Ronald H. Cooper

TL;DR: It is concluded that the inhibition of pyruvate dehydrogenase kinase by dichloroacetate may account for the activation of pyrivate dehydration and pyruVate oxidation which it induces in isolated rat heart and diaphragm muscles, subject to certain assumptions as to the distribution of dichlorOacetate across the plasma membrane and the mitochondrial membrane.

TL;DR: This paper showed that pyruvate dehydrogenase in perfused rat heart was decreased by alloxan-diabetes or by perfusion with media containing acetate, n-octanoate or palmitate.

TL;DR: It is presented that in both adipose tissue and heart muscle, differences in activity of pyruvate dehydrogenase in the intact tissue persist during preparation and subsequent incubation of mitochondria.

TL;DR: It is suggested that acetoin formation may contribute to activation of the kinase reaction by low pyruvate concentrations in the presence of thiamin pyrophosphate, and that ADP and adenylyl imidodiphosphate inhibit the Kinase mainly by binding to the ATP site and that the adenosine moiety may be involved in this binding.

TL;DR: The inhibition of pyruvate oxidation by diabetes and by oxidation of fatty acids and ketone bodies is considered to be of crucial importance in the selection of fuels for respiration and in the metabolic changes in heart and other tissues in diabetes and starvation.