cGMP-independent inhibition of integrin alphaIIbbeta3- mediated platelet adhesion and outside-in signalling by nitric oxide
Naseem, Khalid M. Oberprieler, Nikolaus G. Riba, Rocio Roberts, Wayne Homer-Vanniasinkam, Shervanthi
Naseem, Khalid M.
Oberprieler, Nikolaus G.
Riba, Rocio
Roberts, Wayne
Homer-Vanniasinkam, Shervanthi
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2007
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Abstract
We examined the influence of S-nitrosoglutathione (GSNO) on alpha(IIb)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.
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Oberprieler, N.G., Roberts, W., Riba, R., Graham, A.M., Naseem, K.M. and Homer-Vanniasinkam, S. (2007). cGMP-independent inhibition of integrin alphaIIbbeta3- mediated platelet adhesion and outside-in signalling by nitric oxide. FEBS Letters. Vol. 581, No. 7, pp. 1529-34.
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