Selective activation of the γ‐subspecies of protein kinase C from bovine cerebellum by arachidonic acid and its lipoxygenase metabolites

FEBS Letters

Naor, Zvi¹  Kishimoto, Akira¹  Sekiguchi, Kazuo¹  Shearman, Mark S.¹  Nishizuka, Yasutomi¹ 

[1] Department of Biochemistry, Kobe University School of Medicine, Kobe 650, Japan

关键词: Protein kinase C;    Arachidonic acid;    Lipoxygenase metabolite;    PKC;    protein kinase C;    PtdSer;    phosphatidylserine;    DO;    diolein;    FPLC;    fast-protein liquid chromatography;    AA;    arachidonic acid;    LxA;    5(S);    6(R);    15(S)-trihydroxy-7;    9;    13-trans;    -11-cis-eicosatetraenoic acid;    lipoxin A;    12-HETE;    12(S)-hydroxy-5;    8;    10;    14-eicosatetraenoic acid;    5-HETE;    5(S)-hydroxy-6;    8;    11;    14-eicosatetraenoic acid;    TxB2;    thromboxane B2;    PGE2;    prostaglandin E2;    LTC4;    leukotriene C4;    NMDA;    N-methyl-D-aspartate;    PLA2;    phospholipase A2;    LTP;    long-term potentiation;   

DOI  :  10.1016/0014-5793(89)80125-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown