| Nitric oxide inhibits platelet adhesion to collagen through cGMP-dependent and independent mechanisms: The potential role for S-nitrosylation. | |
MedLine Citation:
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PMID: 19757323 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Nitric oxide (NO)-mediated inhibition of platelet function occurs primarily through elevations in cGMP, although cGMP-independent mechanisms such as S-nitrosylation have been suggested as alternative NO-signaling pathways. In the present study we investigated the potential for S-nitrosylation to act as a NO-mediated cGMP-independent signaling mechanism in platelets. The NO-donor, S-nitrosoglutathione (GSNO), induced a concentration-dependent inhibition of platelet adhesion to immobilized collagen. In the presence of the soluble guanylyl cyclase inhibitor, ODQ, NO-mediated activation of the cGMP/protein kinase G signaling pathway was ablated. However, ODQ failed to completely abolish the inhibitory effect of NO on collagen-mediated adhesion, confirming that cGMP-independent signaling events contribute to the regulation of platelet adhesion by NO. Biotin-switch analysis of platelets demonstrated the presence of several S-nitrosylated proteins under basal conditions. Treatment of platelets with exogenous NO-donors, at concentrations that inhibited platelet adhesion, increased the number of S-nitrosylated bands and led to hyper-nitrosylation of basally S-nitrosylated proteins. The extent of S-nitrosylation in response to exogenous NO was unaffected by platelet activation. Importantly, platelet activation in the absence of exogenous NO failed to increase S-nitrosylation beyond basal levels, indicating that platelet-derived NO was unable to induce this type of protein modification. Our data demonstrate that S-nitrosylation of platelet proteins in response to exogenous NO may act as a potentially important cGMP-independent signaling mechanism for controlling platelet adhesion. |
Authors:
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Catherine Irwin; Wayne Roberts; Khalid M Naseem |
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1691903 - Physiology of thrombospondin. 11791923 - Improved haemocompatibility of cysteine-modified polymers via endogenous nitric oxide. 2544653 - Neutrophil oxidative metabolism after exposure to bacterial phospholipase c. |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2009-9-15 |
Journal Detail:
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Title: Platelets Volume: - ISSN: 1369-1635 ISO Abbreviation: Platelets Publication Date: 2009 Sep |
Date Detail:
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Created Date: 2009-9-16 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9208117 Medline TA: Platelets Country: - |
Other Details:
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Languages: ENG Pagination: 1-9 Citation Subset: - |
Affiliation:
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Centre for Atherothrombosis Research, University of Bradford, Bradford, BD7 1DP, UK. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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