TY - JOUR
T1 - Selective activation of the γ-subspecies of protein kinase C from bovine cerebellum by arachidonic acid and its lipoxygenase metabolites
AU - Shearman, Mark S.
AU - Naor, Zvi
AU - Sekiguchi, Kazuo
AU - Kishimoto, Akira
AU - Nishizuka, Yasutomi
N1 - Funding Information:
Acknowledgements: The research in the Department of Biochemistry, Kobe University School of Medicine was supported in part by research grants from the Scientific Research Fund of the Ministry of Education, Science and Culture, Japan; Muscular Dystrophy Association; Juvenile Diabetes Foundation International, USA; Yamanouchi Foundation for Research on Metabolic Disorders; Merck Sharp & Dohme Research Laboratories; Biotechnology Laboratories of Takeda Chemical Industries; Ajinomoto Central Research Laboratories; Meiji Institute of Health Sciences, and New Lead Research Laboratories of Sankyo Company. M.S.S. is a recipient of a research fellowship from the Japan Society for the Promotion of Science.
PY - 1989/1/30
Y1 - 1989/1/30
N2 - The γ-subspecies of protein kinase C (PKC) apparently is expressed only in central nervous tissues, and at a high level in the cerebellum and hippocampus. γ-PKC from bovine cerebellum, but not the α-or βI/βII-subspecies, is activated by micromolar concentrations of arachidonic acid (AA), in the absence of both phospholipid and diacylglycerol. A significant component of this activation is also calcium independent. Other unsaturated fatty acids are much less active in this respect. Among the AA metabolites tested, lipoxin A (5(S),6(R),15(S)-11-cis-isomer) was a potent, selective activator of the γ-subspecies, and also, to a lesser extent, 12(S)-hydroxy-5,8,10,14-eicosatetraenoic acid could support activation. These results raise the possibility that AA and some of its lipoxygenase metabolites may function as messenger molecules in neurones to activate the γ-subspecies of PKC.
AB - The γ-subspecies of protein kinase C (PKC) apparently is expressed only in central nervous tissues, and at a high level in the cerebellum and hippocampus. γ-PKC from bovine cerebellum, but not the α-or βI/βII-subspecies, is activated by micromolar concentrations of arachidonic acid (AA), in the absence of both phospholipid and diacylglycerol. A significant component of this activation is also calcium independent. Other unsaturated fatty acids are much less active in this respect. Among the AA metabolites tested, lipoxin A (5(S),6(R),15(S)-11-cis-isomer) was a potent, selective activator of the γ-subspecies, and also, to a lesser extent, 12(S)-hydroxy-5,8,10,14-eicosatetraenoic acid could support activation. These results raise the possibility that AA and some of its lipoxygenase metabolites may function as messenger molecules in neurones to activate the γ-subspecies of PKC.
KW - Arachidonic acid
KW - Lipoxygenase metabolite
KW - Protein kinase C
UR - https://www.scopus.com/pages/publications/0024543387
U2 - 10.1016/0014-5793(89)80125-5
DO - 10.1016/0014-5793(89)80125-5
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AN - SCOPUS:0024543387
SN - 0014-5793
VL - 243
SP - 177
EP - 182
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -