Diacylglycerol activation of protein kinase C is modulated by long-chain acyl-CoA.
The activity of rat brain protein kinase C, measured in the presence of diacylglycerol, phosphatidylserine and Ca+2, was found to be greatly increased by micromolar amounts of long chain acyl-CoAs, using two different assay systems (lipids added as sonicated dispersion or as mixed micelles with Triton X-100). The potentiation phenomenon required the presence of both diacylglycerol and phosphatidylserine; it was observed at low and saturating concentrations of these effectors, and it was inhibited at high, non physiological Ca+2 concentrations. Under similar conditions, fatty acids alone or coenzyme A were ineffective. The data strongly suggest that acyl-CoAs at the intracellular concentration levels, are important in the modulation of protein kinase C, after activation of the enzyme by the phospholipase C/phosphatidylinositol pathway.
Bronfman
M
M
Department of Cell Biology, P. Universidad Católica de Chile, Santiago.
Morales
M N
MN
Orellana
A
A
D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002118:Calcium / Q000494:pharmacology; D004075:Diglycerides / Q000494:pharmacology*; D004357:Drug Synergism; D004789:Enzyme Activation; D005989:Glycerides / Q000494:pharmacology*; D017830:Octoxynol; D010718:Phosphatidylserines / Q000494:pharmacology; D011092:Polyethylene Glycols; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D013329:Structure-Activity Relationship
D000214:Acyl Coenzyme A; D004075:Diglycerides; D005989:Glycerides; D010718:Phosphatidylserines; D011092:Polyethylene Glycols; D017830:Octoxynol; D011493:Protein Kinase C; D002118:Calcium