Overexpression of protein kinase C-epsilon enhances the stimulatory effect of ethanol on phospholipase C-mediated hydrolysis of phosphatidylethanolamine in NIH 3T3 fibroblasts.
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-epsilon 15-fold to examine the possible role of this enzyme in the regulation of PtdEtn hydrolysis by ethanol. Overexpressed PKC-epsilon (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-epsilon is a potential positive regulator of the PtdEtn-hydrolyzing PLC activity, and that the functional interaction between PKC-epsilon and PLC is facilitated by ethanol.
Kiss
Z
Z
Hormel Institute, University of Minnesota, Austin 55912.
Garamszegi
N
N
D016475:3T3 Cells; D000818:Animals; D015153:Blotting, Western; D000431:Ethanol / Q000494:pharmacology*; D005347:Fibroblasts / Q000201:enzymology; D015870:Gene Expression; D006868:Hydrolysis; D007527:Isoenzymes / Q000096:biosynthesis* / Q000302:isolation & purification; D051379:Mice; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D011493:Protein Kinase C / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D007527:Isoenzymes; D010714:Phosphatidylethanolamines; D000431:Ethanol; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate