Assembly of collagen types II, IX and XI into nascent hetero-fibrils by a rat chondrocyte cell line
被引:29
作者:
Fernandes, RJ
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机构:Univ Washington, Dept Orthopaed & Sports Med, Orthopaed Res Labs, Seattle, WA 98195 USA
Fernandes, RJ
Schmid, TM
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机构:Univ Washington, Dept Orthopaed & Sports Med, Orthopaed Res Labs, Seattle, WA 98195 USA
Schmid, TM
Eyre, DR
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机构:Univ Washington, Dept Orthopaed & Sports Med, Orthopaed Res Labs, Seattle, WA 98195 USA
Eyre, DR
机构:
[1] Univ Washington, Dept Orthopaed & Sports Med, Orthopaed Res Labs, Seattle, WA 98195 USA
[2] Rush Univ, Rush Med Coll, Dept Biochem, Chicago, IL 60612 USA
[3] Univ Washington, Dept Biochem, Seattle, WA 98195 USA
来源:
EUROPEAN JOURNAL OF BIOCHEMISTRY
|
2003年
/
270卷
/
15期
关键词:
chondrocyte;
type II procollagen;
pyridinoline cross-links;
collagen fibril;
extracellular matrix;
D O I:
10.1046/j.1432-1033.2003.03711.x
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:
The cell line, RCS-LTC (derived from the Swarm rat chondrosarcoma), deposits a copious extracellular matrix in which the collagen component is primarily a polymer of partially processed type II N-procollagen molecules. Transmission electron microscopy of the matrix shows no obvious fibrils, only a mass of thin unbanded filaments. We have used this cell system to show that the type II N-procollagen polymer nevertheless is stabilized by pyridinoline cross-links at molecular sites (mediated by N- and C-telopeptide domains) found in collagen II fibrils processed normally. Retention of the N-propeptide therefore does not appear to interfere with the interactions needed to form cross-links and mature them into trivalent pyridinoline residues. In addition, using antibodies that recognize specific cross-linking domains, it was shown that types IX and XI collagens, also abundantly deposited into the matrix by this cell line, become covalently cross-linked to the type II N-procollagen. The results indicate that the assembly and intertype cross-linking of the cartilage type II collagen heteropolymer is an integral, early process in fibril assembly and can occur efficiently prior to the removal of the collagen II N-propeptides.