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• W2017450138 abstract "G proteins play a major role in signal transduction upon platelet activation. We have previously reported a patient with impaired agonist-induced aggregation, secretion, arachidonate release, and Ca 2+ mobilization. Present studies demonstrated that platelet phospholipase A 2 (cytosolic and membrane) activity in the patient was normal. Receptor-mediated activation of glycoprotein (GP) IIb-IIIa complex measured by flow cytometry using antibody PAC-1 was diminished despite normal amounts of GPIIb-IIIa on platelets. Ca 2+ release induced by guanosine 5′-[γ-thio]triphosphate (GTP[γS]) was diminished in the patient’s platelets, suggesting a defect distal to agonist receptors. GTPase activity (a function of α-subunit) in platelet membranes was normal in resting state but was diminished compared with normal subjects on stimulation with thrombin, platelet-activating factor, or the thromboxane A 2 analog U46619. Binding of 35 S-labeled GTP[γS] to platelet membranes was decreased under both basal and thrombin-stimulated states. Iloprost (a stable prostaglandin I 2 analog) -induced rise in cAMP (mediated by Gα s ) and its inhibition (mediated by Gα i ) by thrombin in the patient’s platelet membranes were normal. Immunoblot analysis of Gα subunits in the patient’s platelet membranes showed a decrease in Gα q (<50%) but not Gα i , Gα z , Gα 12 , and Gα 13 . These studies provide evidence for a hitherto undescribed defect in human platelet G-protein α-subunit function leading to impaired platelet responses, and they provide further evidence for a major role of Gα q in thrombin-induced responses." @default.
• W2017450138 created "2016-06-24" @default.
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• W2017450138 date "1997-08-05" @default.
• W2017450138 modified "2023-10-16" @default.
• W2017450138 title "Platelet signal transduction defect with Gα subunit dysfunction and diminished Gα _q in a patient with abnormal platelet responses" @default.
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• W2017450138 doi "https://doi.org/10.1073/pnas.94.16.8750" @default.
• W2017450138 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/23110" @default.
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