Please ensure Javascript is enabled for purposes of website accessibility PURE LEUCINE POST WORKOUT INCREASES MUSCLE GROWTH FACTOR (IGF-1)

My Cart

Close

science nutrition blog

science nutrition <strong>blog</strong>

By Steve Blechman

 

Leucine is an essential amino acid that serves as a building block for muscle protein synthesis. Leucine is a powerful anabolic trigger— it’s the most potent branched-chain amino acid (BCAA) of the mTOR pathway that is critical for muscle protein synthesis that promotes muscle growth. Leucine has many growth benefits: preventing muscle loss, increasing insulin sensitivity, enhancing fat metabolism and enhancing recovery.

A randomized controlled study published in the Journal of the American College of Nutrition found that taking 3 grams of pure leucine after resistance training exercise increased muscle insulin-like growth factor 1 (IGF-1). IGF-1 is a potent anabolic hormone derived from growth hormone. Increased IGF-1 in muscle can increase muscle protein synthesis and muscle growth. IGF-1 also increases lean body mass and enhances tissue repair and accelerates recovery. What’s most significant of this randomized trial was the acute increase of IGF-1, not only in blood, but significantly, two hours and six hours post resistance training exercise in muscle after a single dose of 3 grams of leucine but not the placebo! Increasing igf-1 in muscle is key for stimulating muscle protein synthesis. In this study, “Nine resistance-trained men performed 3 lower-body resistance exercise sessions involving 4 sets of 8-10 repetitions at 75%-80% one repetition maximum (1-RM) on the angled leg press and knee extension exercises. Immediately following each session, participants orally ingested 3 g cellulose placebo (PLC), l-leucine (LEU), or ursolic acid (UA). Blood samples were obtained pre-exercise and at 0.5, 2, and 6 hours postexercise. Muscle biopsies were obtained pre-exercise and at 2 and 6 hours postexercise.”

The conclusion of this study was, “Three grams of l-leucine and ursolic acid had no effect on Akt/mTORC1 signaling or serum insulin or IGF-1; however, l-leucine increased skeletal muscle IGF-1 concentration in resistance-trained men.”

Leucine, not branched-chain amino acids, is the most important chemical that turns on the mTOR pathway, so it is likely that consuming leucine after exercise would be more effective (and cheaper) than consuming BCAAs. The addition of isoleucine and valine may hinder the benefits of leucine due to competition for transport into muscle cells. The BCAAs share the same active transport system into cells and muscle cells. Indeed, isoleucine and valine have been shown to inhibit absorption of leucine.

Robert R. Wolfe, noted amino acid researcher, said in the Journal of the International Society of Sports Nutrition (2017) that “BCAAs also compete with other amino acids for transport, including phenylalanine, and this competition could affect the intramuscular availability of other EAAs. As a result of competition for transporters, it is possible that leucine alone, for example, could have a transitory stimulatory effect on muscle protein synthesis where the BCAAs fail to elicit such response.”

Studies indicate increases in muscle protein synthesis are dependent on leucine concentration! Leucine stimulates the anabolic effects of muscle protein by itself. A Japanese study published on October 18, 2018 in the journal Nutrients found that taking leucine supplements alone may be better for muscle protein synthesis and more anabolic than leucine from food! Japanese researchers found that blood levels of leucine were higher from pure, free leucine taken alone compared to the same amount of leucine in a meal. Increase in muscle protein synthesis is dependent on leucine concentration. Research has shown that leucine stimulates the anabolic effect of muscle protein on its own (Wilkinson et al., J Physiol, 2013). The Nutrients study showed that, “based on these findings, it is presumed that compared to the intake of protein alone or free amino acids alone, the intake of dietary protein from mixed meals may result in a lower maximum plasma leucine concentration. However, no study to date has investigated the changes in amino acid concentrations after the ingestion of mixed meals in comparison to those after the intake of a similar amount of free amino acids.”

In a randomized crossover study, 10 healthy, young Japanese men underwent tests under different conditions: consuming 2 grams of leucine alone; a mixed meal with 2.15 grams of leucine without any additional leucine supplementation; 2 grams of leucine right after a meal; and the final serving consisted of 2 grams of leucine, 180 minutes after a meal.

