Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.B3 extracted from

  • Motrescu, E.R.; Blaise, S.; Etique, N.; Messaddeq, N.; Chenard, M.P.; Stoll, I.; Tomasetto, C.; Rio, M.C.
    Matrix metalloproteinase-11/stromelysin-3 exhibits collagenolytic function against collagen VI under normal and malignant conditions (2008), Oncogene, 27, 6347-6355.
    View publication on PubMed
Search for more literature for 3.4.24.B3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
collagen VI + H2O Mus musculus 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 ?
-
 ?
collagen VI + H2O Homo sapiens 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell
-
 Mus musculus
-
SAOS-2 cell
-
 Homo sapiens
-
U-87MG cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
collagen VI + H2O 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 Mus musculus ?
-
 ?
collagen VI + H2O 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 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
matrix metalloproteinase-11/stromelysin-3
-
 Mus musculus
matrix metalloproteinase-11/stromelysin-3
-
 Homo sapiens
MMP11
-
 Mus musculus
MMP11
-
 Homo sapiens