tailieunhanh - Báo cáo khoa học: Assembly of collagen types II, IX and XI into nascent hetero-fibrils by a rat chondrocyte cell line

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-pro-collagen polymer nevertheless is stabilized by pyridinoline cross-links at molecular sites (mediated by N- and C-telo-peptide domains) found in collagen II fibrils processed nor-mally | Eur. J. Biochem. 270 3243-3250 2003 FEBS 2003 doi Assembly of collagen types II IX and XI into nascent hetero-fibrils by a rat chondrocyte cell line Russell J. Fernandes1 Thomas M. Schmid2 and David R. Eyre1 3 1 Department of Orthopedics and Sports Medicine University of Washington Seattle WA USA department of Biochemistry Rush Medical College Rush University Chicago IL USA 3Department of Biochemistry University of Washington Seattle WA USA 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-pro-collagen polymer nevertheless is stabilized by pyridinoline cross-links at molecular sites mediated by N- and C-telo-peptide 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 usingantibodies that recognize specific cross-linking domains it was shown that types X and XII 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. Keywords chondrocyte type II procollagen pyridinoline cross-links collagen fibril extracellular matrix. The collagen framework of the extracellular matrix of developinghyaline cartilaeg is assembled primarily from three cartilage-specific collagens type II type IX and type XI 1 . These three .

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