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(7-methoxy-coumarin-4-yl)acetyl-Ala-Pro-Lys-2,4-dinitrophenol + 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
(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
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg amide + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg amide + H2O
?
-
-
-
-
?
(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
?
-
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
?
-
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
?
-
-
-
-
?
(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
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
?
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser + H2O
?
-
optimized fluorogenic substrate
-
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg + H2O
?
-
-
-
-
?
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
7-amino-4-methylcoumaryl-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
-
-
-
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
7-methoxycoumarin-4acetyl-PLG + ?
-
-
-
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
?
-
-
-
?
alpha1-antitrypsin + H2O
?
-
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
-
-
?
alpha1PI + H2O
?
-
protein, inhibitor of elastase, inactivation by cleavage of Pro357-Met358 peptide bond of its reactive centre
-
-
?
annexin II + H2O
?
-
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
-
-
?
bovine carboxymethylated-transferrin + H2O
?
-
-
-
?
C-type lectin domain family 3 member A + H2O
?
-
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
?
-
-
-
?
collagen type IV + H2O
?
-
-
-
?
Cy5.5-M7 peptide + H2O
?
-
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
?
-
synthetic fluorescent peptide
-
?
decorin + H2O
transforming growth factor-beta + ?
-
-
-
?
Dinitrophenyl-Pro-Leu-Gly-Ile-Ala-Gly-Pro-D-Arg + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
ectodomain shedding
-
-
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
-
matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
-
-
?
elastin + H2O
elastin peptides
entactin + H2O
peptide fragment ranging from 29000 to 115000 MW
-
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
-
?
FasL + H2O
sFasL + ?
-
human and murine FasL
-
?
fibrin + H2O
fibrin fragments + ?
-
-
-
?
fibronactin + H2O
fibronectin peptide fragments
-
-
MWs of 30 to 175 kDa
-
?
fibronecin + H2O
?
pericellular proteolysis
-
-
?
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln + H2O
?
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln + H2O
?
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln + H2O
?
-
-
-
-
?
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln + H2O
?
-
-
-
-
?
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln + H2O
?
-
-
-
-
?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
-
-
-
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
Insulin B-chain + H2O
?
-
cleavage at 2 points: Ala14-Leu15 and Tyr16-Leu17
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
insulin-like growth factor binding protein-5 + H2O
?
Laminin-1 + H2O
?
-
-
-
-
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
i.e. LN5, composed of alpha3, beta3,and gamma2 chains, is an important component of epithelial basement membranes where it induces firm adhesion and hemidesmosome formation, LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, MMP7-processed LN5 significantly enhances cell motility, overview
-
-
?
laminin-5/laminin-332 + H2O
90 kDa beta3 chain fragment + ?
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
?
-
-
-
?
osteopontin + H2O
?
-
-
-
?
Oxidized alpha1PI + H2O
?
-
cleavage of Phe352-Leu353 bond
-
-
?
PB-M7vis + H2O
?
-
fluorogenic substrate based on a polyamino amino dendrimer core of 14.2 kDa covalently coupled with an fluorescein-labeled peptide fluorescein(aminohexanoic acid)RPLALWRS(aminohexanoic acid)Cand with tetramethylrhodamine
-
-
?
pig gelatin type A + H2O
?
-
-
-
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
-
-
-
-
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
-
i.e. procryptdins
-
-
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
-
-
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
Pro-matrix metalloproteinase 1 + H2O
?
-
activation by specific cleavage at the Gln80-Phe81 bond
-
-
?
proADAM28s + H2O
ADAM28s + propeptide
-
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
-
-
?
tenascin-C + H2O
?
-
production of protein fragments
-
-
?
tumor necrosis factor-alpha + H2O
?
activation
-
-
?
tumor-associated antigen 90K + H2O
?
type IV basement membrane collagen + H2O
?
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
additional information
?
-
(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
?
-
MOCAc-PLGL(Dpa)AR
-
-
?
(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
?
-
MOCAc-PLGL(Dpa)AR, Lot 480429
-
?
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
-
-
-
-
?
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
-
-
-
?
Azocoll + H2O
?
