Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites.
Type IX collagen, a quantitatively minor collagenous component of cartilage, is known to be associated with and covalently cross-linked to type II collagen fibrils in chick and bovine cartilage. Type IX collagen molecules have also been shown to form covalent cross-links with each other in bovine cartilage. In the present study we demonstrate by structural analysis and location of cross-linking sites that, in human cartilage, type IX collagen is covalently cross-linked to type II collagen and to other molecules of type IX collagen. We also present evidence that, if the proteoglycan form of type IX collagen is present in human cartilage, it can only be a minor component of the matrix, similar to findings with bovine cartilage.
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Department of Orthopaedics, University of Washington, Seattle 98195-6500, USA.
Wu
J J
JJ
Eyre
D R
DR
D000595:Amino Acid Sequence; D015153:Blotting, Western; D001894:Borohydrides; D002356:Cartilage / Q000737:chemistry*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D010504:Periodic Acid; D017421:Sequence Analysis
D001894:Borohydrides; D010455:Peptides; D010504:Periodic Acid; C025364:sodium borohydride; D003094:Collagen; C009288:metaperiodate; D010434:Pepsin A