A DISCRETE SEQUENCE IN A PLATELET INTEGRIN IS INVOLVED IN LIGAND RECOGNITION

被引：195

作者：

DSOUZA, SE ^{[1
]}

GINSBERG, MH ^{[1
]}

MATSUEDA, GR ^{[1
]}

PLOW, EF ^{[1
]}

机构：

[1] PRINCETON UNIV, SQUIBB LABS BIOL, PRINCETON, NJ 08544 USA

来源：

NATURE | 1991年 / 350卷 / 6313期

关键词：

D O I：

10.1038/350066a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

PLATELET membrane glycoprotein IIb-IIIa (gpIIb-IIIa; alpha-IIb-beta-3), the most prominent member of the integrin family of adhesion receptors on these cells, mediates platelet aggregation by binding fibrinogen and is critical in thrombosis and haemostasis 1-5. A short amino-acid sequence at the carboxy terminus of the gamma-chain of fibrinogen is recognized by gpIIb-IIIa (ref. 6) and peptides containing this sequence are selectively crosslinked to residues 294-314 of gpIIb (ref. 7). Here we show that an 11-residue peptide from this region of gpIIb inhibits platelet aggregation and binding of fibrinogen to platelets and to purified gpIIb-IIIa, and that it interacts directly with fibrinogen. These results implicate this segment of gpIIb-IIIa in the ligand-binding function of the receptor. Moreover, as this region is highly conserved among integrins, it may have a general function in ligand recognition by this broadly distributed family of adhesion receptors.

引用

页码：66 / 68

页数：3

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