Branched-chain amino acid interactions in skeletal muscle: isoleucine and L-alloisoleucine.

  title={Branched-chain amino acid interactions in skeletal muscle: isoleucine and L-alloisoleucine.},
  author={Richard S. Downey and Irene E. Karl and Dennis Bier},
  journal={JPEN. Journal of parenteral and enteral nutrition},
  volume={10 5},
  • R. Downey, I. Karl, D. Bier
  • Published 1 September 1986
  • Chemistry, Medicine
  • JPEN. Journal of parenteral and enteral nutrition
Parenteral administration of a mixture of branched-chain amino acid (BCAA) solutions is known to alter plasma levels of the BCAA (ILE, LEU, VAL), their corresponding alpha-ketoacids (KMV, KIC, KIV) and L-alloisoleucine (ALLO), a stereoisomer of ILE. Although variously formulated mixtures of BCAA are administered, the metabolic implications of individual BCAA interactions have been only partially elucidated. Using the incubated, isolated, and intact rat epitrochlearis muscle, we measured the… Expand
4 Citations
Role of branched-chain ketoacids in protein metabolism.
  • M. Walser
  • Biology, Medicine
  • Kidney international
  • 1990
The purpose of this review is to summarize the current knowledge concerning the role of endogenous BCKA in protein metabolism and the effect of exogenous BCKA on N balance, with particular reference to renal failure. Expand
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The mechanism of action of sparkers has been re-assessed and there are certain sparker effects with glutamine and glutamate which cannot be explained on the basis of the earlier hypothesis that sparkers provide ATP for the synthesis of fatty acyl CoA cannot explain their effect on ketoleucine metabolism. Expand
Nitrogen sparing induced early in starvation by infusion of branched-chain ketoacids.
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Racemization and amination of the keto-analog of isoleucine in the intact dog.
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Valine metabolism in vivo: effects of high dietary levels of leucine and isoleucine.
Consumption of excess leucine had no significant effect on either muscle or liver aminotransferase activities, but was associated with a greater than two-fold increase in hepatic dehydrogenase activity. Expand
Demonstration of a new mammalian isoleucine catabolic pathway yielding an Rseries of metabolites.
The further oxidation of 2-ethylhydracrylic acid to ethylmalonic acid was demonstrated, and may be analogous to S-metabolite oxidation via methyl malonate. Expand
Leucine. A possible regulator of protein turnover in muscle.
  • M. Buse, S. Reid
  • Medicine, Biology
  • The Journal of clinical investigation
  • 1975
The concentration of leucine in muscle cells or a compartment thereof may play a role in regulating the turnover of muscle proteins and influence the transition to negative nitrogen balance during fasting, uncontrolled diabetes, and the posttraumatic state. Expand
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It is concluded that this mixture and dosage of amino acid analogues can meet the dietary requirements of chronic uremic patients for methionine, valine, leucine and isoleucine. Expand
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Although the two complete amino acid mixtures produced similar nitrogen preservation and muscle synthesis in the septic animals, the crystalline amino acid diet containing 50% branched chain amino acids resulted in the greatest preservation of total liver nitrogen and the highest fractional synthetic rate. Expand