Type X collagen isolated from the hypertrophic cartilage of embryonic chick tibiae contains both hydroxylysyl- and lysylpyridinoline cross-links

被引:6
作者
Orth, MW
Luchene, LJ
Schmid, TM
机构
[1] Department of Biochemistry, Rush Medical College, Rush Presbyt.-St. Luke's Med. Center, Chicago
关键词
D O I
10.1006/bbrc.1996.0227
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hypertrophic cartilage from the tibiotarsus of Day 20 chick embryonic tibiae was found to contain an unusually high concentration of lysylpyridinoline (LP), a nonreducible collagen cross-link normally found only in bone and dentin but not in cartilage. Since type X collagen is abundant in this cartilage, research was conducted to see if type X was tile primary source of LP. The 45-kDa pepsin-resistant form of type X was purified by immunoaffinity chromatography. It contained a high concentration of the LP cross-link while type II contained primarily hydroxylysylpyridinoline (HP), the predominant cross-link in cartilage. This, to our knowledge is the first time that type X has been shown directly to form nonreducible cross-links and that a collagen other than type I has a high level of LP. Also, it is interesting that the HP and LP cross-links are found in a collagen in a collagen that is degraded so rapidly. Possible explanations for these findings are discussed. (C) 1996 Academic Press, Inc.
引用
收藏
页码:301 / 305
页数:5
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