The study concluded that “based on the aforementioned discussions, the intake of free leucine alone markedly increased the plasma leucine concentration. However, the increase in leucine concentration after the intake of a mixed meal containing the same amount of leucine was significantly less than that of free leucine intake alone. Moreover, when free leucine was ingested after a mixed meal with the purpose of increasing the plasma leucine concentration, the maximum plasma concentration was attenuated when it was ingested immediately after the mixed meal, despite the fact that the total leucine content was doubled. These results suggest that when free amino acids ingested with the purpose of increasing plasma amino acid concentrations, the timing in relation to the mixed meal intake needs to be considered.”

For best results to use as an anabolic trigger, take 5 grams of leucine (on an empty stomach) 30 minutes before a post-workout meal, or protein shake. A meta-analysis (Nutrition, 2017) that combined the results of seven studies showed that BCAA supplements are best taken after exercise, not before or during exercise (intra-workout.) (Nutrition 2017, 42: 30-36; American Journal of Clinical Nutrition 2016; 104:1594-606; Med Sci Sports Exercise 2011, 43: 2249-2258; Nat Med 2015, 22: 421-426; Biochemical Journal 1996, 100: 7-11; International Journal of Sport Nutrition and Exercise Metabolism, March 2018, 28: 170-177; Amino Acids, June 2008, 35: 147-155; Amino Acids, July 2015, 47: 1389-98).

By taking pure leucine on an empty stomach, you will get a better spike in blood levels than if you take leucine with food, because food can slow leucine’s absorption. The addition of isoleucine and valine may hinder the benefits of leucine due to competition for transport into muscle cells. When leucine is taken on an empty stomach, it’s a powerful metabolic switch that turns on protein synthesis. Leucine increases mTOR activity for several hours after training. When leucine is taken after resistance exercise and before a post-workout, protein-containing meal rich in essential amino acids, it triggers greater protein synthesis for improved recovery and greater gains.  

THE BEST LEUCINE SUPPLEMENT

AML Post Workout contains 5 grams of pure leucine. It also contains 5 grams of creatine monohydrate and 2.5 grams of betaine. Creatine has been reported in the scientific literature to function as a myostatin inhibitor supporting muscle growth. Betaine has also been found in the scientific research to stimulate growth hormone (GH) and insulin-like-growth-factor-1 (IGF-1). Combining 5 grams of pure leucine along with 5 grams of creatine monohydrate and 2.5 grams of betaine makes AML Post Workout a potent, muscle growth and recovery supplement. For best results we suggest taking one serving of AML Post Workout by itself (on an empty stomach) 15-30 minutes before a post-workout meal, providing all the essential amino acids required for muscle protein synthesis.

References:

