Regulation of branched-chain amino acid metabolism and pharmacological effects of branched-chain amino acids

2004 ◽  
Vol 30 ◽  
pp. 3-8 ◽  
Author(s):  
Y SHIMOMURA ◽  
T MURAKAMI ◽  
M NAGASAKI ◽  
T HONDA ◽  
H GOTO ◽  
...  
2004 ◽  
Vol 82 (7) ◽  
pp. 506-514 ◽  
Author(s):  
Enoka P Wijekoon ◽  
Craig Skinner ◽  
Margaret E Brosnan ◽  
John T Brosnan

We investigated amino acid metabolism in the Zucker diabetic fatty (ZDF Gmi fa/fa) rat during the prediabetic insulin-resistant stage and the frank type 2 diabetic stage. Amino acids were measured in plasma, liver, and skeletal muscle, and the ratios of plasma/liver and plasma/skeletal muscle were calculated. At the insulin-resistant stage, the plasma concentrations of the gluconeogenic amino acids aspartate, serine, glutamine, glycine, and histidine were decreased in the ZDF Gmi fa/fa rats, whereas taurine, α-aminoadipic acid, methionine, phenylalanine, tryptophan, and the 3 branched-chain amino acids were significantly increased. At the diabetic stage, a larger number of gluconeogenic amino acids had decreased plasma concentrations. The 3 branched-chain amino acids had elevated plasma concentrations. In the liver and the skeletal muscles, concentrations of many of the gluconeogenic amino acids were lower at both stages, whereas the levels of 1 or all of the branched-chain amino acids were elevated. These changes in amino acid concentrations are similar to changes seen in type 1 diabetes. It is evident that insulin resistance alone is capable of bringing about many of the changes in amino acid metabolism observed in type 2 diabetes.Key words: plasma amino acids, liver amino acids, muscle amino acids, gluconeogenesis.


2002 ◽  
Vol 27 (6) ◽  
pp. 646-662 ◽  
Author(s):  
Donald K. Layman

Exercise produces changes in protein and amino acid metabolism. These changes include degradation of the branched-chain amino acids, production of alanine and glutamine, and changes in protein turnover. One of the amino acid most affected by exercise is the branched-chain amino acid leucine. Recently, there has been an increased understanding of the role of leucine in metabolic regulations and remarkable new findings about the role of leucine in intracellular signaling. Leucine appears to exert a synergistic role with insulin as a regulatory factor in the insulin/phosphatidylinositol-3 kinase (PI3-K) signal cascade. Insulin serves to activate the signal pathway, while leucine is essential to enhance or amplify the signal for protein synthesis at the level of peptide initiation. Studies feeding amino acids or leucine soon after exercise suggest that post-exercise consumption of amino acids stimulates recovery of muscle protein synthesis via translation regulations. This review focuses on the unique roles of leucine in amino acid metabolism in skeletal muscle during and after exercise. Key words: branched-chain amino acids, insulin, protein synthesis, skeletal muscle


1990 ◽  
Vol 258 (5) ◽  
pp. E878-E887
Author(s):  
S. Del Prato ◽  
R. A. DeFronzo ◽  
P. Castellino ◽  
J. Wahren ◽  
A. Alvestrand

The effect of epinephrine on amino acid (AA) metabolism was examined in 33 healthy volunteers who participated in four studies. Nine subjects participated in study I, which consisted of four parts: euglycemic insulin clamp, insulin plus epinephrine, insulin plus epinephrine plus propranolol, and insulin plus propranolol. In study II six subjects received epinephrine with hepatic-femoral venous catheterization. In study III five individuals received epinephrine with somatostatin plus basal insulin replacement. In study IV quadriceps muscle biopsy was performed in six subjects after epinephrine or insulin infusion. Both epinephrine and insulin caused a generalized decline in all plasma AA except alanine. With combined epinephrine-insulin infusion, the decrease in plasma AA was additive. Propranolol blocked the hypoaminoacidemic effect of epinephrine but failed to alter the AA lowering action of insulin. Epinephrine, while maintaining basal insulinemia, reduced the catechol's hypoaminoacidemic effect by 39%. After epinephrine, splanchnic alanine uptake increased, but plasma alanine remained constant because of a parallel rise in muscle alanine production. Plasma/intracellular concentrations of branched-chain amino acids (BCAA) and all gluconeogenic amino acids, except alanine, decreased after both epinephrine and insulin. In summary, the effect of epinephrine on plasma/intracellular total, gluconeogenic, and BCAA concentrations is similar to insulin.


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