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Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage
Author(s) -
Eyre David R.,
Apon Stephen,
Wu Jiann-Jiu,
Ericsson Lowell H.,
Walsh Kenneth A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80842-6
Subject(s) - pyridinoline , chemistry , collagen, type i, alpha 1 , type ii collagen , type i collagen , peptide , peptide sequence , n terminal telopeptide , cartilage , biochemistry , amino acid , covalent bond , sequence (biology) , fibril , biology , enzyme , alkaline phosphatase , anatomy , extracellular matrix , organic chemistry , gene , osteocalcin , endocrinology
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 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.