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    Platelet nitric oxide synthase is activated by tyrosine dephosphorylation: Possible role for SHP-1 phosphatase.

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    Publication date
    2006
    Author
    Naseem, Khalid M.
    Milward, A.D.
    Parkin, Susan M.
    Patel, B.
    Sharifi, M.
    Oberprieler, Nikolaus G.
    Gibbins, J.M.
    Keyword
    Nitric oxide synthase
    Platelets
    SHP-1
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Summary. Background: Endothelial nitric oxide synthase (eNOS) activity in endothelial cells is regulated by post-translational phosphorylation of critical serine, threonine and tyrosine residues in response to a variety of stimuli. However, the post-translational regulation of eNOS in platelets is poorly defined. Objectives: We investigated the role of tyrosine phosphorylation in the regulation of platelet eNOS activity. Methods: Tyrosine phosphorylation of eNOS and interaction with the tyrosine phosphatase SHP-1 were investigated by coimmunoprecipitation and immunoblotting. An in vitro immunoassay was used to determine eNOS activity together with the contribution of protein tyrosine phosphorylation. Results: We found platelet eNOS was tyrosine phosphorylated under basal conditions. Thrombin induced a dose- and time-dependent increase in eNOS activity without altering overall level of tyrosine phosphorylation, although we did observe evidence of minor tyrosine dephosphorylation. In vitro tyrosine dephosphorylation of platelet eNOS using a recombinant protein tyrosine phosphatase enhanced thrombin-induced activity compared to thrombin alone, but had no effect on endothelial eNOS activity either at basal or after stimulation with bradykinin. Having shown that dephosphorylation could modulate platelet eNOS activity we examined the role of potential protein phosphatases important for platelet eNOS activity. We found SHP-1 protein tyrosine phosphatase, co-associated with platelet eNOS in resting platelets, but does not associate with eNOS in endothelial cells. Stimulation of platelets with thrombin increased SHP-1 association with eNOS, while inhibition of SHP-1 abolished the ability of thrombin to induce elevated eNOS activity. Conclusions: Our data suggest a novel role for tyrosine dephosphorylation in platelet eNOS activation, which may be mediated by SHP-1.
    URI
    http://hdl.handle.net/10454/3250
    Version
    No full-text available in the repository
    Citation
    Naseem, K.M., Milward, A.D., Parkin, S.M. and Patel, B. et al. (2006). Platelet nitric oxide synthase is activated by tyrosine dephosphorylation: Possible role for SHP-1 phosphatase. Journal of Thrombosis and Haemostasis. Vol. 4, No. 11, pp. 2423-2432.
    Link to publisher’s version
    Http://dx.doi.org/10.1111/j.1538-7836.2006.02160.x
    Type
    Article
    Collections
    Life Sciences Publications

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