The present study was conducted to investigate the metabolic regulation of leucine oxidation during exercise. Ten rats per group were run at 27 m/min (0% grade) on a treadmill for 30 and 120 min or until exhausted, and the total and basal activity of branched-chain keto acid dehydrogenase was examined in the muscle, liver, and heart. The total activity of the dehydrogenase in the heart, liver, or skeletal muscle was unchanged by exercise. However, exercise increased the basal activity levels of the dehydrogenase about 10-fold in muscle and 5-fold in heart. The basal dehydrogenase activity in the liver was unchanged by exercise. Activation of the dehydrogenase in both muscle and heart was statistically elevated after 30 min exercise and continued to increase during the remainder of the exercise bout. The basal activity of the dehydrogenase returned to resting levels by 10 min postexercise. The activation of the dehydrogenase in muscle and heart during exercise likely is due to dephosphorylation because activity of the enzyme in mitochondria isolated from exercised muscles reverts to control values when the mitochondria are incubated in the presence of ATP. Thus the increased leucine oxidation observed during exercise is due to activation of the branched-chain keto acid dehydrogenase by dephosphorylation. This is the first example of a large increase in branched-chain keto acid dehydrogenase activity caused by a physiological process. This demonstrates that the muscle's latent capacity of oxidize branched-chain amino acids is much larger than previously thought and that this capacity is used in exercising muscle.
Effects of dietary protein intake on branched-chain keto acid dehydrogenase activity of the rat. Immunochemical analysis of the enzyme complex.
