Open AccessCloning of the chicken α 3(IX) collagen chain completes the primary structure of type IX collagen
Author(s) -
BREWTON Randolph G.,
OUSPENSKAIA Maia V.,
REST Michel,
MAYNE Richard
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16798.x
Subject(s) - fibril , collagen, type i, alpha 1 , chemistry , collagen vi , triple helix , collagen helix , glycosaminoglycan , hyaline cartilage , complementary dna , type ii collagen , cartilage , microbiology and biotechnology , biochemistry , extracellular matrix , anatomy , biology , stereochemistry , articular cartilage , gene , pathology , medicine , alternative medicine , osteoarthritis
Type IX collagen is composed of three genetically distinct polypeptides that contain several collagenous and non‐collagenous domains. The α2(IX) chain also contains a covalently bound glycosaminoglycan side chain. Type IX collagen is located on the surface of collagen fibrils of both hyaline cartilage and vitreous humor, such that one of the collagenous domains (COL3) projects from the surface of the fibril in a periodic manner. We have cloned and sequenced a full‐length cDNA for the chicken α3(IX) collagen chain from a cartilage cDNA library. Together with the sequence of the α1(IX) and α2(IX) chains, this completes the primary structure of type IX collagen for one species. These sequences will be useful to better understand the mechanism of triple‐helix formation in type IX collagen and the nature of type II and type IX collagen interactions in fibril formation.