  1. Church DD, Schwarz NA, Spillane MB, et al. l-Leucine Increases Skeletal Muscle IGF-1 but Does Not Differentially Increase Akt/mTORC1 Signaling and Serum IGF-1 Compared to Ursolic Acid in Response to Resistance Exercise in Resistance-Trained Men. J Am Coll Nutr 2016;35(7):627-638. doi:10.1080/07315724.2015.1132019 
  1. Yoshii at al. Nutrients 2018, 10(10), 1543; https://doi.org/10.3390/nu10101543Effect of Mixed Meal and Leucine Intake on Plasma Amino Acid Concentrations in Young Men/
  1. Rahimi MH, Shab-Bidar S et al. Branched-chain amino acid supplementation and exercise-induced muscle damage in exercise recovery: A meta-analysis of randomized clinical trials. Nutrition 2017. 
  1. Chad M Kerksick, Colin D Wilborn, Michael D. ISSN exercise & sports nutrition review update: research & recommendations. 
  1. Roberts, et al. Journal of the International Society of Sports Nutrition 2018;15:38 https://doi.org/10.1186/s12970-018-0242-y 1 June 2018
  1. Robert R. Wolfe. Branched-chain amino acids and muscle protein synthesis in humans: myth or reality? Journal of the International Society of Sports Nutrition 2017;14:30 https://doi.org/10.1186/s12970-017-0184-9 
  1. Szmelcman S, Guggenheim K. Interference between leucine, isoleucine and valine during intestinal absorption. Biochemical Journal 1966;100(1):7-11. 
  1. Wilkinson, DJ et al. Effects of leucine and its metabolite beta-hydroxy-beta-methylbutyrateonhumanskeletalmuscleproteinmetabolism. J Physiol 2013;591,2911-2923.
  1. Cummings NE, Williams EM, Kasza I, Konon EN et al. (2018), Restoration of metabolic health by decreased consumption of branched‐chain amino acids. J Physiol, 596: 623-645. doi:10.1113/JP275075
  1. Duke University. Diabetes researchers find switch for fatty liver disease: Carbs, fats and protein: One molecule to rule them all? ScienceDaily, 17 May 2018. www.sciencedaily.com/releases/2018/05/180517113847.htm
  1. PJ White, RW McGarrah, PA Grimsrud, S Tso, W Yang, JM Haldeman, C Newgard et al. The BCKDH Kinase and Phosphatase Integrate BCAA and Lipid Metabolism via Regulation of ATP-Citrate Lyase. Cell Metabolism, 2018; DOI: 10.1016/j.cmet.2018.04.015
  1. NutraIngredients-USA.com, December 17, 2017. Nathan Gray. Could dropping specific amino acids from diet be key to weight loss? 
  1. CB Newgard, J An, JR Bain et al. A Branched-Chain Amino Acid-Related Metabolic Signature that Differentiates Obese and Lean Humans and Contributes to Insulin Resistance Cell Metab 2009 April; 9(4): 311-326. doi:10.1016/j.cmet.2009.02.002 
  1. Zheng Y, Li Y, Qi Q et al. Cumulative consumption of branched-chain amino acids and incidence of type 2 diabetes. Int J Epidemiol. 2016; 45: 1482-92.
  1. Isanejad M, LaCroix AZ, Thomson CA et al. Branched-chain amino acid, meat intake and risk of type 2 diabetes in the Women’s Health Initiative. Br J Nutr 2017; 117:1523-30. 
  1. Newgard CB, An J, Bain JR et al. A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistance. Cell Metab 2009; 9: 311-26 
  1. Tremblay F, Krebs M, Dombrowski L et al. Overactivation of S6 kinase 1 as a cause of human insulin resistance during increased amino acid availability. Diabetes 2005; 54: 2674-84. 
  1. Tremblay F, Krebs M, Dombrowski L et al. Overactivation of S6 kinase 1 as a cause of human insulin resistance during increased amino acid availability. Diabetes 2005; 54: 2674-84.
  1. Lee CC, Watkins SM, Lorenzo C et al. Branched-chain amino acids and insulin metabolism: The Insulin Resistance Atherosclerosis Study (IRAS). Diabetes Care 2016; 39: 582-8. 
  1. Yoon M-S. The emerging role of branched-chain amino acids in insulin resistance and metabolism. Forum Nutr 2016; 8: 405-17.
  1. Abdul-Ghani MA, Tripathy D and DeFronzo RA. Contributions of beta-cell dysfunction and insulin resistance to the pathogenesis of impaired glucose tolerance and impaired fasting glucose. Diabetes Care 2006; 29:1130-9. 
