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  • Title: Interrelationship in the regulation of pyruvate dehydrogenase and adenine-nucleotide translocase by palmitoyl-CoA in isolated mitochondria.
    Author: Shrago E, Ball M, Sul HS, Baquer NZ, McLean P.
    Journal: Eur J Biochem; 1977 May 02; 75(1):83-9. PubMed ID: 862623.
    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 also 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.
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