Influence of exercise on free amino acid concentrations in rat tissues

1981 ◽  
Vol 50 (1) ◽  
pp. 41-44 ◽  
Author(s):  
G. L. Dohm ◽  
G. R. Beecher ◽  
R. Q. Warren ◽  
R. T. Williams

Levels of free amino acids in muscle, liver, and plasma were measured in rats that had either swum (1 or 2 h) or run (until exhausted). Exercise lowered alanine levels in all three tissues except for liver of exhausted rats. Exercise decreased the plasma levels of the acidic amino acids and their amides. Glutamate and glutamine levels were depressed in muscle, and the glutamine level was lowered in liver by exercise. Aspartate concentration was lowered by exercise in liver but elevated in muscle. The branched-chain amino acids were generally elevated by exercise as were tyrosine, phenylalanine, methionine, and lysine. Plasma 3-methylhistidine concentration was also elevated by an exercise bout. The changes observed in the amino acid contents of muscle, liver, and plasma are consistent with the increase in protein degradation during exercise that we previously reported. The lowered levels of some amino acids (e.g., alanine, glutamine, glutamate) seem to suggest that amino acid catabolism and/or gluconeogenesis is increased by exercise.

1983 ◽  
Vol 244 (2) ◽  
pp. E151-E158 ◽  
Author(s):  
J. T. Brosnan ◽  
K. C. Man ◽  
D. E. Hall ◽  
S. A. Colbourne ◽  
M. E. Brosnan

Amino acid concentrations in whole blood, liver, kidney, skeletal muscle, and brain were measured and arteriovenous differences calculated for head, hindlimb, kidney, gut, and liver in control and streptozotocin-diabetic rats. In the control rats, glutamine was released by muscle and utilized by intestine, intestine released citrulline and alanine, liver removed alanine, and the kidneys removed glycine and produced serine. In diabetic rats, the major changes from the pattern of fluxes seen in the normal rat were the release of many amino acids from muscle, with glutamine and alanine predominating, and the uptake of these amino acids by the liver. Glutamine removal by the intestine was suppressed in diabetes, but a large renal uptake of glutamine was evident. Branched-chain amino acids were removed by the diabetic brain, and consequently, brain levels of a number of large neutral amino acids were decreased in diabetes.


Author(s):  
Yu. E. Razvodovsky ◽  
V. Yu. Smirnov ◽  
I. N. Semenenya

The effects of complex compositions, containing branched-chain amino acids (BCAA), taurine and tryptophan, on the pool of free amino acids in the liver of rats were studied under the conditions of subchronic alcohol intoxication (SHAI). It was established that SHAI led to the decreased levels of treonine, lysine, oxyproline, arginine, b-alanine, as well as the depletion of the pool of irreplaceable amino acids in the liver of rats. Administration of the composition of BCAA and taurine was found to normalize the ratio of replaceable irreplaceable amino acids, the ratio of glycogenic and ketogenic amino acids, to activate the reaction of nitrogen utilization, and to increase Fisher’s index. The effects of the composition, containing BCAA, taurine and tryptophan, were similar to those of amino acid composition that did not contain tryptophan.


1988 ◽  
Vol 118 (3) ◽  
pp. 311-320 ◽  
Author(s):  
Diane M. Hargrove ◽  
Quinton R. Rogers ◽  
Christopher C. Calvert ◽  
James G. Morris

1991 ◽  
Vol 160 (1) ◽  
pp. 149-165
Author(s):  
J. Henriksson

Protein is not normally an important energy fuel for exercising muscle. In spite of this, there is a significant increase in the rate of amino acid catabolism during exercise. This is secondary to the exercise-induced increase in several metabolic processes, such as hepatic gluconeogenesis and the citric acid cycle, where amino acid carbon is utilized. The suppression of protein synthesis during an exercise bout leaves amino acids available for catabolism. There is some evidence that basal amino acid concentrations in plasma and muscle may be higher in trained than in untrained individuals. In the rat, the concentration of free amino acids is higher in slow-twitch than in fast-twitch muscles. With short-term exercise, the transamination of glutamate by alanine aminotransferase leads to increased levels of alanine in muscle and plasma, and an increased release of alanine from the muscle. At the same time, the muscle and plasma glutamate concentrations are markedly decreased. The plasma glutamine level is elevated with short-term exercise, but changes in muscle glutamine concentration are more variable. With prolonged exercise, there is a depletion of the plasma amino acid pool, which may be explained by an increased consumption in organs other than muscle. With the exception of alanine, we found, however, that the muscle levels of free amino acids are kept stable throughout a 3.5-h exercise period. There is a significant activation of branched-chain amino acid metabolism with prolonged exercise, and the current data indicate that this is more pronounced in endurance-trained subjects than in untrained controls.


Author(s):  
David G Le Couteur ◽  
David J Handelsman ◽  
Fiona Stanaway ◽  
Louise M Waite ◽  
Fiona M Blyth ◽  
...  

Abstract Although characteristic changes in amino acid concentrations occur in obesity and sarcopenia, amino acids concentrations have not been reported in sarcopenic obesity. We studied n=831 men aged 75 years and older from the five-year follow-up of the Concord Health and Ageing in Men Project (CHAMP). Sarcopenia was defined using the Foundation of the National Institutes of Health (FNIH) criteria and obesity was defined as >30% fat mass. There were 31 men (3.7%) who had sarcopenic obesity. Branched chain amino acids were elevated in the obese (but not sarcopenic) group (n=348) but reduced in both the sarcopenic (but not obese) (n=44) and the sarcopenic obese groups. Apart from this, most of the amino acid concentrations were between those for the obese and the sarcopenic groups. Yet despite low concentrations of branched chain amino acids, the sarcopenic obese group had indications of insulin resistance and diabetes mellitus (fasting glucose and insulin concentrations, homeostatic model assessment (HOMA-IR) and percentage of participants taking diabetes medications) that were similar to the obese group. In summary, sarcopenic obese subjects did not have a unique amino acid signature. In obesity, elevated branched chain amino acids are not a prerequisite for insulin resistance and diabetes if obesity is associated with sarcopenia.


2001 ◽  
Vol 40 (3) ◽  
pp. 255-263 ◽  
Author(s):  
Franck Dufour ◽  
Katarzyna A Nalecz ◽  
Maciej J Nalecz ◽  
Astrid Nehlig

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