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
-
-
?
beta-casein + H2O
?
-
-
-
?
beta-casein + H2O
?
-
casein zymography
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
fluorescence-labeled substrate
-
-
?
casein + H2O
?
-
casein zymography
-
-
?
casein + H2O
?
-
non-specific substrate used in zymography
-
-
?
casein + H2O
?
degradation
-
-
?
casein + H2O
?
-
non-specific substrate used in zymography
-
-
?
connexin-43 + H2O
?
-
-
-
?
connexin-43 + H2O
?
cleavage site determination, overview
-
-
?
Elastin + H2O
?
-
-
-
-
?
elastin + H2O
elastin peptides
-
degradation
in the range of 500-8000 Da
-
?
elastin + H2O
elastin peptides
-
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
in the range of 500-8000 Da
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
-
-
?
Fibronectin + H2O
?
-
pericellular substrate
-
-
?
Fibronectin + H2O
?
degradation
-
-
?
Fibronectin + H2O
?
-
production of protein fragments
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
type III
-
-
?
Gelatin + H2O
?
-
type IV
-
-
?
Gelatin + H2O
?
-
type V
-
-
?
Gelatin + H2O
?
-
type I
-
-
?
Gelatin + H2O
?
-
type I, II, IV and V
-
?
Gelatin + H2O
?
degradation
-
-
?
Gelatin + H2O
?
-
type III
-
-
?
Gelatin + H2O
?
-
type IV
-
-
?
Gelatin + H2O
?
-
type V
-
-
?
Gelatin + H2O
?
-
digests the alpha2(I) chain of gelatin in preference to the alpha1(I) chain
-
-
?
Gelatin + H2O
?
-
cleaves the alpha2(I) chain of rat gelatin producing major cuts at Gly713-Ile714, Gly775-Leu776, Gly809-Ile810
-
-
?
Gelatin + H2O
?
-
type I
-
-
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
membrane-bound, biotinylated Kunitz-type inhibitor HAI-1, cell-bound MMP-7 cleaves HAI-1 mainly between Gly451 and Leu452 and thereby releases the extracellular region as soluble HAI-1 (sHAI-1, comprising amino acids 141-249). The peptide bonds corresponding to Gly375-Phe376 and Glu378-Leu379 in HAI-1 are slightly susceptible to MMP-7 cleavage
-
-
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
membrane-bound, biotinylated Kunitz-type inhibitor HAI-1
-
-
?
IGFBP-3 + H2O
?
-
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
-
-
?
IGFBP-3 + H2O
?
-
i.e. insulin-like growth factor binding protein 3, hydrolysis leads to four major fragments. Cleavage sites include K144-I145 and R95-L96
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
MMP-7 generates IGF-IIand triggers its matricine action by degradation of the IGF-II/IGFBP-2 complex binding to heparan sulfate proteoglycan in the extracellular matrix, MMP-7 induces phosphorylation of the insulin-like growth factor type-1 receptor in colon cancer cells involving IGF-II but not IGFBP-2, overview
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
degradation, three distinct cleavage sites
-
-
?
insulin-like growth factor binding protein-5 + H2O
?
-
-
-
?
insulin-like growth factor binding protein-5 + H2O
?
in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
-
-
?
kappa-casein + H2O
?
-
-
-
-
?
kappa-casein + H2O
?
-
-
-
?
Laminin + H2O
?
-
-
-
?
laminin-332 + H2O
?
-
-
analysis of peptide fragment degradation products
-
?
laminin-332 + H2O
?
-
pericellular substrate
-
-
?
laminin-332 + H2O
?
pericellular proteolysis
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
Notch-1 + H2O
?
-
-
-
?
Notch-1 + H2O
?
MMP-7 interacts with the Notch pathway and is required for Notch activation, which leads to dedifferentiation of acinar cells to the nestin-positive transitional cell and further into duct-like epithelia. Besides being necessary for acinar transdifferentiation, it MMP-7 activity is sufficient to induce the process, overview
-
-
?
Notch-1 + H2O
?
