CGMP-independent inhibition of integrin αIIbβ3-mediated platelet adhesion and outside-in signalling by nitric oxide

被引：21

作者：

Oberprieler, Nikolaus G.

Roberts, Wayne

Graham, Anne M.

Homer-Vanniasinkam, Shervanthi

Naseem, Khalid M.

机构：

[1] Univ Bradford, Ctr Atherothrombosis Res, Dept Med Biosci, Bradford BD7 1DP, W Yorkshire, England

[2] Leeds Gen Infirm, Vasc Surg Unit, Leeds LS1 3EX, W Yorkshire, England

来源：

FEBS LETTERS | 2007年 / 581卷 / 07期

关键词：

nitric oxide; platelets; cGMP; integrin alpha(IIb)beta(3); tyrosine phosphorylation;

D O I：

10.1016/j.febslet.2007.02.072

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：

We examined the influence of S-nitrosoglutathione (GSNO) on alpha(llb)beta(3) integrin-mediated platelet adhesion to immobilised fibrinogen. GSNO induced a time- and concentration dependent inhibition of platelet adhesion. Inhibition was cGMP-independent and associated with both reduced platelet spreading and protein tyrosine phosphorylation. To investigate the cGMP-independent effects of NO we evaluated integrin beta(3) phosphorylation. Adhesion to fibrinogen induced rapid phosphorylation of beta(3) on tyrosines 773 and 785, which was reduced by GSNO in a cGMP independent manner. Similar results were observed in suspended platelets indicating that NO-induced effects were independent of spreading-induced signalling. This is the first demonstration that NO directly regulates integrin beta(3) phosphorylation. (c) 2007 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：1529 / 1534

页数：6

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