix metalloproteinase 7 levels predict poor prognosis after radical prostatectomy
Int. J. Cancer
128
1486-1492
2010
Homo sapiens
Manually annotated by BRENDA team
Ra, H.J.; Harju-Baker, S.; Zhang, F.; Linhardt, R.J.; Wilson, C.L.; Parks, W.C.
Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans
J. Biol. Chem.
284
27924-27932
2009
Homo sapiens
Manually annotated by BRENDA team
Ryu, H.Y.; Lee, J.; Yang, S.; Park, H.; Choi, S.; Jung, K.C.; Lee, S.T.; Seong, J.K.; Han, I.O.; Oh, E.S.
Syndecan-2 functions as a docking receptor for pro-matrix metalloproteinase-7 in human colon cancer cells
J. Biol. Chem.
284
35692-35701
2009
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Wilson, C.L.; Schmidt, A.P.; Pirilae, E.; Valore, E.V.; Ferri, N.; Sorsa, T.; Ganz, T.; Parks, W.C.
Differential processing of alpha- and beta-defensin precursors by matrix metalloproteinase-7 (MMP-7)
J. Biol. Chem.
284
8301-8311
2009
Homo sapiens
Manually annotated by BRENDA team
Fang, Y.J.; Pan, Z.Z.; Li, L.R.; Lu, Z.H.; Zhang, L.Y.; Wan, D.S.
MMP7 expression regulated by endocrine therapy in ERbeta-positive colon cancer cells
J. Exp. Clin. Cancer Res.
28
132
2009
Homo sapiens
Manually annotated by BRENDA team
Rand, L.; Green, J.A.; Saraiva, L.; Friedland, J.S.; Elkington, P.T.
Matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade
J. Immunol.
182
5865-5872
2009
Homo sapiens
Manually annotated by BRENDA team
Kaner, R.J.; Santiago, F.; Crystal, R.G.
Up-regulation of alveolar macrophage matrix metalloproteinases in HIV1(+) smokers with early emphysema
J. Leukoc. Biol.
86
913-922
2009
Homo sapiens
Manually annotated by BRENDA team
Tilakaratne, W.M.; Kobayashi, T.; Ida-Yonemochi, H.; Swelam, W.; Yamazaki, M.; Mikami, T.; Alvarado, C.G.; Shahidul, A.M.; Maruyama, S.; Cheng, J.; Saku, T.
Matrix metalloproteinase 7 and perlecan in oral epithelial dysplasia and carcinoma in situ: an aid for histopathologic recognition of their cell proliferation centers
J. Oral Pathol. Med.
38
348-355
2009
Homo sapiens
Manually annotated by BRENDA team
Zeldich, E.; Koren, R.; Dard, M.; Weinberg, E.; Weinreb, M.; Nemcovsky, C.E.
Enamel matrix derivative induces the expression of tissue inhibitor of matrix metalloproteinase-3 in human gingival fibroblasts via extracellular signal-regulated kinase
J. Periodontal Res.
45
200-206
2010
Homo sapiens
Manually annotated by BRENDA team
Kitamura, T.; Biyajima, K.; Aoki, M.; Oshima, M.; Taketo, M.
Matrix metalloproteinase 7 is required for tumor formation, but dispensable for invasion and fibrosis in SMAD4-deficient intestinal adenocarcinomas
Lab. Invest.
89
98-105
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Zohny, S.F.; Fayed, S.T.
Clinical utility of circulating matrix metalloproteinase-7 (MMP-7), CC chemokine ligand 18 (CCL18) and CC chemokine ligand 11 (CCL11) as markers for diagnosis of epithelial ovarian cancer
Med. Oncol.
27
1246-1253
2009
Homo sapiens
Manually annotated by BRENDA team
Scherer, R.L.; VanSaun, M.N.; McIntyre, J.O.; Matrisian, L.M.
Optical imaging of matrix metalloproteinase-7 activity in vivo using a proteolytic nanobeacon
Mol. Imaging
7
118-131
2009
Homo sapiens
Manually annotated by BRENDA team
Ansell, A.; Jerhammar, F.; Ceder, R.; Grafstroem, R.; Grenman, R.; Roberg, K.
Matrix metalloproteinase-7 and -13 expression associate to cisplatin resistance in head and neck cancer cell lines
Oral Oncol.
45
866-871
2009
Homo sapiens
Manually annotated by BRENDA team
Souza Freitas, V.; Ferreira de Araujo, C.R.; Alves, P.M.; de Souza, L.B.; Galvao, H.C.; de Almeida Freitas, R.
Immunohistochemical expression of matrilysins (MMP-7 and MMP-26) in ameloblastomas and adenomatoid odontogenic tumors
Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod.
