TY - JOUR
T1 - A role of calcium-activated, phospholipid-dependent protein kinase in platelet-activating factor-induced serotonin release from rabbit platelets
AU - Ieyasu, Hidetaka
AU - Takai, Yoshimi
AU - Kaibuchi, Kozo
AU - Sawamura, Makoto
AU - Nishizuka, Yasutomi
N1 - Funding Information:
*/ This investigation has been supported in part by research grants from the Scientific Research Fund of the Ministry of Education, Science and Culture (1981-1982), the Intractable Diseases Division, Public Health Bureau, the Ministry of Health and Welfare (1980-1982), a Grant-in-Aid of New Drug Development from the Ministry of Health and Welfare, Japan (1980-1982) and the Yamanouchi Foundation for Research on Metabolic Disorders (1980-1982). §/ To whom correspondence should be addressed at Department of Biochemistry, Kobe University School of Medicine, Kobe 650, Japan. ~/ The abbreviations used are: PAF, platelet-activating factor; PI, phosphatidylinositol; DG, diacylglycerol; DBcAMP, dibutyryl cyclic AMP; PGEI, prostaglandin El; SDS, sodium dodecyl sulfate.
PY - 1982/10/29
Y1 - 1982/10/29
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(82)80107-1
DO - 10.1016/S0006-291X(82)80107-1
M3 - Article
C2 - 7181916
AN - SCOPUS:0020284815
SN - 0006-291X
VL - 108
SP - 1701
EP - 1708
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -