Oberprieler, NG and Roberts, W and Graham, AM and Homer-Vanniasinkam, S and Naseem, KM (2007) CGMP-independent inhibition of integrin alpha(IIb)beta(3)-mediated platelet adhesion and outside-in signalling by nitric oxide. FEBS LETT , 581 (7) 1529 - 1534. 10.1016/j.febslet.2007.02.072.
Full text not available from this repository.
Abstract
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.
| Type: | Article |
|---|---|
| Title: | CGMP-independent inhibition of integrin alpha(IIb)beta(3)-mediated platelet adhesion and outside-in signalling by nitric oxide |
| DOI: | 10.1016/j.febslet.2007.02.072 |
| Keywords: | nitric oxide, platelets, cGMP, integrin alpha(IIb)beta(3), tyrosine phosphorylation, PROTEIN-TYROSINE KINASE, ACTIVATION, AGGREGATION, PHOSPHORYLATION, RECEPTORS |
| UCL classification: | UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Surgery and Interventional Science (Division of) |
Archive Staff Only: edit this record