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- W2094654811 abstract "Liver mitochondria isolated from glucagon-treated rats have been previously shown to exhibit stimulated rates of pyruvate carboxylation and pyruvate decarboxylation as compared with controls. Under these same conditions there is no change in the total activity of pyruvate carboxylase as assayed with saturating concentrations of substrates and acetyl-CoA. Arsenite additions to mitochondria have been used to cause inhibition of pyruvate dehydrogenase, allowing a study of the relationship between pyruvate dehydrogenase and the glucagon stimulation of pyruvate carboxylation. Preincubation of mitochondria with arsenite inhibits pyruvate carboxylation 95%, presumably through inhibition of pyruvate dehydrogenase and subsequent loss of acetyl-CoA, NADH, and ATP. Addition of 30 μm palmitoyl-carnitine restores pyruvate carboxylation to the same level as in uninhibited mitochondria without palmitoyl-carnitine, and the glucagon stimulation is still observed. In mitochondria not inhibited with arsenite, progressive inhibition of pyruvate decarboxylation with increasing palmitoyl-carnitine is seen. Pyruvate carboxylation shows a biphasic response, increasing at palmitoyl-carnitine concentrations up to 30 μm but then decreasing above these concentrations. These results indicate that pyruvate dehydrogenase and pyruvate carboxylase are not necessarily linked in a compulsory manner and that pyruvate dehydrogenase can be ruled out as a primary site of glucagon action. Glucagon stimulation of pyruvate entry into mitochondria is consistent with the above observations." @default.
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- W2094654811 title "Dissociation of pyruvate dehydrogenase from the glucagon stimulation of pyruvate carboxylation in rat liver mitochondria" @default.
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