Activation of mitogen‐activated protein kinase by protein kinase C isotypes α, β I and γ, but not ϵ

FEBS Letters

Tavaré, Jeremy M.¹  Dickens, Martin¹  Young, Stephen W.¹ 

[1] Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK

关键词: MAP kinase;    Phorbol ester;    Insulin;    Protein kinase C;    MAP kinase;    mitogen-activated protein kinase;    Erk;    extracellular signal-regulated protein kinase;    PMA;    phorbol 12-myristate 13-acetate;    PKC;    protein kinase C;    MBP;    myelin basic protein;   

DOI  :  10.1016/0014-5793(96)00287-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Treatment of CHO.T cells with either PMA or insulin led to the activation of MAP kinase by ∼3-fold, and p90 ^rsk by ∼ 4-fold. Over-expression of the α, β _I or γ isoforms of protein kinase C caused a substantial enhancement of the effect of PMA on the activation of MAP kinase and p90 ^rsk , however, the effect of insulin was unchanged. Over-expression of the ϵ isoform of protein kinase C did not alter the effect of either PMA or insulin on the activation of MAP kinase and p90 ^rsk . The results suggest that protein kinase C isotypes α, β _I and γ, but not ϵ, can mediate MAP kinase activation by PMA, and strongly support the hypothesis that protein kinase C isoforms can initiate distinct signalling pathways.

【 授权许可】

Unknown