MMP-7 interacts with the Notch pathway and is required for Notch activation, which leads to dedifferentiation of acinar cells to the nestin-positive transitional cell and further into duct-like epithelia. Besides being necessary for acinar transdifferentiation, it MMP-7 activity is sufficient to induce the process, overview
-
-
?
perlecan + H2O
?
i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
-
-
?
perlecan + H2O
?
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
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
-
i.e. pro-human neutrophil peptide-1, in a cell-based assay system
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
-
i.e. pro-human neutrophil peptide-1
-
-
?
Proteoglycan + H2O
?
-
-
-
-
?
Proteoglycan + H2O
?
-
-
-
?
Proteoglycan + H2O
?
degradation
-
-
?
Proteoglycan + H2O
?
-
-
-
-
?
syndecan-2 + H2O
?
-
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
-
-
?
syndecan-2 + H2O
?
-
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
-
-
?
tumor-associated antigen 90K + H2O
?
-
-
-
-
?
tumor-associated antigen 90K + H2O
?
-
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
-
-
?
additional information
?
-
-
no action on: pro-matrix metalloproteinase 2 and 3
-
-
?
additional information
?
-
-
activates collagenase
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
at subsite P1': hydrophobic aliphatic residues preferred, strong preference for Leu
-
-
?
additional information
?
-
-
activates pro-matrix metalloproteinase 9
-
-
?
additional information
?
-
-
activates progelatinase A by removing the propeptide in a process that does not require any autolytic cleavage
-
-
?
additional information
?
-
-
at P3': prefers Met
-
-
?
additional information
?
-
-
enzyme could play a role in inflammatory tissue damage by proteolytically inactivating alpha1PI
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme in mesangial cells may contribute to the progression of injury during glomerular inflammatory states
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
releases TNFalphaand Fas-L from the cell surface, after which they modulate macrophage migration and cell apoptosis
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
MMP-7 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
-
-
?
additional information
?
-
MMP-7 content is elevated in tumors copared to healthy mucosa
-
-
?
additional information
?
-
-
MMP-7 content is elevated in tumors copared to healthy mucosa
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
MMP-7 plays a role in tumor angiogenesis
-
-
?
additional information
?
-
-
MMP-7 plays a role in tumor angiogenesis
-
-
?
additional information
?
-
MMP-7 plays an important role in the development and progression of renal cancer
-
-
?
additional information
?
-
MMP7 plays an essential role in cancer, innate immunity, and in inflammatory disorders
-
-
?
additional information
?
-
the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
-
-
?
additional information
?
-
the expression of MMP-7 in gliomas is not related to the invasive behaviour
-
-
?
additional information
?
-
-
the expression of MMP-7 in gliomas is not related to the invasive behaviour
-
-
?
additional information
?
-
MMP-7 interacts with anionic, cationic and neutral lipid membranes, it interacts strongest with anionic membranes, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
matrilysins proteolyze a number of extracellular matrix/basement membrane components, including type IV collagens and proteoglycans
-
-
?
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
?
additional information
?
-
-
matrix metalloproteinases are zinc-dependent neutral endopeptidases
-
-
?
additional information
?
-
-
MMP-7 interacts with insulin-like growth factor binding protein 5, inhibitor of metalloproteinase-3, fibronectin 1, and TFPI
-
-
?
additional information
?
-
-
MMP-7 is capable of degrading many extracellular matrix proteins and cellular adhesions
-
-
?
additional information
?
-
-
MMP-7 participates in activation other members of the MMP family
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-7 assay using DQ-gelatin fluorescent substrate
-
-
?
additional information
?
-
-
binding of MMP-7 to EJ-1 cell surface
-
-
?
additional information
?
-
-
immunohistochemic analysis of peptide fragment degradation products
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
cholesterol sulfate modulates the substrate preference of the enzyme, thereby regulating its pericellular proteolytic action
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
MMP-7 is an endopeptidase that degrades a broad range of substrates
-
-
?
additional information
?
-
-
rapid identification of highly active and selective substrates using bacteriophage peptide display libraries
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
potentially important role of the enzyme in disruption of basement membranes by tumor or inflammatory cells
-
-
?
additional information
?
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
MMP-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction, MMP-7 is implicated in post-MI remodeling, overview
-
-
?
additional information
?
