Tarun B. Patel

TL;DR: It is contention that the inactivation of pyruvate dehydrogenase complex at low propionate levels may be due to an increase in the mitochondrial acyl-CoA/CoASH ratios, whereas the activation of the enzyme complex demonstrated at high propionATE levels is due to the inhibition of the pyruVate dehydrogensase kinase in a manner similar to that caused by pyruviate or dichloroacetic acid.

TL;DR: Evidence is provided suggesting that the stimulation of the flux through the pyruvate dehydrogenase reaction by β-hydroxybutyrate or other precursors of acetoacetate observed at low pyruviate concentrations is a result of an accelerated exchange of cytosolic pyruVate for intramitochondrially generated aceto acetate on the monocarboxylate translocator.

TL;DR: The regulatory consequences of acetate infusion on the pyruvate and the branched chain α-keto acid dehydrogenase reactions in the isolated, perfused rat liver were investigated.

TL;DR: It is demonstrated that glucagon and phenylephrine stimulation of the rate of 14CO2 production from [1-14C]lactate is a result of increased metabolic flux through the phosphoenolpyruvate carboxykinase reaction, and Phenylephrine-stimulated gluconeogenesis from pyruvates is regulated at step(s) between phosphoenolate and glucose.

TL;DR: Results indicate that during rapid ketogenesis, cytosolic transamination of alanine contributes at least 19% and 55% of the pyruvate for gluconeogenesis.