CLONING OF THE CHICKEN ALPHA-3(IX) COLLAGEN CHAIN COMPLETES THE PRIMARY STRUCTURE OF TYPE-IX COLLAGEN

被引:26
|
作者
BREWTON, RG
OUSPENSKAIA, MV
VANDERREST, M
MAYNE, R
机构
[1] UNIV ALABAMA,SCH MED,DEPT CELL BIOL,BOX 302,UAB STN,BIRMINGHAM,AL 35294
[2] CNRS,INST BIOL & CHEM PROT,F-69373 LYONS,FRANCE
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 205卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1992.tb16798.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
Type IX collagen is composed of three genetically distinct polypeptides that contain several collagenous and non-collagenous domains. The alpha-2(IX) chain also contains a covalently bound glycosaminoglycan side chain. Type IX collagen is located on the surface of collagen fibrils of both hyaline cartilage and vitreous humor, such that one of the collagenous domains (COL3) projects from the surface of the fibril in a periodic manner. We have cloned and sequenced a full-length cDNA for the chicken alpha-3(IX) collagen chain from a cartilage cDNA library. Together with the sequence of the alpha-1(IX) and alpha-2(IX) chains, this completes the primary structure of type IX collagen for one species. These sequences will be useful to better understand the mechanism of triple-helix formation in type IX collagen and the nature of type II and type IX collagen interactions in fibril formation.
引用
收藏
页码:443 / 449
页数:7
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