-
MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
-
-
?
additional information
?
-
-
MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
-
-
?
additional information
?
-
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, enzyme-deficient mice show a much lower mortality rate compared to wild-type mice, overview
-
-
?
additional information
?
-
-
MMP-7 cleaves E-cadherin from lung epithelium
-
-
?
additional information
?
-
-
MMP-7 assay using DQ-gelatin fluorescent substrate
-
-
?
additional information
?
-
MMP-7 is an endopeptidase that degrades a broad range of substrates
-
-
?
additional information
?
-
-
MMP-7 assay using DQ-gelatin fluorescent substrate
-
-
?
additional information
?
-
-
MMP-7 cleaves E-cadherin from lung epithelium
-
-
?
additional information
?
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
-
-
?
additional information
?
-
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, enzyme-deficient mice show a much lower mortality rate compared to wild-type mice, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
rat and human enzyme do not activate rat collagenase 3
-
-
?
additional information
?
-
-
phenylazo-Pro-Leu-Gly-Pro-D-Arg
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
collagens of type I, III or V
-
-
?
additional information
?
-
the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
beta-casein + H2O
?
-
-
-
?
casein + H2O
?
degradation
-
-
?
connexin-43 + H2O
?
-
-
-
?
E-cadherin + H2O
?
ectodomain shedding
-
-
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
-
matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
-
-
?
elastin + H2O
elastin peptides
-
degradation
in the range of 500-8000 Da
-
?
fibronactin + H2O
fibronectin peptide fragments
-
-
MWs of 30 to 175 kDa
-
?
Gelatin + H2O
?
degradation
-
-
?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
-
-
-
?
hepatocyte growth factor activator inhibitor type 1 + H2O
?
membrane-bound, biotinylated Kunitz-type inhibitor HAI-1, cell-bound MMP-7 cleaves HAI-1 mainly between Gly451 and Leu452 and thereby releases the extracellular region as soluble HAI-1 (sHAI-1, comprising amino acids 141-249). The peptide bonds corresponding to Gly375-Phe376 and Glu378-Leu379 in HAI-1 are slightly susceptible to MMP-7 cleavage
-
-
?
IGFBP-3 + H2O
?
-
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
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
MMP-7 generates IGF-IIand triggers its matricine action by degradation of the IGF-II/IGFBP-2 complex binding to heparan sulfate proteoglycan in the extracellular matrix, MMP-7 induces phosphorylation of the insulin-like growth factor type-1 receptor in colon cancer cells involving IGF-II but not IGFBP-2, overview
-
-
?
insulin-like growth factor binding protein-5 + H2O
?
in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
-
-
?
laminin-332 + H2O
?
-
pericellular substrate
-
-
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
i.e. LN5, composed of alpha3, beta3,and gamma2 chains, is an important component of epithelial basement membranes where it induces firm adhesion and hemidesmosome formation, LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, MMP7-processed LN5 significantly enhances cell motility, overview
-
-
?
perlecan + H2O
?
i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
-
-
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
-
-
-
-
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
-
i.e. procryptdins
-
-
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
-
-
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
-
i.e. pro-human neutrophil peptide-1, in a cell-based assay system
-
-
?
Proteoglycan + H2O
?
degradation
-
-
?
syndecan-2 + H2O
?
-
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
-
-
?
tenascin-C + H2O
?
-
production of protein fragments
-
-
?
tumor necrosis factor-alpha + H2O
?
activation
-
-
?
tumor-associated antigen 90K + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
additional information
?
-
Fibronectin + H2O
?
-
also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
-
-
?
Fibronectin + H2O
?
degradation
-
-
?
Fibronectin + H2O
?
-
production of protein fragments
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
N-cadherin + H2O
?
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
-
-
?
Notch-1 + H2O
?
MMP-7 interacts with the Notch pathway and is required for Notch activation, which leads to dedifferentiation of acinar cells to the nestin-positive transitional cell and further into duct-like epithelia. Besides being necessary for acinar transdifferentiation, it MMP-7 activity is sufficient to induce the process, overview
-
-
?
Notch-1 + H2O
?
