title: The low molecular weight collagen synthesized by chick tibial chondrocytes is deposited in the extracellular matrix both in culture and in vivo.
abstract: The low mol. wt. collagen (64 K) synthesized by chick embryo chondrocytes in culture is deposited in the extracellular matrix; its deposition is strictly dependent upon a correct hydroxylation. In vivo the 64 K collagen has been isolated from the cartilage of tibiae obtained from 17-day-old chick embryos. The turnover of this collagen in the extracellular matrix is very rapid: within a few hours it is matured into a 30-K fragment released in the medium. Also this maturation is dependent upon a correct hydroxylation of the molecule. The underhydroxylated form, synthesized in the absence of ascorbic acid or in the presence of alpha-alpha' dipyridyl, is not deposited in the extracellular matrix and is directly secreted as 64 K collagen in the culture medium.
mesh_terms: D015082:2,2'-Dipyridyl / Q000494:pharmacology; D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology; D002356:Cartilage / Q000187:drug effects / Q000196:embryology / Q000378:metabolism*; D002478:Cells, Cultured; D002642:Chick Embryo; D003094:Collagen / Q000096:biosynthesis* / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism*; D006900:Hydroxylation; D007700:Kinetics; D008970:Molecular Weight
chemical_list: D015082:2,2'-Dipyridyl; D003094:Collagen; D001205:Ascorbic Acid