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A stimulatory role for cGMP-dependent protein kinase in platelet activation.

Cell (2003-01-16)
Zhenyu Li, Xiaodong Xi, Minyi Gu, Robert Feil, Richard D Ye, Martin Eigenthaler, Franz Hofmann, Xiaoping Du
RÉSUMÉ

It is currently accepted that cGMP-dependent protein kinase (PKG) inhibits platelet activation. Here, we show that PKG plays an important stimulatory role in platelet activation. Expression of recombinant PKG in a reconstituted cell model enhanced von Willebrand factor (vWF)-induced activation of the platelet integrin alpha(IIb)beta(3). PKG knockout mice showed impaired platelet responses to vWF or low doses of thrombin and prolonged bleeding time. Human platelet aggregation induced by vWF or low-dose thrombin was inhibited by PKG inhibitors but enhanced by cGMP. Furthermore, a cGMP-enhancing agent, sildenafil, promoted vWF- or thrombin-induced platelet aggregation. The cGMP-stimulated platelet responses are biphasic, consisting of an initial transient stimulatory response that promotes platelet aggregation and a subsequent inhibitory response that limits the size of thrombi.

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Sigma-Aldrich
PKG1α Protein, active, 10 µg, Active, N-terminal 6His-tagged, recombinant, full length PKG1α. For use in Kinase Assays.
Le tarif et la disponibilité ne sont pas disponibles actuellement.
Sigma-Aldrich
PRKG1, active, GST tagged human, PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Le tarif et la disponibilité ne sont pas disponibles actuellement.