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Activation of protein kinase C by cis- and trans-fatty acids and its potentiation by diacylglycerol

Item Type:Article
Title:Activation of protein kinase C by cis- and trans-fatty acids and its potentiation by diacylglycerol
Creators Name:Seifert, R., Schaechtele, C., Rosenthal, W. and Schultz, G.
Abstract:Both cis- and trans-unsaturated but not saturated fatty acids activated protein kinase C purified to apparent homogeneity from rat brain. Fatty-acid-induced enzyme activation was not more than additive with that by phospholipids and was potentiated by diacylglycerol. Recently, we demonstrated that cis- and trans-unsaturated fatty acids induced platelet aggregation and phosphorylation of specific proteins. Both events were potentiated by a cell-permeable diacylglycerol [(1987) Biochem. Biophys. Res. Commun. 149, 762-768]. Thus, trans-unsaturated fatty acids may provide useful experimental tools for the study of protein kinase C activation in vitro and in vivo. Our results suggest that fatty acids and diacylglycerol may synergistically be involved in hormonal stimulation of protein kinase C, as certain hormonal stimuli cause release of diacylglycerol and fatty acids from phospholipids by parallel activation of phospholipases C and A2.
Keywords:Brain, Calcium, Diglycerides, Enzyme Activation, Unsaturated Fatty Acids, Glycerides, Kinetics, Protein Kinase C, Stereoisomerism, Structure-Activity Relationship, Animals, Rats
Source:Biochemical and Biophysical Research Communications
Publisher:Academic Press
Page Range:20-26
Date:15 July 1988
Official Publication:https://doi.org/10.1016/0006-291X(88)90643-2
PubMed:View item in PubMed

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