The effect of dichloroacetate on the phosphorylation of mitochondria proteins.
Succinyl-CoA synthetase and the alpha-subunit of pyruvate dehydrogenase are phosphorylated after incubation of mitochondria from brain, heart, and liver with [gamma-32P]ATP. Dichloroacetate, a known specific inhibitor for pyruvate dehydrogenase kinase, inhibits not only the phosphate incorporation into the alpha-subunit of pyruvate dehydrogenase but also the autophosphorylation of succinyl-CoA synthetase. AMP also inhibits the phosphorylation of both proteins. Phosphorylation of the alpha-subunit of pyruvate dehydrogenase in liver mitochondria is significantly lower than in mitochondria from other tissues.
D000085:Acetates / Q000494:pharmacology*; D000818:Animals; D001921:Brain / Q000201:enzymology; D003066:Coenzyme A Ligases / Q000037:antagonists & inhibitors*; D003999:Dichloroacetic Acid / Q000494:pharmacology*; D005260:Female; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011768:Pyruvate Dehydrogenase Complex / Q000037:antagonists & inhibitors*; D051381:Rats; D011919:Rats, Inbred Strains; D013389:Succinate-CoA Ligases / Q000037:antagonists & inhibitors*
D000085:Acetates; D010750:Phosphoproteins; D011768:Pyruvate Dehydrogenase Complex; D003999:Dichloroacetic Acid; D003066:Coenzyme A Ligases; D013389:Succinate-CoA Ligases