Sea urchin fibrillar collagen 2α chain participates in heterotrimeric molecules of (1α)22α stoichiometry

被引：12

作者：

Cluzel, C ^{[1
]}

Lethias, C ^{[1
]}

Garrone, R ^{[1
]}

Exposito, JY ^{[1
]}

机构：

[1] Univ Lyon 1, CNRS, UMR 5086, Inst Biol & Chim Prot, F-69367 Lyon 07, France

来源：

MATRIX BIOLOGY | 2000年 / 19卷 / 06期

关键词：

fibrillar collagen; molecular composition; sea urchin;

D O I：

10.1016/S0945-053X(00)00109-8

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：

In sea urchin, two fibrillar collagen chains (1 alpha and 2 alpha) have been characterized by molecular biology while two biochemically detected chains (alpha1 and alpha2) have been reported. Here, to determine the relationship between these results, Western-blotting and Edman degradation sequencing of the amino-termini of pepsinized sea urchin fibrillar collagen chains were performed. The data demonstrate that the 2 alpha chain corresponds to the alpha2 chain and is involved in the formation of heterotrimeric molecules [(1 alpha)(2)2 alpha]. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.

引用

页码：545 / 547

页数：3

共 11 条

[1]

EXPOSITO JY, 1992, J BIOL CHEM, V267, P17404

[2]

EXPOSITO JY, 1992, J BIOL CHEM, V267, P15559

[3] Collagen fibrillogenesis during sea urchin development - Retention of SURF motifs from the N-propeptide of the 2 alpha chain in mature fibrils [J].