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Selective activation of the γ‐subspecies of protein kinase C from bovine cerebellum by arachidonic acid and its lipoxygenase metabolites
Author(s) -
Shearman Mark S.,
Naor Zvi,
Sekiguchi Kazuo,
Kishimoto Akira,
Nishizuka Yasutomi
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80125-5
Subject(s) - protein kinase c , arachidonic acid , diacylglycerol kinase , activator (genetics) , biochemistry , cerebellum , lipoxygenase , second messenger system , prkcq , chemistry , subspecies , biology , enzyme , receptor , endocrinology , mitogen activated protein kinase kinase , paleontology
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.