Exercise in ZDF rats does not attenuate weight gain, but prevents hyperglycemia concurrent with modulation of amino acid metabolism and AKT/mTOR activation in skeletal muscle

2014 ◽  
Vol 54 (5) ◽  
pp. 751-759 ◽  
Author(s):  
Olasunkanmi A. J. Adegoke ◽  
Holly E. Bates ◽  
Michael A. Kiraly ◽  
Mladen Vranic ◽  
Michael C. Riddell ◽  
...  
1978 ◽  
Vol 96 (3) ◽  
pp. 309-317 ◽  
Author(s):  
William M. Pardridge ◽  
Mayer B. Davidson ◽  
Delia Casanello-Ertl

2019 ◽  
Vol 76 (22) ◽  
pp. 4551-4568 ◽  
Author(s):  
Felix Schmöhl ◽  
Verena Peters ◽  
Claus Peter Schmitt ◽  
Gernot Poschet ◽  
Michael Büttner ◽  
...  

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


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