Overexpression of protein kinase C‐ϵ enhances the stimulatory effect of ethanol on phospholipase C‐mediated hydrolysis of phosphatidylethanolamine in NIH 3T3 fibroblasts

FEBS Letters

Garamszegi, Nandor¹  Kiss, Zoltan¹ 

[1] The Hormel Institute, University of Minnesota, 801 16th Avenue NE, Austin, MN 55912, USA

关键词: Ethanol;    Phospholipase C;    Protein kinase C;    PKC;    protien kinase C;    PMA;    phorbol 12-myristate 13-acetate;    PtdEtn;    phosphatidylethanolamine;    PLC;    phospholipase C;    EtnP;    ethanolamine phosphate;   

DOI  :  10.1016/0014-5793(93)80659-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Previously, ethanol and the protein kinase C (PKC) activators phorbol 12-myristate 13-acetate (PMA) and bombesin were shown to synergistically stimulate phospholipase C (PLC)-mediated hydrolysis of phosphatidylethanolamine (PtdEtn) in NIH 3T3 fibroblasts. Here we used fibroblasts overexpressing PKC-ϵ 15-fold to examine the possible role of this enzyme in the regulation of PtdEtn hydrolysis by ethanol. Overexpressed PKC-ϵ (i) greatly enhanced the stimulatory effects of ethanol (37.5–150 mM) on PLC-mediated PtdEtn hydrolysis, and (ii) eliminated the need for the co-presence of a PKC activator for maximal (3,3-fold) stimulation of PLC by 150 mM ethanol. Results suggest that PKC-ϵ is a potential positive regulator of the PtdEtn-hydrolyzing PLC activity, and that the functional interaction between PKC-ϵ and PLC is facilitated by ethanol.

【 授权许可】

Unknown