Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis following Resistance Exercise in Humans
- PMID: 28638350
- PMCID: PMC5461297
- DOI: 10.3389/fphys.2017.00390
Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis following Resistance Exercise in Humans
Abstract
The ingestion of intact protein or essential amino acids (EAA) stimulates mechanistic target of rapamycin complex-1 (mTORC1) signaling and muscle protein synthesis (MPS) following resistance exercise. The purpose of this study was to investigate the response of myofibrillar-MPS to ingestion of branched-chain amino acids (BCAAs) only (i.e., without concurrent ingestion of other EAA, intact protein, or other macronutrients) following resistance exercise in humans. Ten young (20.1 ± 1.3 years), resistance-trained men completed two trials, ingesting either 5.6 g BCAA or a placebo (PLA) drink immediately after resistance exercise. Myofibrillar-MPS was measured during exercise recovery with a primed, constant infusion of L-[ring13C6] phenylalanine and collection of muscle biopsies pre and 4 h-post drink ingestion. Blood samples were collected at time-points before and after drink ingestion. Western blotting was used to measure the phosphorylation status of mTORC1 signaling proteins in biopsies collected pre, 1-, and 4 h-post drink. The percentage increase from baseline in plasma leucine (300 ± 96%), isoleucine (300 ± 88%), and valine (144 ± 59%) concentrations peaked 0.5 h-post drink in BCAA. A greater phosphorylation status of S6K1Thr389 (P = 0.017) and PRAS40 (P = 0.037) was observed in BCAA than PLA at 1 h-post drink ingestion. Myofibrillar-MPS was 22% higher (P = 0.012) in BCAA (0.110 ± 0.009%/h) than PLA (0.090 ± 0.006%/h). Phenylalanine Ra was ~6% lower in BCAA (18.00 ± 4.31 μmol·kgBM-1) than PLA (21.75 ± 4.89 μmol·kgBM-1; P = 0.028) after drink ingestion. We conclude that ingesting BCAAs alone increases the post-exercise stimulation of myofibrillar-MPS and phosphorylation status mTORC1 signaling.
Keywords: amino acid ingestion; fractional synthesis rate; intracellular signaling proteins; leucine; muscle anabolism.
Figures
![Figure 1](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/5461297/bin/fphys-08-00390-g0001.gif)
![Figure 2](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/5461297/bin/fphys-08-00390-g0002.gif)
![Figure 3](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/5461297/bin/fphys-08-00390-g0003.gif)
![Figure 4](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/5461297/bin/fphys-08-00390-g0004.gif)
![Figure 5](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/5461297/bin/fphys-08-00390-g0005.gif)
![Figure 6](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/5461297/bin/fphys-08-00390-g0006.gif)
Similar articles
-
Co-Ingestion of Branched-Chain Amino Acids and Carbohydrate Stimulates Myofibrillar Protein Synthesis Following Resistance Exercise in Trained Young Men.Int J Sport Nutr Exerc Metab. 2023 May 24;33(4):189-197. doi: 10.1123/ijsnem.2023-0015. Print 2023 Jul 1. Int J Sport Nutr Exerc Metab. 2023. PMID: 37225168
-
Branched-chain amino acid and branched-chain ketoacid ingestion increases muscle protein synthesis rates in vivo in older adults: a double-blind, randomized trial.Am J Clin Nutr. 2019 Oct 1;110(4):862-872. doi: 10.1093/ajcn/nqz120. Am J Clin Nutr. 2019. PMID: 31250889 Free PMC article. Clinical Trial.
-
Activation of mTORC1 by leucine is potentiated by branched-chain amino acids and even more so by essential amino acids following resistance exercise.Am J Physiol Cell Physiol. 2016 Jun 1;310(11):C874-84. doi: 10.1152/ajpcell.00374.2015. Epub 2016 Apr 6. Am J Physiol Cell Physiol. 2016. PMID: 27053525 Clinical Trial.
-
The effects of branched-chain amino acids on muscle protein synthesis, muscle protein breakdown and associated molecular signalling responses in humans: an update.Nutr Res Rev. 2023 Sep 8:1-14. doi: 10.1017/S0954422423000197. Online ahead of print. Nutr Res Rev. 2023. PMID: 37681443 Review.
-
International society of sports nutrition position stand: nutrient timing.J Int Soc Sports Nutr. 2017 Aug 29;14:33. doi: 10.1186/s12970-017-0189-4. eCollection 2017. J Int Soc Sports Nutr. 2017. PMID: 28919842 Free PMC article. Review.
Cited by
-
Influence of Amino Acids and Exercise on Muscle Protein Turnover, Particularly in Cancer Cachexia.Cancers (Basel). 2024 May 18;16(10):1921. doi: 10.3390/cancers16101921. Cancers (Basel). 2024. PMID: 38791998 Free PMC article. Review.
-
The biphasic activity of autophagy and heat shock protein response in peripheral blood mononuclear cells following acute resistance exercise in resistance-trained males.Eur J Appl Physiol. 2024 May 21. doi: 10.1007/s00421-024-05503-5. Online ahead of print. Eur J Appl Physiol. 2024. PMID: 38771358
-
Chilean Market Protein Shakes Composition.Nutrients. 2024 Apr 11;16(8):1129. doi: 10.3390/nu16081129. Nutrients. 2024. PMID: 38674821 Free PMC article.
-
Supplementation for Performance and Health in Patients with Phenylketonuria: An Exercise-Based Approach to Improving Dietary Adherence.Nutrients. 2024 Feb 25;16(5):639. doi: 10.3390/nu16050639. Nutrients. 2024. PMID: 38474766 Free PMC article. Review.
-
Marine-derived protein: peptide bioresources for the development of nutraceuticals for improved athletic performance.Front Sports Act Living. 2023 Oct 30;5:1281397. doi: 10.3389/fspor.2023.1281397. eCollection 2023. Front Sports Act Living. 2023. PMID: 37964773 Free PMC article. No abstract available.
References
-
- Anthony J. C., Anthony T. G., Kimball S. R., Vary T. C., Jefferson L. S. (2000). Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation. J. Nutr. 130, 139–145. - PubMed
-
- Anthony J. C., Anthony T. G., Layman D. K. (1999). Leucine supplementation enhances skeletal muscle recovery in rats following exercise. J. Nutr. 129, 1102–1106. - PubMed
-
- Atherton P. J., Etheridge T., Watt P. W., Wilkinson D., Selby A., Rankin D., et al. . (2010a). Muscle full effect after oral protein: time-dependent concordance and discordance between human muscle protein synthesis and mTORC1 signaling. Am. J. Clin. Nutr. 92, 1080–1088. 10.3945/ajcn.2010.29819 - DOI - PubMed
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous