Effect of isoproterenol on amino acid levels and protein turnover in skeletal muscle.

1977 ◽  
Vol 232 (2) ◽  
pp. E243
Author(s):  
J B Li ◽  
L S Jefferson

The effect of isoproterenol on amino acid concentrations in perfusate and skeletal muscle was studied during a 3-h perfusion of the isolated rat hemicorpus. The beta-adrenergic agonist inhibited the accumulation of alanine, threonine, phenylalanine, tyrosine, lysine, arginine, leucine, and valine and increased the loss of glutamate, aspartate, serine, and isoleucine from the pool of free amino acids in perfusate and muscle. The loss of glutamate was accompanied by a greater accumulation of glutamine. Changes in alanine levels showed the greatest response with a net accumulation of 98 mumol in the controls becoming a net loss of 54 mumol in the experimentals. These changes in amino acid levels were accounted for in part by a 20% decrease in protein degradation. Protein synthesis was not affected by isoproterenol. In addition to an effect on degradation, it appeared that isoproterenol affected amino acid levels by increasing alanine utilization and causing formation of glutamine instead of alanine. Other effects of the drug included increased rates of lactate production, muscle glycogen breakdown, and oxygen consumption, whereas no effects were observed on ATP and creatine phosphate levels. Pyruvate content of muscle was maintained at a higher level in the presence of the drug than in control perfusions.

1973 ◽  
Vol 59 (1) ◽  
pp. 57-63 ◽  
Author(s):  
W. DE LOECKER ◽  
M. L. STAS

SUMMARY Changes in the concentrations of free amino acids in intracellular fluids and blood plasma were measured in rats treated with cortisol. Increasing age raised the concentrations of free amino acids in plasma, while in liver, with the exception of glycine and alanine, decreased concentrations were observed. Cortisol treatment reduced free amino acid levels in plasma and liver which suggested a progressive catabolism of body proteins and increased protein synthesis in the liver. In skeletal muscle of control rats the free amino acid concentrations increased during the experimental period. Cortisol increased the concentration of certain amino acids and decreased that of others due to an increased protein turnover in muscle.


1985 ◽  
Vol 40 (5-6) ◽  
pp. 427-437 ◽  
Author(s):  
Klaus-Joachim Schott ◽  
Jochen Gehrmann ◽  
Ulla Potter ◽  
Volker Neuhoff

Abstract 1. The effect of ʟ-norleucine, an isomer of leucine, on protein metabolism in vivo was studied in suckling rats. Rats were injected subcutaneously with various doses of ʟ-norleucine (0.5 and 5.0 μmol/g body wt.) every 12 h from 3 to 15 days post partum. Protein concentration, amino acid concentrations, and incorporation of [3H]tyrosine into protein were analyzed in liver, muscles of thigh and small intestine. Amino acid concentrations and insulin levels in serum were also measured. 2. At 5 days of age, norleucine induced an increase in protein concentration of skeletal muscle with an increased incorporation of [3H]tyrosine into protein indicating an accelerated protein synthesis. Changes in protein metabolism were paralleled by alterations in the amino acid pattern of this tissue. 3. When protein concentration and protein synthesis were increased in skeletal muscle, protein concentration of small intestine was decreased, accompanied by elevated levels of amino acids in tissue. Protein synthesis of small intestine was not altered by the norleucine treatment. The results suggest a close interrelationship between skeletal muscle and small intestine with respect to protein turnover. 4. The effects of norleucine were less pronounced at 10 and 15 days of age, which indicates a metabolic adaptation to the treatment. 5. Alterations in amino acid concentrations of tissue due to changes in protein metabolism were not uniform but tissue-specific. 6. Current concepts for explaining the effects of branched-chain amino acids (BCAA) on protein turnover in skeletal muscle are based on the assumption that the BCAA or leucine alone might become rate-limiting for protein synthesis in muscle under catabolic conditions. The amino acid analogue norleucine, however, cannot replace any of the BCAA in protein. Additionally, norleucine affected protein metabolism in highly anabolic organisms. Therefore, the present thoughts on this issue appear to be incomplete.


2019 ◽  
Vol 90 (4) ◽  
pp. 604-609 ◽  
Author(s):  
Daisuke Mashima ◽  
Yoshiaki Oka ◽  
Takafumi Gotoh ◽  
Shozo Tomonaga ◽  
Shoko Sawano ◽  
...  

1962 ◽  
Vol 5 (6) ◽  
pp. 525-532 ◽  
Author(s):  
Yo Aelony ◽  
John Logothetis ◽  
Bruce Bart ◽  
Frank Morrell ◽  
Magdaline Bovis

SpringerPlus ◽  
2013 ◽  
Vol 2 (1) ◽  
pp. 622 ◽  
Author(s):  
Véronique Roucher ◽  
Emmanuelle Desnots ◽  
Charlotte Naël ◽  
Aurore Agnoux ◽  
Marie-Cécile Alexandre-Gouabau ◽  
...  

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