Persistent activity modification of phosphatidate phosphohydrolase and fatty acyl-CoA synthetase on incubation of adipocytes with the tumour promoter 12-O-tetradecanoylphorbol 13-acetate.
Incubation of rat adipocytes with the phorbol ester TPA caused a dose-dependent, persistent increase in phosphatidate phosphohydrolase activity and decrease in fatty acyl-CoA synthetase activity. Half-maximal effects were obtained with 1-2 X 10(-10) M TPA. TPA did not alter basal or noradrenaline-stimulated lipolysis. It is suggested that these two enzymes might be modified by protein kinase C.
Hall
M
M
Taylor
S J
SJ
Saggerson
E D
ED
D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D003066:Coenzyme A Ligases / Q000037:antagonists & inhibitors*; D004789:Enzyme Activation / Q000187:drug effects; D008066:Lipolysis / Q000187:drug effects; D009638:Norepinephrine / Q000494:pharmacology; D010704:Phorbols / Q000494:pharmacology*; D010711:Phosphatidate Phosphatase / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011493:Protein Kinase C; D011494:Protein Kinases / Q000502:physiology; D051381:Rats; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D010704:Phorbols; D011494:Protein Kinases; D011493:Protein Kinase C; D010744:Phosphoric Monoester Hydrolases; D010711:Phosphatidate Phosphatase; D003066:Coenzyme A Ligases; D013755:Tetradecanoylphorbol Acetate; D009638:Norepinephrine