3.4.24.B3: matrix metalloproteinase-11
This is an abbreviated version!
For detailed information about matrix metalloproteinase-11, go to the full flat file.
Word Map on EC 3.4.24.B3
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3.4.24.B3
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metalloproteinases
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metastasis
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mmp-2
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timps
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gelatinase
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microperoxidase-11
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metamorphosis
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tadpole
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matrilysin
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menstrual
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medicine
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stromelysin-2
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microperoxidase
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collagenase-3
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pharmacology
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diagnostics
- 3.4.24.B3
- metalloproteinases
- metastasis
- mmp-2
- timps
- gelatinase
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microperoxidase-11
-
metamorphosis
- tadpole
- matrilysin
-
menstrual
- medicine
- stromelysin-2
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microperoxidase
- collagenase-3
- pharmacology
- diagnostics
Reaction
proteolytic degradation of proteins =
Synonyms
M10.007, matrix metalloproteinase 11, matrix metalloproteinase-11, matrix metalloproteinase-11/stromelysin-3, matrixin, matrixin 11, MMP stromelysin-3, MMP-11, MMP-11 proteinase, MMP11, More, MP-11, SL-3, ST-3, ST3, stromelysin 3, stromelysin-3
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General Information
General Information on EC 3.4.24.B3 - matrix metalloproteinase-11
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malfunction
metabolism
physiological function
additional information
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MMP11-deficient mice develop higher numbers of metastases than wild-type mice
malfunction
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overexpression of MMP-11 correlates with patients having poorly differentiated tumors and lymph node metastasis. A synergistic effect between MMP-11 and cytoskeleton-20 on risk elevation is significant in patients with advanced tumor stage and lymph node metastasis
malfunction
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role of MMP11 in cancer progression, MMP11 expression correlates with aggressive profile and invasiveness of different types of carcinoma
malfunction
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role of MMP11 in cancer progression, MMP11 expression correlates with aggressive profile and invasiveness of different types of carcinoma
malfunction
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stromelysin-3 plays a key role in human tumor progression and poor clinical outcome, increased matrix metalloproteinase 11 expression levels are associated with advanced-stage and high-grade tumors, overview
malfunction
the levels of proliferation and migration of cells transfected with MMP-11 siRNA are significantly reduced, while the levels in MMP-11-plasmid-transfected cells are increased. Variations in intracellular MMP-11 significantly alters the amount of phospho-p65 in thyroid cells, while p65 knockdown does not affect MMP-11 expression
malfunction
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role of MMP11 in cancer progression, MMP11 expression correlates with aggressive profile and invasiveness of different types of carcinoma
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malfunction
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MMP11-deficient mice develop higher numbers of metastases than wild-type mice
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effects of MMP-11 expression on regulation of focal adhesion kinase/Src kinase (FAK/Src) and MAP-Kinase signalling pathway, overview
metabolism
MMP-11 regulatory migration is associated with the NF-kappaB p65 signaling pathway
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role of MMP11 or stromelysin-3, during the thyroid hormone-dependent amphibian metamorphosis, a process that resembles the so-called postembryonic development in mammals, overview. The metamorphosis requires the removal of unwanted larval cells through programmed cell death, or apoptosis, and proliferation followed by differentiation of adult cell types. Stromelysin-3 controls apoptosis in different tissues via at least two distinct mechanisms, detailed overview
physiological function
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MMP-11 plays a role in lobular carcinogenesis through increasing resistance to anoikis
physiological function
the enzyme is required for optimal postnatal ductal morphogenesis and function of the mammary gland but does not influence the intrinsic organization of the mammary epithelium
physiological function
the enzyme plays a significant role in the turnover of extracellular matrix constituents
physiological function
enzyme MMP-11 is involved in breast cancer initiation, progress and metastases development, MMP-11 plays a key role in the progression of cancer
physiological function
matrix metalloproteinases (MMPs) are a group of zinc-dependent endopeptidases that digest the intercellular matrix, thereby affecting the tumor microenvironment by promoting angiogenesis, tumor growth, and metastasis. Role of MMP-11 in the mediation of thyroid cancer cell development, as well as in regulation of thyroid cell proliferation and migration. MMP-11 is the most differentially expressed matrix metalloproteinase, MMP. The change in cyclin D1 is consistent with MMP-11 expression, which may explain the changes in proliferation. MMP-11 is located upstream of p65 and regulates its activity. MMP-11 regulatory migration is also associated with the NF-kappaB p65 signaling pathway. MMP-11 promotes activation of p65
physiological function
MMP-11 overexpression in OSCC cells increases in vitro cell migration. Mechanistically, MMP-11 increases the cell motility of oral squamous cell carcinoma (OSCC) cells through focal adhesion kinase/Src kinase (FAK/Src) pathway
physiological function
MMP-11, which is a secreted protein, not only takes effect in the cytoplasm, but is secreted to the extracellular space as an important component in the microenvironment, affecting both the tumors and the extracellular matrix. Role of MMP-11 in tumorigenesis and cancer progression is regarded as a tumor-facilitating factor by promoting colony formation, remodeling extracellular matrix and suppressing apoptosis. Importance of MMP-11 in modifying tumor microenvironment and potent antitumoral effects on solid tumors. The enzyme degrades proteins of the extracellular matrix. MMP-11 may work as a tumor repressor by inhibiting metastasis in certain tumors. MMP-11 is not only correlated with advanced-stage and high-grade tumors, but significantly associated with metastasis, especially for lymph node metastasis rather than peritoneal seeding and distant organ metastasis
physiological function
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the enzyme is involved in skeletal muscle development in zebrafish, morphogenesis of the myotendinous junction (MTJ), overview. Mmp11 localization to the MTJ is regulated by laminin. Laminin polymerization indirectly promotes fibronectin (Fn) downregulation at the MTJ, via a matrix metalloproteinase 11 (Mmp11)-dependent mechanism. Laminin deposition and organization is required for localization of Mmp11 to the MTJ, where Mmp11 is both necessary and sufficient for Fn downregulation in vivo. Furthermore, reduction of residual Mmp11 in laminin mutants promotes a Fn-rich MTJ that partially rescues skeletal muscle architecture. Mmp11 is necessary and sufficient for fibronectin downregulation
the 5-year survival rates of patients with high expression of both MMP-11 and IGF-1 is significantly lower compared to the patients with low expression levels of both MMP-11 and IGF-1
additional information
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the 5-year survival rates of patients with high expression of both MMP-11 and IGF-1 is significantly lower compared to the patients with low expression levels of both MMP-11 and IGF-1