Interaction between GPIbα and FcγIIA receptor in human platelets

被引：27

作者：

Sun, B ^{[1
]}

Li, J ^{[1
]}

Kambayashi, J ^{[1
]}

机构：

[1] Otsuka Amer Pharmaceut Inc, Maryland Res Labs, Vasc Biol Div, Rockville, MD USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 266卷 / 01期

关键词：

D O I：

10.1006/bbrc.1999.1761

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：

Glycoprotein (GP) m (alpha and beta) in platelets forms a noncovalent hetero-oligomeric complex with GPIX and GPV and serves as a receptor for von Willebrand factor (vWF), which mediates the initial adhesion of platelets to the subendothelium after vascular damage and also plays a role in thrombin-induced platelet activation. We investigated the interaction between GPIb alpha and Fc gamma IIA receptor using a yeast two-hybrid system and mutagenesis, and we identified residues R542G543R544 in GPIb alpha and D298D299D300 in Fc gamma IIA receptor as the primary interaction sites. These results further confirmed the interaction between GPIb alpha and Fc gamma IIA receptor and support the hypothesis that the signal transduction of GPIb-IX-V that leads to platelet activation may be partially mediated through Fc gamma HA receptor. (C) 1999 Academic Press.

引用

页码：24 / 27

页数：4

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