Interrelationship in the Regulation of Pyruvate Dehydrogenase and Adenine-Nucleotide Translocase by Palmitoyl-CoA in Isolated Mitochondria

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Abstract
Full activation of rat liver pyruvate dehydrogenase in vitro by ADP was prevented by palmitoyl-CoA at a concentration sufficiently low to preclude substrate effects secondary to its oxidation by mitochondria. Activation of pyruvate dehydrogenase by ADP in livers of fat-fed rats was less than in the control animal. The results are consistent with the experiments demonstrating an inhibition of adenine nucleotide translocase and on increased intramitochondrial ATP/ADP ratio by palmitoyl-CoA which could account for the effect on pyruvate dehydrogenase. Inactivation of brain pyruvate dehydrogenase by ATP was diminished by palmitoyl-CoA indicating that the effect was at the level of the adenine nucleotides rather than at either the pyruvate dehydrogenase kinase or phosphatase enzymes.