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    Phosphorylation of the PKG substrate, vasodilator-stimulated phosphoprotein (VASP), in human cultured prostatic stromal cells

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    Authors
    Cook, Anna
    Haynes, J.
    Date
    2007
    Type
    Journal Article
    
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    Citation
    Cook, Anna-Louise M. and Haynes, John. 2007. Phosphorylation of the PKG substrate, vasodilator-stimulated phosphoprotein (VASP), in human cultured prostatic stromal cells. Nitric Oxide: Biology and Chemistry 16 (1): 10-17.
    Source Title
    Nitric Oxide: Biology and Chemistry
    DOI
    10.1016/j.niox.2006.09.003
    Faculty
    Division of Health Sciences
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/18890
    Collection
    • Curtin Research Publications
    Abstract

    Nitric oxide (NO) is known to regulate contractility and proliferation of cells within the prostate, however, the mechanism by which this occurs is unknown. The cGMP-dependent protein kinase (PKG) signalling pathway may be involved, and recent work has shown that activation of this pathway can be assessed by analysis of phosphorylation of vasodilator-stimulated phosphoprotein (VASP). The aim of the current study is to characterise the expression of VASP in the human prostate and human cultured prostatic stromal cells (HCPSCs), and to investigate whether NO activates PKG in these cells. Our studies revealed that VASP is expressed, and that incubation of HCPSCs with PKG-activating cGMP-analogues or the NO-donor, SNP, caused a significant PKG-dependent increase in VASP serine-239 phosphorylation. In addition, SNP elicited a reduction in intracellular K+ in a time frame consistent with the phosphorylation of VASP and activation of PKG. These data demonstrate that VASP can be used to assess the NO/cGMP/PKG signalling pathway in HCPSCs. In addition, we demonstrate for the first time that SNP, probably via NO release, leads to phosphorylation of VASP in a manner consistent with PKG activation.

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