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• W2121530981 startingPage "13336" @default.
• W2121530981 abstract "A role for glycoprotein (GP)V in platelet function has been proposed on the basis of observations that GP V is the major thrombin substrate on intact platelets cleaved during thrombin-induced platelet aggregation, and that GP V promotes GP Ib-IX surface expression in heterologous cells. We tested the hypotheses that GP V is involved in thrombin-induced platelet activation, in GP Ib-IX expression, and in other platelet responses by generating GP V null mice. Contrary to expectations, GP V -/- platelets were normal in size and expressed normal amounts of GP Ib-IX that was functional in von Willebrand factor binding, explaining why defects in GP V have not been observed in Bernard-Soulier syndrome, a bleeding disorder caused by a lack of functional GP Ib-IX-V. Moreover, in vitro analysis demonstrated that GP V -/- platelets were hyperresponsive to thrombin, resulting in increased fibrinogen binding and an increased aggregation response. Consistent with these findings, GP V -/- mice had a shorter bleeding time. These data support a role for GP V as a negative modulator of platelet activation. Furthermore, they suggest a new mechanism by which thrombin enhances platelet responsiveness independent of activation of the classical G-protein-coupled thrombin receptors." @default.
• W2121530981 created "2016-06-24" @default.
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• W2121530981 date "1999-11-09" @default.
• W2121530981 modified "2023-09-27" @default.
• W2121530981 title "Increased thrombin responsiveness in platelets from mice lacking glycoprotein V" @default.
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• W2121530981 doi "https://doi.org/10.1073/pnas.96.23.13336" @default.
• W2121530981 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/23948" @default.
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