Stimulation by a tumor-promoting phorbol ester of acetyl-CoA carboxylase activity in isolated rat hepatocytes.
Acetyl-CoA carboxylase (EC 6.4.1.2) in hepatocytes from meal-fed rats was activated by phorbol myristate acetate (PMA) in a time- and concentration-dependent fashion. This activation can account for the PMA-induced stimulation of de novo fatty acid synthesis. Purified rat-liver acetyl-CoA carboxylase was found to be phosphorylated and activated by protein kinase C, thus providing a possible mechanism for the metabolic action of PMA in intact hepatocytes.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000494:Allosteric Regulation; D000818:Animals; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation / Q000187:drug effects; D005227:Fatty Acids / Q000096:biosynthesis; D006843:Hydrocarbons, Chlorinated; D007773:Lactates / Q000378:metabolism; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D010766:Phosphorylation; D011422:Propionates / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism; D051381:Rats; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D005227:Fatty Acids; D006843:Hydrocarbons, Chlorinated; D007773:Lactates; D011422:Propionates; C021974:2-chloropropionic acid; D011493:Protein Kinase C; D008025:Ligases; D000103:Acetyl-CoA Carboxylase; D013755:Tetradecanoylphorbol Acetate