Nutritional regulation of muscle protein synthesis with resistance exercise: strategies to enhance anabolism - PubMed (original) (raw)

Nutritional regulation of muscle protein synthesis with resistance exercise: strategies to enhance anabolism

Tyler A Churchward-Venne et al. Nutr Metab (Lond). 2012.

Abstract

Provision of dietary amino acids increases skeletal muscle protein synthesis (MPS), an effect that is enhanced by prior resistance exercise. As a fundamentally necessary process in the enhancement of muscle mass, strategies to enhance rates of MPS would be beneficial in the development of interventions aimed at increasing skeletal muscle mass particularly when combined with chronic resistance exercise. The purpose of this review article is to provide an update on current findings regarding the nutritional regulation of MPS and highlight nutrition based strategies that may serve to maximize skeletal muscle protein anabolism with resistance exercise. Such factors include timing of protein intake, dietary protein type, the role of leucine as a key anabolic amino acid, and the impact of other macronutrients (i.e. carbohydrate) on the regulation of MPS after resistance exercise. We contend that nutritional strategies that serve to maximally stimulate MPS may be useful in the development of nutrition and exercise based interventions aimed at enhancing skeletal muscle mass which may be of interest to elderly populations and to athletes.

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Figures

Figure 1

Figure 1

Resistance exercise stimulates a prolonged elevation of muscle protein synthesis (MPS) that can remain elevated for ≥ 24 h (dashed lines). Thus, we propose that protein ingestion at any point during this enhanced period of ‘anabolic potential’ will be additive to these already elevated exercise mediated rates (solid line).

Figure 2

Figure 2

Enhanced amino acid sensitivity of myofibrillar protein synthesis (FSR) persists for up to 24 h only after resistance exercise that results in maximal muscle fibre activation induced by high load low volume resistance exercise (90FAIL) or low load high volume resistance exercise (30FAIL). 30WM represents a worked-match control to the 90FAIL condition that did not result in full muscle fibre recruitment. The change in myofibrillar protein synthesis rates are determined from the transition from fasting (FAST) to feeding 15 g of protein at rest (FED) or 24–27 h after resistance exercise in the fasting- (24 h EX FAST) or fed-state (24 h EX-FED). *Significantly different from FED (P < 0.05). †Significantly different from 30WM (P < 0.05). Adptated from Burd and colleagues [27].

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References

    1. Burd NA, Tang JE, Moore DR, Phillips SM. Exercise training and protein metabolism: influences of contraction, protein intake, and sex-based differences. J Appl Physiol. 2009;106:1692–1701. - PubMed
    1. Kumar V, Atherton P, Smith K, Rennie MJ. Human muscle protein synthesis and breakdown during and after exercise. J Appl Physiol. 2009;106:2026–2039. - PubMed
    1. Biolo G, Tipton KD, Klein S, Wolfe RR. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am J Physiol. 1997;273:E122–E129. - PubMed
    1. Cuthbertson D, Smith K, Babraj J, Leese G, Waddell T, Atherton P, Wackerhage H, Taylor PM, Rennie MJ. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. The FASEB journal: official publication of the Federation of American Societies for Experimental Biology. 2005;19:422–424. - PubMed
    1. Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, Prior T, Tarnopolsky MA, Phillips SM. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr. 2009;89:161–168. - PubMed

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