MODULATION OF BRANCHED-CHAIN KETO ACID DEHYDROGENASE ACTIVITY IN RAT LIVER

1981 ◽  
Vol 9 (2) ◽  
pp. 235P-235P
Author(s):  
B. H. Robinson ◽  
N. MacKay
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Keto Acid ◽  
Acid Dehydrogenase ◽  
Branched Chain

Activation of branched-chain keto acid dehydrogenase by exercise

1985 ◽  
Vol 248 (2) ◽  
pp. R166-R171 ◽  
Author(s):  
G. J. Kasperek ◽  
G. L. Dohm ◽  
R. D. Snider
Keyword(s):  
Dehydrogenase Activity ◽  
Metabolic Regulation ◽  
Exercise Bout ◽  
Total Activity ◽  
Activity Levels ◽  
Keto Acid ◽  
Leucine Oxidation ◽  
Basal Activity ◽  
Acid Dehydrogenase ◽  
Branched Chain

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.

scholarly journals Alteration in gene expression of branched-chain keto acid dehydrogenase kinase but not in gene expression of its substrate in the liver of clofibrate-treated rats

1996 ◽  
Vol 317 (2) ◽  
pp. 411-417 ◽  
Author(s):  
Harbhajan S. PAUL ◽  
Wei-Qun LIU ◽  
Siamak A. ADIBI
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
Fold Increase ◽  
Branched Chain Amino Acids ◽  
The Other ◽  
Mrna Levels ◽  
Keto Acid ◽  
Protein Mass ◽  
Acid Dehydrogenase ◽  
Branched Chain

We previously showed that the oxidation of branched-chain amino acids is increased in rats treated with clofibrate [Paul and Adibi (1980) J. Clin. Invest. 65, 1285–1293]. Two subsequent studies have reported contradictory results regarding the effect of clofibrate treatment on gene expression of branched-chain keto acid dehydrogenase (BCKDH) in rat liver. Furthermore, there has been no previous study of the effect of clofibrate treatment on gene expression of BCKDH kinase, which regulates the activity of BCKDH by phosphorylation. The purpose of the present study was to investigate the above issues. Clofibrate treatment for 2 weeks resulted in (a) a 3-fold increase in the flux through BCKDH in mitochondria isolated from rat liver, and (b) a modest but significant increase in the activity of BCKDH. However, clofibrate treatment had no significant effect on the mass of E1α, E1β, and E2 subunits of BCKDH or the abundance of mRNAs encoding these subunits. On the other hand, clofibrate treatment significantly reduced the activity, the protein mass and the mRNA levels of BCKDH kinase in the liver. In contrast to the results obtained in liver, clofibrate treatment had no significant effect on any of these parameters of BCKDH kinase in the skeletal muscle. In conclusion, our results show that clofibrate treatment increases the activity of BCKDH in the liver and the mechanism of this effect is the inhibition of gene expression of the BCKDH kinase.

scholarly journals Regulation of Branched-Chain α-Keto Acid Dehydrogenase Kinase Expression in Rat Liver

2001 ◽  
Vol 131 (3) ◽  
pp. 841S-845S ◽  
Author(s):  
Robert A. Harris ◽  
Rumi Kobayashi ◽  
Taro Murakami ◽  
Yoshiharu Shimomura
Keyword(s):  
Rat Liver ◽  
Keto Acid ◽  
Acid Dehydrogenase ◽  
Branched Chain ◽  
Kinase Expression
Sign in / Sign up

Export Citation Format

Share Document