CONFORMATION-DEPENDENT PLATELET-ADHESION TO COLLAGEN INVOLVING INTEGRIN ALPHA-2-BETA-1-MEDIATED AND OTHER MECHANISMS - MULTIPLE ALPHA-2-BETA-1-RECOGNITION SITES IN COLLAGEN TYPE-I

被引：89

作者：

MORTON, LF

PEACHEY, AR

ZIJENAH, LS

GOODALL, AH

HUMPHRIES, MJ

BARNES, MJ

机构：

[1] STRANGEWAYS RES LAB, CAMBRIDGE CB1 4RN, ENGLAND

[2] ROYAL FREE HOSP, SCH MED, LONDON NW3 2PF, ENGLAND

[3] UNIV MANCHESTER, SCH BIOL SCI, MANCHESTER M13 9PT, ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1994年 / 299卷

关键词：

D O I：

10.1042/bj2990791

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：

Platelet adhesion has been measured to type-I monomeric collagen, collagen fibres, alpha 1(I) and alpha 2(I) chains and the chain fragments alpha 1(I)CB3, alpha 1(I)CB6, alpha 1(I)CB7 and alpha 1(I)CB8, and alpha 2(I)CB3,5 and alpha 2(I)CB4. Little if any adhesion occurred to any denatured species at 37 degrees C, demonstrating the importance of the collagen helix. However, on coating at 4 degrees C to promote helix formation, and assaying at room temperature to avoid denaturation, adhesion was observed to both a-chain types and all fragments, the exact level of which depended on the identity of the species in question. Adhesion was strongly Mg2+-dependent. Antibodies against the integrin alpha 2 beta 1 partially inhibited adhesion to alpha-chains and all fragments except alpha 1(I)CB6, indicating a wide distribution of alpha 2 beta 1-binding sites in the collagen molecule. 'Activation-dependent' adhesion to monomeric collagen, totally

引用

页码：791 / 797

页数：7

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