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Literature summary for 3.4.24.B12 extracted from

  • Didangelos, A.; Mayr, U.; Monaco, C.; Mayr, M.
    Novel role of ADAMTS-5 protein in proteoglycan turnover and lipoprotein retention in atherosclerosis (2012), J. Biol. Chem., 287, 19341-19345.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B12

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
aorta
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aggrecan + H2O
-
 Mus musculus fragment 74ALGS + ?
-
 ?
brevican + H2O + H2O
-
 Mus musculus ?
-
 ?
versican + H2O + H2O
-
 Mus musculus fragment DPEAAE441 + ?
-
 ?

Expression

Organism Comment Expression
Mus musculus fibroblast growth factor 2 inhibits ADAMTS-5 expression in isolated aortic smooth muscle cells and blocks the spontaneous release of ADAMTS-generated versican and aggrecan fragments from aortic explants down

General Information

General Information Comment Organism
physiological function ADAMTS-5 is markedly reduced in atherosclerotic aortas of apolipoprotein E-null mice. The reduction of ADAMTS-5 is accompanied by accumulation of biglycan and versican, the major lipoprotein-binding proteoglycans, in atherosclerosis. ADAMTS-5 activity induced the release of ADAMTS-specific versican and aggrecan fragments as well as biglycan and link protein from the aortic wall. Fibroblast growth factor 2 inhibits ADAMTS-5 expression in isolated aortic smooth muscle cells and blocked the spontaneous release of ADAMTS-generated versican and aggrecan fragments from aortic explants. In aortas of ADAMTS-5-deficient mice, ADAMTS-specific versican neoepitopes are not detectable. Biglycan levels are increased. ADAMTS-5 proteolytic activity reduces the low density lipoprotein binding ability of biglycan and releases low density lipoprotein from human aortic lesions Mus musculus