Prostacyclin inhibition of phosphatidic acid synthesis in human platelets is not mediated by protein kinase C
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. Phospholipid degradation and signal translation for protein phosphorylation
2. A role of calcium-activated, phospholipid-dependent protein kinase in platelet-activating factor-induced serotonin release from rabbit platelets
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4. The role of phospholipase C in platelet responses
5. Shape change induced in human platelets by platelet-activating factor. Correlation with the formation of phosphatidic acid and phosphorylation of a 40,000-dalton protein.
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1. Regulation of platelet glycoprotein IIb/IIIa (integrin αIIBβ3) function via the thrombin receptor;Biochemical Journal;1995-07-15
2. Clinical evaluation on combined administration of oral prostacyclin analogue beraprost and phosphodiesterase inhibitor cilostazol;Pharmacological Research;1995-01
3. Protein kinase C stimulates dense tubular Ca2+ uptake in the intact human platelet by increasing the Vm of the Ca2+-ATPase pump: stimulation by phorbol ester, inhibition by calphostin C;Biochimica et Biophysica Acta (BBA) - Biomembranes;1992-06
4. Modes of inhibitory action of 4β-phorbol 12-myristate 13-acetate in thrombin-stimulated arachidonic acid release in intact and permeabilized platelets;Archives of Biochemistry and Biophysics;1990-01
5. Role of phosphoinositides in transmembrane signaling.;Physiological Reviews;1990-01
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