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
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
screening, identification, and characterization of affinity peptides, AF7p and Cy5.5-HS7, specific to MT1-MMP and application in tumor imaging, overview. Feasibility of using the subtraction biopanning strategy to screen the affinity peptide targeting MT-loop regions and HS7 is a superior probe for noninvasively imaging MT1-MMP expression in MT1-MMP-positive tumor models. Usage of HS7 in early diagnosis of tumors and in peptide-mediated drugs
diagnostics
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MMP-14 can be a biomarker in early development of mesothelioma tumours, overview
drug development
medicine
additional information
drug development
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MMP-14 is an effective therapeutic target in therapy of mesothelioma tumours
drug development
dimeric MT1-MMP inhibitors might be further developed and exploited as an alternative tool to reduce cancer cell invasion
medicine
the understanding of the regulatory mechanisms that control the activity of the key proteinase in tumor cell invasion, is essential for the design of potent and safe anti-cancer therapies
medicine
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complex reciprocal effects of ERK1/2 and p38 MAPK in the regulation of MT1-MMP activity, which may complicate the use of MAPK-specific inhibitors as therapeutic agents to down-regulate the biologic effects of TGF-beta1 on pericellular collagen degradation and tumor invasion
medicine
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full enzymatic activity of MT1-MMP is required for a specific up-regulation of VEGF-A through an activation of Src tyrosine kinase pathways
medicine
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mechanistic association between MT1-MMP levels and post-I/R remodeling, multiple targets for the interruption of augmented MT1-MMP activity and abundance with I/R
medicine
MT1-MMP and MMP gelatinase A function together in the extracellular matrix degradation or remodeling associated with metamorphosis, MT1-MMP has additional MMP gelatinase A independent roles in the development of adult longitudinal muscle in the intestine
medicine
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MT1-MMP initiates substrate degradation and enhances cell migration, hemopexin-like domain and a nonenzymatic component of the catalytic domain of MT1-MMP are essential for MT1-MMP-mediated cell migration, Rac1 participates in the MT1-MMP signal transduction pathway
medicine
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MT1-MMP is involved in cell migration and collagen-induced mitogen-activated protein kinase-extracellular signal-related kinase activation, collagen-induced mitogen-activated protein kinase-extracellular signal-related kinase activation inhances MT1-MMP activity, hemopexin-like domain of MT1-MMP inhibits collagen-induced mitogen-activated protein kinase-extracellular signal-related kinase activation and migration
medicine
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MT1-MMP proteolysis of protective antigen markers makes the MT1-MMP-expressing aggressive invasive cells resistant to the cytotoxic effect of bipartite PA/FP59 toxin, synthetic inhibitors of MMPs are likely to increase the therapeutic anti-cancer effect of anthrax toxin, unique role of furin in the activation of protective antigen markers
medicine
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MT1-MMP proteolysis of T cell CD44 regulates adhesion and subsequent transmigration and homing of T cells into the pancreas, inhibition of T cell MT1-MMP is key to delaying the onset of diabetes
medicine
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some mercaptosulfide inhibitors effectively inhibit activation of proMMP-2 by endogenous MT1-MMP produced by HT1080 human fibrosarcoma cells, block fibronectin degradation by prostate cancer LNCaP cells stably transfected with MT1-MPP
medicine
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MT1-MMP is involved in keratinocyte growth factor receptor expression and epithelial cell proliferation after acute airway injury
medicine
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considering the important role of apolipoproteinE for lipid metabolism and atherosclerosis protection, MMP-14 might play an essential role for the development of hyperlipidemia and atherosclerosis as a result of degradation of apolipoprotein E
medicine
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the relationship between serum MT1-MMP and bone mineral density as well as bone metabolic markers in 206 Chinese postmenopausal women aged 43-80 years is investigated by Western analysis and ELISA. Multiple linear stepwise regression analysis shows that MT1-MMP is not a determinant factor for bone mineral density. Significant positive correlations between MT1-MMP and serum alkaline phosphatase, N-telopeptides of type I collagen are found, and remain significant after adjustment for age and body-mass index. Moreover, serum MT1-MMP, BAP, and NTX decreased in response to alendronate therapy MT1-MMP and bone turnover markers are correlated, and serum MT1-MMP levels may rise with increase in bone turnover
additional information
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association of MT1-MMP with different membrane subdomains may be crucial in the control of its different activities like cell migration, invasion or MT1-MMP-dependent signaling pathways
additional information
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degradomics method that efficiently identifies substrates of MMP-14
additional information
glycolysation of MT1-MMP may protect against autolysis and thus stabilize ative MT1-MMP
additional information
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glycolysation of MT1-MMP may protect against autolysis and thus stabilize ative MT1-MMP
additional information
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MMP-2 and MT1-MMP are cooperative dynamic components of a cell surface proteolytic axis involved in regulating the cellular signaling environment and pericellular collagen homeostasis