MMP-7 interacts with the Notch pathway and is required for Notch activation, which leads to dedifferentiation of acinar cells to the nestin-positive transitional cell and further into duct-like epithelia. Besides being necessary for acinar transdifferentiation, it MMP-7 activity is sufficient to induce the process, overview
-
-
?
additional information
?
-
-
enzyme could play a role in inflammatory tissue damage by proteolytically inactivating alpha1PI
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme in mesangial cells may contribute to the progression of injury during glomerular inflammatory states
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
releases TNFalphaand Fas-L from the cell surface, after which they modulate macrophage migration and cell apoptosis
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
MMP-7 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
-
-
?
additional information
?
-
MMP-7 content is elevated in tumors copared to healthy mucosa
-
-
?
additional information
?
-
-
MMP-7 content is elevated in tumors copared to healthy mucosa
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
MMP-7 plays a role in tumor angiogenesis
-
-
?
additional information
?
-
-
MMP-7 plays a role in tumor angiogenesis
-
-
?
additional information
?
-
MMP-7 plays an important role in the development and progression of renal cancer
-
-
?
additional information
?
-
MMP7 plays an essential role in cancer, innate immunity, and in inflammatory disorders
-
-
?
additional information
?
-
the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is regulated involving estrogen, which affects enzyme expression and secretion, mechanism, overview
-
-
?
additional information
?
-
the expression of MMP-7 in gliomas is not related to the invasive behaviour
-
-
?
additional information
?
-
-
the expression of MMP-7 in gliomas is not related to the invasive behaviour
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
matrilysins proteolyze a number of extracellular matrix/basement membrane components, including type IV collagens and proteoglycans
-
-
?
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
?
additional information
?
-
-
matrix metalloproteinases are zinc-dependent neutral endopeptidases
-
-
?
additional information
?
-
-
MMP-7 interacts with insulin-like growth factor binding protein 5, inhibitor of metalloproteinase-3, fibronectin 1, and TFPI
-
-
?
additional information
?
-
-
MMP-7 is capable of degrading many extracellular matrix proteins and cellular adhesions
-
-
?
additional information
?
-
-
MMP-7 participates in activation other members of the MMP family
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
binding of MMP-7 to EJ-1 cell surface
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
potentially important role of the enzyme in disruption of basement membranes by tumor or inflammatory cells
-
-
?
additional information
?
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
MMP-7 affects connexin-43 levels, electrical conduction, and survival after myocardial infarction, MMP-7 is implicated in post-MI remodeling, overview
-
-
?
additional information
?
-
MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
-
-
?
additional information
?
-
-
MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
-
-
?
additional information
?
-
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, enzyme-deficient mice show a much lower mortality rate compared to wild-type mice, overview
-
-
?
additional information
?
-
-
MMP-7 cleaves E-cadherin from lung epithelium
-
-
?
additional information
?
-
-
MMP-7 cleaves E-cadherin from lung epithelium
-
-
?
additional information
?
-
matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor, it upregulates ErbB4 receptor expression, mediates ErbB4 localization in cytoplasm and nucleus, solubilizes the ErbB4 receptor cognate ligand heaprin-bound epidermal growth factor, and mediates the proteolytic processing of ErbB4, overview, MMP-7 shows in vitro and in vivo proliferative activity
-
-
?
additional information
?
-
MMP-7 plays a role in innate immunity and participates in the control of the pathogen Chlamydia trachomatis during the early stages of the infection
-
-
?
additional information
?
-
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, which can be lethal to mice, enzyme-deficient mice show a much lower mortality rate compared to wild-type mice, overview
-
-
?
additional information
?
