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Branched-chain amino acids and muscle protein synthesis in humans: myth or reality?
The branched chain amino acids (BCAAs) are leucine, valine and isoleucine. A multi-million dollar industry of nutritional supplements has grown around the concept that dietary supplements of BCAAs alone produce an anabolic response in humans driven by a stimulation of muscle protein synthesis. In this brief review the theoretical and empirical bases for that claim are discussed. Theoretically, the maximal stimulation of muscle protein synthesis in the post-absorptive state in response to BCAAs alone is the difference between muscle protein breakdown and muscle protein synthesis (about 30% greater than synthesis), because the other EAAs required for synthesis of new protein can only be derived from muscle protein breakdown. Realistically, a maximal increase in muscle protein synthesis of 30% is an over-estimate because the obligatory oxidation of EAAs can never be completely suppressed. An extensive search of the literature has revealed no studies in human subjects in which the response of muscle protein synthesis to orally-ingested BCAAs alone was quantified, and only two studies in which the effect of intravenously infused BCAAs alone was assessed. Both of these intravenous infusion studies found that BCAAs decreased muscle protein synthesis as well as protein breakdown, meaning a decrease in muscle protein turnover. The catabolic state in which the rate of muscle protein breakdown exceeded the rate of muscle protein synthesis persisted during BCAA infusion.
We conclude that the claim that consumption of dietary BCAAs stimulates muscle protein synthesis or produces an anabolic response in human subjects is unwarranted.
Conclusion
A physiologically-significant increase in the rate of muscle protein synthesis requires adequate availability of all amino acid precursors. The source of EAAs for muscle protein synthesis in the post-absorptive state is the free intracellular pool. Intracellular free EAAs that are available for incorporation into protein are derived from muscle protein breakdown. Under normal conditions about 70% of EAAs released by muscle protein breakdown are reincorporated into muscle protein. The efficiency of reincorporation of EAAs from protein breakdown back into muscle protein can only be increased to a limited extent. For this fundamental reason, a dietary supplement of BCAAs alone cannot support an increased rate of muscle protein synthesis. The availability of the other EAAs will rapidly become rate limiting for accelerated protein synthesis. Consistent with this perspective, the few studies in human subjects have reported decreases, rather than increases, in muscle protein synthesis after intake of BCAAs. We conclude that dietary BCAA supplements alone do not promote muscle anabolism.
Branched-chain amino acids and muscle protein synthesis in humans: myth or reality?
Bron:Journal of the International Society of Sports Nutrition
- Robert R. Wolfe
© The Author(s). 201
Received: 17 February 2017
Accepted: 1 August 2017
Published: 22 August 2017
The branched chain amino acids (BCAAs) are leucine, valine and isoleucine. A multi-million dollar industry of nutritional supplements has grown around the concept that dietary supplements of BCAAs alone produce an anabolic response in humans driven by a stimulation of muscle protein synthesis. In this brief review the theoretical and empirical bases for that claim are discussed. Theoretically, the maximal stimulation of muscle protein synthesis in the post-absorptive state in response to BCAAs alone is the difference between muscle protein breakdown and muscle protein synthesis (about 30% greater than synthesis), because the other EAAs required for synthesis of new protein can only be derived from muscle protein breakdown. Realistically, a maximal increase in muscle protein synthesis of 30% is an over-estimate because the obligatory oxidation of EAAs can never be completely suppressed. An extensive search of the literature has revealed no studies in human subjects in which the response of muscle protein synthesis to orally-ingested BCAAs alone was quantified, and only two studies in which the effect of intravenously infused BCAAs alone was assessed. Both of these intravenous infusion studies found that BCAAs decreased muscle protein synthesis as well as protein breakdown, meaning a decrease in muscle protein turnover. The catabolic state in which the rate of muscle protein breakdown exceeded the rate of muscle protein synthesis persisted during BCAA infusion.
We conclude that the claim that consumption of dietary BCAAs stimulates muscle protein synthesis or produces an anabolic response in human subjects is unwarranted.
Conclusion
A physiologically-significant increase in the rate of muscle protein synthesis requires adequate availability of all amino acid precursors. The source of EAAs for muscle protein synthesis in the post-absorptive state is the free intracellular pool. Intracellular free EAAs that are available for incorporation into protein are derived from muscle protein breakdown. Under normal conditions about 70% of EAAs released by muscle protein breakdown are reincorporated into muscle protein. The efficiency of reincorporation of EAAs from protein breakdown back into muscle protein can only be increased to a limited extent. For this fundamental reason, a dietary supplement of BCAAs alone cannot support an increased rate of muscle protein synthesis. The availability of the other EAAs will rapidly become rate limiting for accelerated protein synthesis. Consistent with this perspective, the few studies in human subjects have reported decreases, rather than increases, in muscle protein synthesis after intake of BCAAs. We conclude that dietary BCAA supplements alone do not promote muscle anabolism.
Branched-chain amino acids and muscle protein synthesis in humans: myth or reality?
Bron:Journal of the International Society of Sports Nutrition
