3.4.24.80: membrane-type matrix metalloproteinase-1
This is an abbreviated version!
For detailed information about membrane-type matrix metalloproteinase-1, go to the full flat file.
Word Map on EC 3.4.24.80
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3.4.24.80
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metalloproteinases
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mmp-2
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metastasis
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endothelial
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zymography
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angiogenesis
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gelatin
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gelatinase
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timps
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prommp-2
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mesenchymal
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invasiveness
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vessel
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basement
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integrins
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angiogenic
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fibrosarcoma
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matrigel
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transwell
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furin
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fibronectin
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zymogen
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gelatinolytic
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progelatinase
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ectodomain
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invadopodia
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hemopexin
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alphavbeta3
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proproteins
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mt-mmps
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collagen-rich
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anti-invasive
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matrix-degrading
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collagenolytic
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pro-matrix
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emmprin
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hemopexin-like
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membrane-tethered
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proenzyme
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convertase
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invasion-promoting
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analysis
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diagnostics
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cona-induced
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medicine
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drug development
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endoglin
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reck
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podosomes
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mmp-dependent
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cortactin
- 3.4.24.80
- metalloproteinases
- mmp-2
- metastasis
- endothelial
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zymography
- angiogenesis
- gelatin
- gelatinase
- timps
- prommp-2
- mesenchymal
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invasiveness
- vessel
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basement
- integrins
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angiogenic
- fibrosarcoma
- matrigel
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transwell
- furin
- fibronectin
- zymogen
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gelatinolytic
- progelatinase
- ectodomain
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invadopodia
- hemopexin
- alphavbeta3
- proproteins
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mt-mmps
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collagen-rich
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anti-invasive
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matrix-degrading
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collagenolytic
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pro-matrix
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emmprin
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hemopexin-like
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membrane-tethered
- proenzyme
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convertase
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invasion-promoting
- analysis
- diagnostics
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cona-induced
- medicine
- drug development
- endoglin
- reck
- podosomes
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mmp-dependent
- cortactin
Reaction
endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-/-Leu. Other bonds hydrolysed include Gly35-/-Ile in the propeptide of collagenase 3, and Asn341-/-Phe, Asp441-/-Leu and Gln354-/-Thr in the aggrecan interglobular domain =
Synonyms
ectMMP-14, gelatinase A, interstitial MT1-MMP, matrix metalloprotease 14, matrix metalloproteinase 14, matrix metalloproteinase MT 1, matrix metalloproteinase MT-MMP-1, matrix metalloproteinase MT1-MMP, matrix metalloproteinase-14, membrane type 1 matrix, membrane type 1 matrix metalloproteinase, membrane type 1 MMP, membrane type 1-matrix metalloproteinase, membrane type 1-MMP, membrane type I MMP, membrane type matrix metalloproteinase, membrane type MMP-1, membrane type MT1-MMP, membrane type-1 matrix metalloprotease, membrane type-1 matrix metalloprotease 1, membrane type-1 matrix metalloproteinase, membrane type-1 MMP, membrane type-I matrix metalloproteinase, membrane type-I MMP, membrane-anchored matrix metalloproteinase 14, membrane-type 1 matrix metalloproteinase, membrane-type 1 matrix metalloproteinase 1, membrane-type 1 MMP, membrane-type 1-matrix metalloproteinase, membrane-type I matrix metalloproteinase, membrane-type matrix metalloproteinase MT1-MMP, membrane-type matrix metalloproteinase-1, membrane-type metalloproteinase MT1-MMP, membrane-type MMP, metalloproteinase, MMP-14, MMP-2, MMP-8, MMP14, mmp14a, mmp14b, More, MT-MMP-1, MT-MMP1, MT1-MMP, MT1-MMP/MMP-14, MT1-MPP, MTI-MMP, pericellular collagenase, proteinase, matrix metallo-, sMT1-MMP
ECTree
3.4.24.80 membrane-type matrix metalloproteinase-1Advanced search results
results (
results (Engineering
Engineering on EC 3.4.24.80 - membrane-type matrix metalloproteinase-1
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C127S
site-directed mutagenesis, no significant difference in activity is observed for the mutant C127S and the wild-type MT1-MMP
C574A
inefficient in stimulating cell adhesion, migration and invasion, mutation negatively affects cell adhesion
C574S
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substitution in the cytoplasmic domain, reduction of pro-MMP2 activation, no up-regulation of VEGF expression
E240A
K44A
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dominant negative dynamin mutation controlled by a separate cytomegalovirus promoter MT1/K44A, leading to increased substrate digestion that is contributed by enhanced cell migration resulting from the accumulation of MT1-MMP ant the plasma membrane