-
the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(-)-5-hydroxypluviatolide
-
50% inhibition at 0.05 mM
(-)-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
(4-phenyl-1,4-dihydropyridine-3,5-diyl)dimethanol
-
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-(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
-
dimethyl sulfoxide
-
competitive inhibition
fibronectin 1
-
fibronectin 1, interacts with MMP-7
-
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
-
-
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-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-[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
-
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
Pseudopeptide inhibitors
-
-
-
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
TIMP-4
-
tissue inhibitor of metalloproteinases-4
-
TIMP3
-
tissue inhibitor of metalloproteinase-3, interacts with MMP-7
-
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
-
Tissue inhibitor of metalloproteinase-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
-
(-)-catechin-3-gallate
-
-
(-)-catechin-3-gallate
-
inhibition is un affected by presence of 10 mM CaCl2
(-)-epicatechin-3-gallate
-
-
(-)-epicatechin-3-gallate
-
inhibition is un affected by presence of 10 mM CaCl2
(-)-gallocatechin-3-gallate
-
-
(-)-gallocatechin-3-gallate
-
inhibitory effect is increased on presence of 10 mM CaCl2, no interaction with Cl-
1,10-phenanthroline
-
-
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
EDTA
-
-
EDTA
inhibits MMP-7-induced cell aggregation
GM6001
-
GM6001
-
a broad-spectrum MMP inhibitor
Hydroxamate
-
-
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
-
tissue inhibitor of metalloprotease-1
-
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
-
TIMP-3
-
tissue inhibitor of metalloproteinases-3
-
TIMP-3
-
is induced by enamel matrix derivative
-
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
-
no inhibition with phosphoramidon
-
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
the enzyme contains an auto-inhibitory peptide
-
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
-
additional information
-
not: phosphoramidon; Zincov
-
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-
high MMP-7 expression level
brenda
-
-
brenda
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
brenda
-
-
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
-
-
brenda
-
immunohistochemic detection of MMP7 expression in biliary tract cancer, semi-quantitative RT-PCR and real-time RT-PCR, overview
brenda
-
from umbilical cord, MMP-7 quantification, overview
brenda
-
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
-
brenda
primary tumors
brenda
early stage primary cancers, MMP-7 correlates with breast cancer development, overexpression of MMP-7 and ErbB4, overview
brenda
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induction of enzyme expression by TNF-alpha and interleukin IL-1beta
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rectal carcinoma cell
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MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
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expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
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low expression of MMP-7, which is induced by physiological processes such as wound healing, but also malignant transformation of epidermal cells
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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
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expression and activity of MMP-7 in fetal membranes during premature rupture of membranes, immunohistochemic analysis, overview
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connective tissue
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highly variable MMP-7 expression in the glioma population
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endometrial carcinoma-derived cell line
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infiltrating
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primary cutaneous and metastatic melanoma
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frp, peripheral blood
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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
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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
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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
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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
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MMP-7 expression analysis semiquantitatively by immunohistochemistry in prostate cancer. E1AF, an ets-oncogene family transcription factor, expression correlates with that of MMP-7
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invasive prostate cancer cells, high enzyme expression level
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presence of enzyme in plasma of normal and azoospermic semen
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induction of enzyme expression by TNF-alpha and interleukin IL-1beta
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mammary gland epithelial cell line
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mammary gland epithelial cell line
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lung adenocarcinoma
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MMP-7 expression analysis, the expression level is increased compared to normal cells
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secretion of the enzyme
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carcinoma in situ, MMP-7+ cells are spread over the whole epithelial layer
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mucosa
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MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
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MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
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MMP-7 overexpression in carcinomas compared to healthy tissue, mucosal, tubular, tubulovillous, or villous colonic adenoma subtypes, MMP-7 expression analysis, overview
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overexpression of MMP-7
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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
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from patients undergoing total colonoscopy
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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
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MMP-7 is overexpressed in colorectal cancer
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MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
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YAP is a critical regulatory factor in upregulating MMP-7 expression on the stiffer substrate in colorectal cancer
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recombinant enzyme
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recombinant enzyme
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active, recombinant
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secreted by COS cells
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transfected mouse myeloma cell conditioned
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release by cytokinine-stimulated mesangial cells
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antifibrotic pulmonary dendritic cell
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antifibrotic pulmonary dendritic cell
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sprouting, of different cancers, the endothelial enzyme is associated with CD34 and/or CD105 expression
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predominantly expressed
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MMP-7 expression analysis
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pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
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vaginal-cervical epithelial cells secrete constitutively MMP-7 into the luminal solution
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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
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MMP-7 is uniquely produced in epithelia
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expression of MMP-7 in the normal oral mucosal epithelium is restricted mainly to the parabasal layers
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lung
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lung
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gingival
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stromal
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aortic and adventitial
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high expression level
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primary specimen, overexpression of MMP-7, realtime PCR, RT-PCR or Western blotting analysis
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wild-type HCT-116 and oxaliplatin-resistant RHCT-116 p53 positive- and p53 negative cell lines
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expression analysis in hearts after transplantation, overview
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LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, distribution, overview
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MMP-7 expression analysis in estrogen-dependently proliferating cells, overview
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wild-type HT-29 and oxaliplatin-resistant RHT-29 cell lines
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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
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MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
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MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