108
417-424
2009
Homo sapiens
Manually annotated by BRENDA team
Almendro, V.; Ametller, E.; Garcia-Recio, S.; Collazo, O.; Casas, I.; Auge, J.M.; Maurel, J.; Gascon, P.
The role of MMP7 and its cross-talk with the FAS/FASL system during the acquisition of chemoresistance to oxaliplatin
PLoS ONE
4
e4728
2009
Homo sapiens
Manually annotated by BRENDA team
Amir, M.; Romano, S.; Goldman, S.; Shalev, E.
Plexin-B1, glycodelin and MMP7 expression in the human fallopian tube and in the endometrium
Reprod. Biol. Endocrinol.
7
152
2009
Homo sapiens
Manually annotated by BRENDA team
Koskensalo, S.; Mrena, J.; Wiksten, J.P.; Nordling, S.; Kokkola, A.; Hagstroem, J.; Haglund, C.
MMP-7 overexpression is an independent prognostic marker in gastric cancer
Tumour Biol.
31
149-155
2010
Homo sapiens
Manually annotated by BRENDA team
Oka, T.; Yamamoto, H.; Sasaki, S.; Ii, M.; Hizaki, K.; Taniguchi, H.; Adachi, Y.; Imai, K.; Shinomura, Y.
Overexpression of beta3/gamma2 chains of laminin-5 and MMP7 in biliary cancer
World J. Gastroenterol.
15
3865-3873
2009
Homo sapiens
Manually annotated by BRENDA team
Ohtani, H.; Maeda, N.; Murawaki, Y.
Functional polymorphisms in the promoter regions of matrix metalloproteinase-2,-3,-7,-9 and TNF-alpha Genes, and the risk of colorectal neoplasm in Japanese
Yonago Acta Med.
52
47-56
2009
Homo sapiens
-
Manually annotated by BRENDA team
Choi, S.; Kim, J.Y.; Park, J.H.; Lee, S.T.; Han, I.O.; Oh, E.S.
The matrix metalloproteinase-7 regulates the extracellular shedding of syndecan-2 from colon cancer cells
Biochem. Biophys. Res. Commun.
417
1260-1264
2012
Homo sapiens
Manually annotated by BRENDA team
Heinz, A.; Taddese, S.; Sippl, W.; Neubert, R.H.; Schmelzer, C.E.
Insights into the degradation of human elastin by matrilysin-1
Biochimie
93
187-194
2011
Homo sapiens
Manually annotated by BRENDA team
Muta, Y.; Yasui, N.; Matsumiya, Y.; Kubo, M.; Inouye, K.
Expression in Escherichia coli, refolding, and purification of the recombinant mature form of human matrix metalloproteinase 7 (MMP-7)
Biosci. Biotechnol. Biochem.
74
2515-2517
2010
Homo sapiens
Manually annotated by BRENDA team
Miyake, T.; Yasukawa, K.; Inouye, K.
Analysis of the mechanism of inhibition of human matrix metalloproteinase 7 (MMP-7) activity by green tea catechins
Biosci. Biotechnol. Biochem.
75
1564-1569
2011
Homo sapiens
Manually annotated by BRENDA team
Muta, Y.; Inouye, K.
Tyr219 of human matrix metalloproteinase 7 is not critical for catalytic activity, but is involved in the broad pH-dependence of the activity
J. Biochem.
150
183-188
2011
Homo sapiens
Manually annotated by BRENDA team
Yamamoto, K.; Miyazaki, K.; Higashi, S.
Cholesterol sulfate alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin
J. Biol. Chem.
285
28862-28873
2010
Homo sapiens
Manually annotated by BRENDA team
Rath, T.; Roderfeld, M.; Halwe, J.M.; Tschuschner, A.; Roeb, E.; Graf, J.
Cellular sources of MMP-7, MMP-13 and MMP-28 in ulcerative colitis
Scand. J. Gastroenterol.
45
1186-1196
2010
Homo sapiens
Manually annotated by BRENDA team
Samukange, V.; Yasukawa, K.; Inouye, K.
Effects of heparin and cholesterol sulfate on the activity and stability of human matrix metalloproteinase 7
Biosci. Biotechnol. Biochem.
78
41-48
2014
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Tan, H.; Yan, H.; Song, X.
Design, synthesis and biological evaluation Of 3,9-diazatetraasteranes as novel matrilysin inhibitors
Chem. Biol. Drug Des.
82
567-578
2013
Homo sapiens (P09237)
Manually annotated by BRENDA team
Keles, D.; Arslan, B.; Terzi, C.; Tekmen, I.; Dursun, E.; Altungoz, O.; Oktay, G.
Expression and activity levels of matrix metalloproteinase-7 and in situ localization of caseinolytic activity in colorectal cancer
Clin. Biochem.
