cGMP‐independent inhibition of integrin α IIb β 3 ‐mediated platelet adhesion and outside‐in signalling by nitric oxide | Zendy

Oberprieler Nikolaus G. | Zendy; Roberts Wayne | Zendy; Graham Anne M. | Zendy; Homer-Vanniasinkam Shervanthi | Zendy; Naseem Khalid M. | Zendy

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cGMP‐independent inhibition of integrin α IIb β 3 ‐mediated platelet adhesion and outside‐in signalling by nitric oxide

Author(s) -

Oberprieler Nikolaus G.,

Roberts Wayne,

Graham Anne M.,

Homer-Vanniasinkam Shervanthi,

Naseem Khalid M.

Publication year - 2007

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2007.02.072

Subject(s) - phosphorylation , integrin , chemistry , tyrosine phosphorylation , platelet , nitric oxide , adhesion , microbiology and biotechnology , fibrinogen , tyrosine , s nitrosoglutathione , biochemistry , biology , immunology , receptor , glutathione , enzyme , organic chemistry

We examined the influence of S ‐nitrosoglutathione (GSNO) on α IIb β 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 β 3 phosphorylation. Adhesion to fibrinogen induced rapid phosphorylation of β 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 β 3 phosphorylation.

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