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expression analysis in kidneys after transplantation, overview
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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
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expression levels of fibulin-5 and MMP-7 are inversely correlated in lung tumors
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primary, monocyte-derived
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primary
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esophageal, expression of proMMP-7 but not secretion in myofibroblasts
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
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Gallus gallus Hy-Line Brown
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
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higher expression of MMP-7 in RCC subtypes, i.e. chromophobe, renal papillary and oncocytomas, compared to benign epithelial neoplasias, overview
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analysis of expression of MMP-7 by immunohistochemistry, overview
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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
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acinic cell carcinoma cell
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cancer patients have higher serum levels of MMP-3 and MMP-7 than those with duodenal ulcer and gastritis, overview
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circulating MMP-7 serum concentration is significantly elevated in patients with distant metastasis of prostate cancer, overview
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from healthy persons and patients with type 2 diabetes
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from umbilical cord, MMP-7 quantification, overview
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the serum MMP-7 level is significantly higher in the patients with cholangiocarcinoma compared to benign biliary tract disease patients
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MMP-7 positivity is reduced from carcinoma cells but instead appears in stromal cells
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colon cancer cell line, high levels of MMP-7
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expression analysis, overview
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stimulated by VEGF, no MMP-7 expression in unstimulated HUVEC
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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
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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
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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
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additional information
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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
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additional information
Gallus gallus Hy-Line Brown
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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
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additional information
immunohistochemic analysis
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additional information
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immunohistochemic analysis
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additional information
immunohistochemic analysis
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additional information
MMP-7 content is elevated in tumors compared to helathy mucosa
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additional information
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MMP-7 content is elevated in tumors compared to helathy mucosa
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additional information
no activity in healthy colon tissue
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additional information
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no activity in healthy colon tissue
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additional information
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heparan sulfate proteoglycans, especially perlecan, are extracellular docking molecules for MMP-7
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additional information
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matrilysin-1 is expressed in injured lung and in cancer but not in normal epithelia and cell line BEAS-2B
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additional information
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MMP-7 activity is significantly higher in atherosclerotic plaques than internal mammary arteries
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additional information
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MMP-7 expression analysis in gastric cancer cell lines, overview
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additional information
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MMP-7 expression analysis in gingival tissue, overview
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additional information
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MMP-7 expression analysis in healthy persons and liver cirrhosis patients, overview
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additional information
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MMP7 basal expression is higher in the oxaliplatin-resistant compared to the parental cell lines
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additional information
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quantitative enzyme expression in ulcerative colitis patients and healthy humans, 35 samples, overview
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additional information
in colon cancer in neoplastic cells but not in stromal cells, enzyme expression and immunohistochemic analysis, overview
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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
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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
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additional information
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MMP-7 is overexpressed in a variety of epithelial cancers, such as stomach, liver, pancreatic, and colon cancer
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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
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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
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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
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evolution
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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
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a nonsynonymous genetic variant D137 of matrix metalloproteinase-7 confers risk of liver cirrhosis, overview
malfunction
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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
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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
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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 is involved in gastrointestinal cancer cell invasiveness
malfunction
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MMP-7 polymorphisms are involved in colorectal cancer progression, overview
malfunction
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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
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transforming growth factor-B1 and matrix metalloproteinase-7 promoter variants induce risk for Helicobacter pylori-associated gastric precancerous lesions
malfunction
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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 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
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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
myofibroblasts exhibit increased migration and invasion in response to conditioned media from OE33 cells that is reduced by MMP-7 knockdown and immunoneutralization
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
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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
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malfunction
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MMP-7-deficient mice show educed beta-catenin activation after lung injury or bleomycin treatment
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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
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
metabolism
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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
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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
physiological function
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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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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
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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
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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
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Helicobacter pylori infection upregulates the expression of matrix metalloproteinases, involved in chronic inflammation, ulceration, and cancer development
physiological function
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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
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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
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matrilysin is important for neutrophil migration into the lung in animal models of lung inflammation