L571A/L572A/L578A/L579A
mutation leads to reduced internalization of enzyme
L571A/L572A/Y573A
mutation leads to reduced internalization of enzyme, no effect on cell motility
R111H
site-directed mutagenesis, MMP14 R111H enzyme is processed normally in human MRC-5V1 cells and is trafficked to the cell surface, the mutation partially impairs the catalytic activity of MMP14, thus MMP14 R111H retains partial gelatinolytic and pro-MMP2 hydrolyzing activity. The mutant demonstrates significantly reduced migratory behavior when compared with wild-type MMP14
R92C
site-directed mutagenesis, the mutation impairs cell surface localization. The mutant demonstrates significantly reduced migratory behavior when compared with wild-type MMP14
S466P
S577A
T17R
site-directed mutagenesis, the mutation impairs cell surface localization, MMP14 T17R distributed throughout the cytoplasm. The mutant demonstrates significantly reduced migratory behavior when compared with wild-type MMP14
T567A
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substitution in the cytoplasmic domain, pro-MMP2-activating capacity not affected, similar VEGF upregulation
Y573A
Y573A/L571A/L572A/L578A/L579A
mutation leads to reduced internalization of enzyme
S466P
naturally occuring mutation causing the Cartoon phenotype, Cartoon mice harbor the single point mutation in the MT1-MMP hemopexin domain, a 200-amino acid segment that is thought to play a critical role in regulating MT1-MMP collagenolytic activity
additional information
E240A
catalytically inactive, inefficient in stimulating cell migration and invasion
E240A
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substitution in the active site, unable to activate exogenous pro-MMP2, fails to induce VEGF mRNA expression
S466P
site-directed mutagenesis, the mutation impairs cell surface localization
S577A
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substitution in the cytoplasmic domain, pro-MMP2-activating capacity not affected, similar VEGF upregulation
additional information
generation of a mmp14a/b knockout zebrafish model, phenotype, overview
additional information
generation of a mmp14a/b knockout zebrafish model, phenotype, overview
additional information
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generation of a mmp14a/b knockout zebrafish model, phenotype, overview
additional information
catalytic domain: TM1 MMPcat, DELTA269-550 and deletion of transmembrane and cytoplasmic domain: DELTA TM MT1 MMP, DELTA501-559
additional information
mutant defective in catalytic domain, deletion of transmembrane/cytoplasmic domain, deletion of hemopexin domain abolishes enzyme activity, whereas substitution of transmembrane/cytoplasmic membrane with Il-2 receptor does not affect it
additional information
truncation mutant MT1DELTAC with more robust pro-MMP-2 activation and cell surface expression than wild type enzyme, mutant is resistant to increased cell surface expression after concanavalin A treatment
additional information
deletions delta Cat or point mutations CHO-1 and CHO-4, which preserve a relative electrophoretic mobility shift following desialylation similar to the wild type protein, moreover mutant CHO-4 is insensitive to sialidase A treatment, CHO-3 and CHO-4 mtuants are unable to effectively catalyze pro-MMP-2 activation
additional information
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deletions delta Cat or point mutations CHO-1 and CHO-4, which preserve a relative electrophoretic mobility shift following desialylation similar to the wild type protein, moreover mutant CHO-4 is insensitive to sialidase A treatment, CHO-3 and CHO-4 mtuants are unable to effectively catalyze pro-MMP-2 activation
additional information
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MMP-14delta279-523, linker and C-terminal hemopexin-like domain deleted, does not undergo rapid autoproteolysis, relatively small differences to wild type
additional information
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mutant Sol.MT, fails to activate pMMP-2, mutant MTdeltaC, pMMP-2 activation as compared with wild type, neither cell type-dependent nor extracellular matrix component-dependent
additional information
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partial deletion of the catalytic domain deltacd or the cytoplasmic tail delta577 of MT1-MMP, unable to activate exogenous pro-MMP2, no up-regulation of VEGF expression
additional information
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specific amino acid substitutions at the Val524-Ile525 site have no effect on shedding of the 50 kDa species, whereas deletion of the entire stem region deltastem-MT1, which lacks Pro509-Gly535, completely abrogates shedding of the 50 kDa species
additional information
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transcription factor EGR1 gene silencing by siRNA blocks collagen-induced MT1-MMP expression and collagen invasion, integrin signaling through a SRC kinase-dependent pathway is necessary for EGR1 induction, overview
additional information
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suppression of MMP14 expression in human MCF-7 breast cells blocks MHC class I chain-related molecule A, MICA, shedding, while overexpression of MMP14 enhances it, overview
additional information
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construction of truncation mutant MT1EADELTATM lacking the pro-peptide and the transmembrane and cytoplasmic domains. Mutant MT1EADELTATM shows different mobility in reducing and non-reducing PAGE compared to the wild-type enzyme, the disulfide bond in the PEX domain is correctly folded, there is no intermolecular disulfide bond formation, and the complex with TIMP-2 is also correctly formed. A PEX-domain-deleted MT1-MMP mutant is no longer able to activate proMMP-2, but retains some proteolytic activity and forms the ternery complex with proMMP-2 and TIMP-2. A MT1-MMP mutant lacking the catalytic domain is catalytically inactive and inhibits the dimerization and complex formation of the enzyme, overview
additional information
deletion of the MT1-MMP cytoplasmic tail or deletion of the hemopexin-like domain
additional information
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enzyme-deficient fibroblasts show impaired invasion of type I collagen matrices, MT1-MMP null fibroblasts fail to penetrate the matrix
additional information
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a MT1-MMP-deficient mouse produces only a faint level of active MMP-2. MT1-MMP-null mice have severe defects in skeletal development and angiogenesis and die within several weeks after birth, phenotype, overview
additional information
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generation of mutant Cola1(I)r/r mice, phenotype, overview. The mouse model of age-related dermal fibrosis, where MMP14 activity and TGFbeta bioavailability are chronically elevated, or in mice that ectopically express TGFbeta in the epidermis, cutaneous vessels are resistant to acute vessel leakage. Inhibition of ALK5 further enhances vascular leakage into the interstitium and facilitated increases delivery of high molecular weight compounds into premalignant tissue and tumors. Steady-state leakage of capillaries in back skin is also higher in MMP14 null mice versus age-matched heterozygous and wild-type littermates, overview
additional information
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suppression of MMP14 expression in mouse MyC-CaP prostate cancer cells blocks MHC class I chain-related molecule A, MICA, shedding, while overexpression of MMP14 enhances it, overview
additional information
MMP14 enzyme knockout in mammary gland epithelial cells
