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
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metamorphosis
- tadpole
- matrilysin
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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
ECTree
3.4.24.B3 matrix metalloproteinase-11Advanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.B3 - matrix metalloproteinase-11
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
laminin receptor precursor + H2O
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laminin receptor precursor is a likely in vivo substrate of stromelysin-3. Its cleavage may alter cell-extracellular matrix interaction, thus playing a role in mediating the effects of stromelysin-3 on cell fate and behavior observed during development and pathogenesis. Human laminin receptor precursor is cleaved by stromelysin-3 at the same two sites as in Xenopus laminin receptor precursor, yielding two N-terminal fragments of sizes identical to the corresponding Xenopus laminin receptor precursor fragments due to amino acid insertion in the C-terminus part of Xenopus laminin receptor precursor
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?
collagen VI + H2O
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MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. Extracellular proteolytic processing of this chain is required for correct collagen VI folding. MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. The native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps
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collagen VI + H2O
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MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. Extracellular proteolytic processing of this chain is required for correct collagen VI folding. MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. The native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps
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protein + H2O
peptides
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enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression
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?
protein + H2O
peptides
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enzyme plays a role in tumor progression and wound healing
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?
protein + H2O
peptides
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the enzyme promotes and modulates tumor progression
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?
protein + H2O
peptides
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enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression
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?
protein + H2O
peptides
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the enzyme promotes and modulates tumor progression
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?
additional information
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adipocytes/pre-adipocytes and MMP-11 participate in a highly complex vicious cycle to support tumor progression, and this process is orchestrated by cancer cells. First, both invasive cancer cells and resting adipocytes/pre-adipocytes do not express MMP-11. When a cancer cell meets an adipocyte/pre-adipocyte, their cross-talk/interaction induces the expression/secretion of MMP-11 by the adipocyte/pre-adipocyte. MMP-11 negatively regulates adipogenesis, leading to a decrease in adipocyte differentiation and accumulation/maintenance of MMP-11-expressing fibroblast like cells. These latter cells then act on adjacent invasive cancer cells to favor their survival and potentiate this vicious cycle
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additional information
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MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
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additional information
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the enzyme regulates cell fate and tissue morphogenesis through direct or indirect remodeling of extracellular matrix
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additional information
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stromelysin-3 expression, in the absence of thyroid hormone, causes significant muscle cell death in the tail of premetamorphic transgenic tadpoles. On the other hand, only relatively low levels of epidermal cell death are induced by precocious thyroid hormone expression in the tail
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