Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage

作者：David R. Eyre, Stephen Apon, Jiann-Jiu Wu, Lowell H. Ericsson, Kenneth A. Walsh · 发表于：FEBS Letters · 年份：1987 · DOI：10.1016/0014-5793(87)80842-6 · 被引用次数：253 · 研究领域：Collagen: Extraction and Characterization、Osteoarthritis Treatment and Mechanisms、Cell Adhesion Molecules Research

A major site of pyridinoline cross-linking in bovine type IX collagen was traced to a tryptic peptide derived from one of the molecule's HMW chains. This peptide gave two amino acid sequences (in 2/1 ratio) consistent with it being a three-chained structure. The major sequence matched exactly that of the C-telopeptide of type II collagen from the same tissue. A second HMW chain that contained pyridinoline cross-links also gave two amino-terminal sequences, one from its own amino terminus, the other matching exactly the N-telopeptide cross-linking sequence of type II collagen. We conclude that type IX collagen molecules are covalently cross-linked in cartilage to molecules of type II collagen, probably at fibril surfaces.