@article{0ac3192aba494846936a213708367d8e,
title = "Phosphatidylinositol turnover in platelet activation; Calcium mobilization and protein phosphorylation",
abstract = "Ca2+-activated, phospholipid-dependent protein kinase (C-kinase) in platelets is normally activated by diacylglycerol, which is derived from phosphatidylinositol through its receptor-linked breakdown. Under appropriate conditions this enzyme can also be activated by synthetic diacylglycerol which is directly added to intact platelets. C-Kinase thus activated preferentially phosphorylates an endogenous platelet protein having a molecular weight of approximately 40,000. This protein phosphorylation is merely a prerequisite but not a sufficient requirement for the release of serotonin. Evidence is presented suggesting that Ca2+ mobilization and C-kinase activation are synergistically involved in the physiological response of platelets to extracellular messengers, such as thrombin, collagen and platelet-activating factor.",
author = "Kozo Kaibuchi and Kimihiko Sano and Masahiko Hoshijima and Yoshimi Takai and Yasutomi Nishizuka",
note = "Funding Information: The authors are grateful to Dr. T. Fujikura for the preparation of l-oleoyl-2-acetyl-3-glyceryl phosphate, and also to Mrs. S. Nishiyama and Miss K. Yamasaki for their skillful secretarial assistance. This investigation has been supported in part by research grants from the Scientific Research Fund of the Ministry of Education, Science and Culture (1982), the Intractable Diseases Division, Public Health Bureau, the Ministry of Health and Welfare (1981-1982), a Grant-in-Aid of New Drug Development from the Ministry of Health and Welfare (1979-1982), the Yamano-uchi Foundation for Research on Metabolic Disorders (1982), and the Mitsuhisa Cancer Research Foundation (1981).",
year = "1982",
month = oct,
doi = "10.1016/0143-4160(82)90020-3",
language = "English",
volume = "3",
pages = "323--335",
journal = "Cell Calcium",
issn = "0143-4160",
publisher = "Elsevier Ltd",
number = "4-5",
}