physiological function
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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
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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
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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
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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
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matrix metalloproteinase-7 polymorphism is a risk factor for endometrial cancer susceptibility, overview
physiological function
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matrix metalloproteinases are extracellular proteolytic enzymes involved in tumor progression
physiological function
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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
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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
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MMP-7 deletion improves survival after myocardial infarction
physiological function
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MMP-7 is a key regulator of cisplatin resistance in cells of head and neck squamous cell carcinomas, overview
physiological function
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MMP-7 is a potential factor in the cascade affecting the malignant potential of extracellular matrix
physiological function
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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
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
the enzyme functions to degrade extracellular matrix and other pericellular substrates including the adherens junction protein E-cadherin to promote wound healing and tissue remodeling. Matrilysin's catalytic activity regulates beta-catenin localization and signaling activation in lung epithelial cells, the enzyme activity releases beta-catenin from the cell membrane after which it is degraded in the cytosol. Matrilysin activity also increases beta-catenin translocation in the presence of a Wnt activating signal
physiological function
the enzyme is responsible for aggressive malignant phenotypes and poor prognoses implicated in many cancers
physiological function
the enzyme plays an important role in tumor microenvironment, it decreases the susceptibility to 5-fluorouracil in colon cancer 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
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
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
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
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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
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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
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
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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
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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
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physiological function
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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
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physiological function
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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
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additional information
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MMP-7 expression in squamous cell carcinoma is inversely correlated with that of the hyaluronan receptor CD44, overview
additional information
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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
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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
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MMP7 is secreted mostly from the endometrial epithelium cells where attachment occurs and is suggested to be important in the implantation process
additional information
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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
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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
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human matrilysin-1 is one of the most potent elastases besides macrophage elastase in the family of matrix metalloproteinases
additional information
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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
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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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A15T
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a naturally occuring polymorphism, not involved in liver cirrhosis
E198A
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site-directed mutagenesis
E198C
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site-directed mutagenesis
E198D
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site-directed mutagenesis
E198Q
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site-directed mutagenesis
G137D
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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
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a naturally occuring polymorphism, not involved in liver cirrhosis
V470M
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a naturally occuring polymorphism, not involved in liver cirrhosis
Y193F
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site-directed mutagenesis, the mutant shows no pH-dependence shift, as does mutants Y219X
Y216F
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site-directed mutagenesis, the mutant shows no pH-dependence shift, as does mutants Y219X
Y219A
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219C
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219D
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219F
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219S
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
E198Q
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site-directed mutagenesis
additional information
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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
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a form of MMP-7 containing an Glu to Gln mutation in the catalytic domain is catalytically inactive
additional information
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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
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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
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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
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host MMP-7 contributes to mammary tumor growth in the bone microenvironment after injection of human tumor cells into tibias of mice
additional information
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matrilysin-1 suppression by siRNA
additional information
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MMP-7 inhibition by siRNA transfection
additional information
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MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
additional information
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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
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MMP-7 tethered to cancer cell surface via cholesterol sulfate degrades fibronectin and laminin-332 coated on a culture plate
additional information
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overexpression of MMP-7, and knocked-down using small inhibitory RNAs
additional information
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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
shRNA interfering MMP7 downregulates MMP
additional information
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shRNA interfering MMP7 downregulates MMP
additional information
construction of MMP-7 knockout mice
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
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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
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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
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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
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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
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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
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MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
additional information
generation of MMP-7 knockout mice
additional information
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MMP-7 knockout or inhibition retards cleavage of N-cadherin and vascular smooth muscle cell apoptosis, overview
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additional information
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MMP-7-deficient cells do not show activation of Notch-1, which can be restored by recombinant MMP-7, phenotype, overview
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additional information
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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
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additional information
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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
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additional information
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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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