Syk Activity Is Dispensable for Platelet GP1b-IX-V Signaling
AbstractThe binding of von Willebrand factor (VWF) to the platelet membrane glycoprotein 1b-IX (GP1b-IX) leads to activation of platelets. GP1b was shown to signal via the FcRγ-ITAM (Fc Receptor γ-Immunoreceptor tyrosine-based activation motif) pathway, activating spleen tyrosine kinase (Syk) and other tyrosine kinases. However, there have been conflicting reports regarding the role of Syk in GP1b signaling. In this study, we sought to resolve these conflicting reports and clarify the role of Syk in VWF-induced platelet activation. The inhibition of Syk with the selective Syk inhibitors, OXSI-2 and PRT-060318, did not inhibit VWF-induced platelet adhesion, agglutination, aggregation, or secretion. In contrast, platelets stimulated with the Glycoprotein VI (GPVI) agonist, collagen-related peptide (CRP), failed to cause any aggregation or secretion in presence of the Syk inhibitors. Furthermore, GP1b-induced platelet signaling was unaffected in the presence of Syk inhibitors, but GPVI-induced signaling was abolished under similar conditions. Thus, we conclude that Syk kinase activity does not play any functional role downstream of GP1b-mediated platelet activation. View Full-Text
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Badolia, R.; Kostyak, J.C.; Dangelmaier, C.; Kunapuli, S.P. Syk Activity Is Dispensable for Platelet GP1b-IX-V Signaling. Int. J. Mol. Sci. 2017, 18, 1238.
Badolia R, Kostyak JC, Dangelmaier C, Kunapuli SP. Syk Activity Is Dispensable for Platelet GP1b-IX-V Signaling. International Journal of Molecular Sciences. 2017; 18(6):1238.Chicago/Turabian Style
Badolia, Rachit; Kostyak, John C.; Dangelmaier, Carol; Kunapuli, Satya P. 2017. "Syk Activity Is Dispensable for Platelet GP1b-IX-V Signaling." Int. J. Mol. Sci. 18, no. 6: 1238.
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