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pubmed-article:2465149pubmed:abstractTextType IX collagen is found in hyaline cartilage, where it is associated with type II collagen in quarter-staggered collagen fibrils. Chicken type IX collagen has been extensively characterized and shown to contain molecules with three triple-helical domains, interspersed with non-triple-helical sequences. The molecule contains three, genetically distinct, subunits and one of these subunits carries a covalently bound glycosaminoglycan side chain. In the present report, we describe for the first time the primary structure of mammalian type IX collagen chains, based on cloning and sequencing of cDNA from rat and human cDNA libraries. The results suggest that mammalian alpha 1(IX) chains have the same multi-domain structure as the avian protein. We also demonstrate, by in situ hybridization of chromosome spreads, that the human alpha 1(IX) collagen gene is located on the long arm of chromosome 6. The cloning of human type IX collagen cDNA provides a probe for molecular studies of human chondrodysplasias that may involve abnormalities in this extracellular collagen-proteoglycan.lld:pubmed
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pubmed-article:2465149pubmed:articleTitleMolecular cloning of rat and human type IX collagen cDNA and localization of the alpha 1(IX) gene on the human chromosome 6.lld:pubmed
pubmed-article:2465149pubmed:affiliationDepartment of Anatomy and Cellular Biology, Harvard Medical School, Boston, Massachusetts 02115.lld:pubmed
pubmed-article:2465149pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2465149pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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