Influence of glucagon or 5-(tetradecyloxy)-2-furoic acid on binding to mitochondria and phosphorylation of ATP-citrate lyase.
To study the binding to mitochondria and the phosphorylation of ATP-citrate lyase (EC 4.1.3.8), isolated rat hepatocytes were fractionated by exposure to digitonin. After incubation of hepatocytes with the hypolipidemic agent 5-(tetradecyloxy)-2-furoic acid, which decreases the cellular CoA, the amount of bound ATP-citrate lyase was increased, but the content of acid-stable phosphate in the enzyme was diminished. Glucagon, in contrast, decreased the amount of bound enzyme but increased phosphorylation. This inverse relationship might indicate either that the bound ATP-citrate lyase is less readily phosphorylated or that the phosphorylated enzyme binds less readily to mitochondria.
D001275:ATP Citrate (pro-S)-Lyase / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D003065:Coenzyme A / Q000378:metabolism; D005663:Furans / Q000494:pharmacology*; D005934:Glucagon / Q000494:pharmacology*; D008297:Male; D008930:Mitochondria, Liver / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats
D005663:Furans; C014289:5-(tetradecyloxy)-2-furancarboxylic acid; D005934:Glucagon; D001275:ATP Citrate (pro-S)-Lyase; D003065:Coenzyme A