A role of calcium-activated, phospholipid-dependent protein kinase in platelet-activating factor-induced serotonin release from rabbit platelets
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説明
Summary When rabbit platelets were stimulated by platelet-activating factor (PAF), phosphatidylinositol disappeared rapidly and diacylglycerol was transiently accumulated. Concurrently, an endogenous protein with a molecular weight of about 40,000 (40K protein) was heavily phosphorylated and serotonin was released. These PAF-induced reactions were associated with one another, and simultaneously inhibited by prostaglandin E1 and dibutyryl cyclic AMP. Fingerprint analysis of the phosphorylation sites in 40K protein suggested that Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) was responsible for the phosphorylation of 40K protein. PAF did not appear to activate protein kinase C directly. It is likely that PAF causes the release of serotonin in a mechanism analogous to the thrombin action through its receptor-mediated activation of this unique protein kinase system.
収録刊行物
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- Biochemical and Biophysical Research Communications
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Biochemical and Biophysical Research Communications 108 1701-1708, 1982-10-01
Elsevier BV