47
1265-1271
2014
Homo sapiens (P09237)
Manually annotated by BRENDA team
Yamamoto, K.; Miyazaki, K.; Higashi, S.
Pericellular proteolysis by matrix metalloproteinase-7 is differentially modulated by cholesterol sulfate, sulfatide, and cardiolipin
FEBS J.
281
3346-3356
2014
Homo sapiens (P09237)
Manually annotated by BRENDA team
Grindel, B.; Martinez, J.; Pennington, C.; Muldoon, M.; Stave, J.; Chung, L.; Farach-Carson, M.
Matrilysin/matrix metalloproteinase-7(MMP7) cleavage of perlecan/HSPG2 creates a molecular switch to alter prostate cancer cell behavior
Matrix Biol.
36
64-76
2014
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Huang, Y.; Yu, H.; Lei, H.; Xie, C.; Zhong, Y.
Matrix metalloproteinase 7 is a useful marker for 5-fluorouracil-based adjuvant chemotherapy in stage II and stage III colorectal cancer patients
Med. Oncol.
31
824
2014
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Fuksiewicz, M.; Kotowicz, B.; Rutkowski, A.; Kowalska, M.
The matrix metalloproteinase-7 and pro-enzyme of metalloproteinase-1 as a potential marker for patients with rectal cancer without distant metastasis
Tumor Biol.
36
3629-3635
2015
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Xiao, Z.; Chen, C.; Meng, T.; Zhang, W.; Zhou, Q.
Resveratrol attenuates renal injury and fibrosis by inhibiting transforming growth factor-beta pathway on matrix metalloproteinase 7
Exp. Biol. Med. (Maywood)
241
140-146
2016
Homo sapiens (P09237), Homo sapiens
Manually annotated by BRENDA team
Ishikawa, T.; Kimura, Y.; Hirano, H.; Higashi, S.
Matrix metalloproteinase-7 induces homotypic tumor cell aggregation via proteolytic cleavage of the membrane-bound Kunitz-type inhibitor HAI-1
J. Biol. Chem.
292
20769-20784
2017
Homo sapiens (P09237)
Manually annotated by BRENDA team
Fu, H.; Zhou, D.; Zhu, H.; Liao, J.; Lin, L.; Hong, X.; Hou, F.F.; Liu, Y.
Matrix metalloproteinase-7 protects against acute kidney injury by priming renal tubules for survival and regeneration
Kidney Int.
95
1167-1180
2019
Homo sapiens (P09237), Mus musculus (Q10738)
Manually annotated by BRENDA team
Nukuda, A.; Sasaki, C.; Ishihara, S.; Mizutani, T.; Nakamura, K.; Ayabe, T.; Kawabata, K.; Haga, H.
Stiff substrates increase YAP-signaling-mediated matrix metalloproteinase-7 expression
Oncogenesis
4
e165
2015
Homo sapiens
Manually annotated by BRENDA team
Garalla, H.M.; Lertkowit, N.; Tiszlavicz, L.; Reisz, Z.; Holmberg, C.; Beynon, R.; Simpson, D.; Varga, A.; Kumar, J.D.; Dodd, S.; Pritchard, D.M.; Moore, A.R.; Rosztoczy, A.I.; Wittman, T.; Simpson, A.; Dockray, G.J.; Varro, A.
Matrix metalloproteinase (MMP)-7 in Barrett's esophagus and esophageal adenocarcinoma expression, metabolism, and functional significance
Physiol. Rep.
6
e13683
2018
Homo sapiens (P09237)
Manually annotated by BRENDA team
Li, M.; Zhang, Y.; Tian, H.; Zheng, M.; Yang, M.; Fang, H.; Xie, Y.; Jin, J.
Nitro-based selective inhibitors against matrix metalloproteinase-7 over matrix metalloproteinase-1
RSC Adv.
5
104725-104732
2015
Homo sapiens (P09237)
-
Manually annotated by BRENDA team
Jang, B.; Yun, J.H.; Choi, S.; Park, J.; Shin, D.H.; Lee, S.T.; Lee, W.; Oh, E.S.
Tyrosine 51 residue of the syndecan-2 extracellular domain is involved in the interaction with and activation of pro-matrix metalloproteinase-7
Sci. Rep.
9
10625
2019
Homo sapiens
Manually annotated by BRENDA team
Prior, S.H.; Fulcher, Y.G.; Koppisetti, R.K.; Jurkevich, A.; Van Doren, S.R.
Charge-triggered membrane insertion of matrix metalloproteinase-7, supporter of innate immunity and tumors
Structure
23
2099-2110
2015
Homo sapiens (P09237)
Manually annotated by BRENDA team