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PYRUVATE DEHYDROGENASE ACTIVATION IN RAT BRAIN CORTICAL SLICES BY ELEVATED CONCENTRATIONS OF EXTERNAL POTASSIUM IONS

Abstract— Cortical slices from rat brain were incubated in Krebs‐Ringer phosphate medium. Activity of the pyruvate dehydrogenase complex (PDH) was measured in homogenates of the incubated tissue. Increasing the extracellular KCI concentration from 5 to 75 mM caused a dose‐dependent increase in activity of this rate‐limiting mitochondrial enzyme. The increase in PDH activity, produced by high concentration of KCI. was associated with a decrease in the tissue content of ATP. Omission of calcium, or replacement of sodium by choline, reduced, and addition of ouabain prevented, the activation of the enzyme in the depolarized tissue.