  1. Jang C, Oh, SF, et al A branched-chain amino acid metabolite drives vascular fatty acid transport and causes insulin resistance. Nat Med 22, 421-426 
  1. Sara B Seidelmann, Brian Claggett, Susan Cheng, Mir Henglin, Amil Shah, Lyn M Steffen, Aaron R Folsom, Eric B Rimm, Walter C Willett, Scott D Solomon, Dietary carbohydrate intake and mortality: a prospective cohort study and meta-analysis, The Lancet Public Health, 2018, ISSN 2468-2667, https://doi.org/10.1016/S2468-2667(18)30135-X. 
  1. Zhaoping Li, Professor of Medicine, UCLA, US National Library of Medicine www. ClinicalTrials.gov Identifier: NCT02684565 Last Update Posted: February 12, 2018 https://clinicaltrials.gov/ct2/show/NCT02684565 
  1. Lotta LA, Scott RA, Sharp SJ, Burgess S, Luan J, et al. (2016) Genetic Predisposition to an Impaired Metabolism of the Branched-Chain Amino Acids and Risk of Type 2 Diabetes: A Mendelian Randomisation Analysis. PLOS Medicine 13(11): e1002179. https://doi.org/10.1371/journal.pmed.1002179 
  1. Avogaro A and Bier DM (1989) Contribution of 3-hydroxyisobutyrate to the measurement of 3-hydroxybutyrate in human plasma: comparison of enzymatic and gas-liquid chromatography-mass spectrometry assays in normal and in diabetic subjects. J Lipid Res 30, 1811-1817 
  1. Giesbertz P, Padberg I et al. (2015) Metabolite profiling in plasma and tissues of ob/ob and db/db mice identifies novel markers of obesity and type 2 diabetes. Diabetologia 58, 2133-2143. 
  1. Insulin Resistance, And What May Contribute to It, by Lila Abassi on March 14, 2016. American Council on Science & Health https://www.acsh.org/news/2016/03/14/branched-chain-amino-metabolite-a-culprit-in-insulin-resistance 
  1. Lydia-Ann LS Harris, Gordon I Smith, Bruce W Patterson, Raja S Ramaswamy et al. Alterations in 3-Hydroxyisobutyrate and FGF21 Metabolism Are Associated With Protein Ingestion-Induced Insulin Resistance Diabetes 2017;66:1871-1878 https://doi.org/10.2337/db16-1475 
  1. Mardinoglu, Adil et al. Elevated Plasma Levels of 3-Hydroxyisobutyric Acid Are Associated With Incident Type 2 Diabetes EBioMedicine, Volume 27, 151-155, Jan. 2018. 
  1. Ulrika Andersson-Hall, Carolina Gustavsson, Anders Pedersen, Daniel Malmodin, Louise Joelsson, and Agneta Holmäng, Higher Concentrations of BCAAs and 3-HIB Are Associated with Insulin Resistance in the Transition from Gestational Diabetes to Type 2 Diabetes, Journal of Diabetes Research, vol. 2018, Article ID 4207067, 12 pages, 2018. https://doi.org/10.1155/2018/4207067. 
  1. Macotela Y, Emanuelli B, Bang AM et al. (2011) Dietary leucine – an environmental modifier of insulin resistance acting on multiple levels of metabolism. PLoS One 6, e21187. 
  1. Cunxi Nie, Ting He, Wenju Zhang, Guolong Zhang, Xi Ma. Branched Chain Amino Acids: Beyond Nutrition Metabolism. Int J Mol Sci. 2018 Apr; 19(4): 954. Published online 2018 Mar 23. doi: 10.3390/ijms19040954
  1. Y Zhang, K Guo, RE LeBlanc, D Loh, GJ Schwartz and Y Yu. Increasing Dietary Leucine Intake Reduces Diet-Induced Obesity and Improves Glucose and Cholesterol Metabolism in Mice via Multimechanisms. Diabetes Jun 2007, 56 (6) 1647-1654; DOI: 10.2337/db07-0123 
  1. Deirdre K Tobias, Clary Clish, Samia Mora, Jun Li, Liming Liang, Frank B. Hu, JoAnn E. Manson, Cuilin Zhang. Dietary Intakes and Circulating Concentrations of Branched-Chain Amino Acids in Relation to Incident Type 2 Diabetes Risk Among High-Risk Women with a History of Gestational Diabetes Mellitus Clinical Chemistry Aug 2018, 64 (8) 1203-1210; DOI: 10.1373/clinchem.2017.285841 
  1. McCormack S.E, Shaham O, McCarthy MA, Deik AA, Wang TJ, Gerszten RE, Clish CB, Mootha VK, Grinspoon SK and Fleischman A. (2013), Branched‐chain amino acids and IR in children. Pediatric Obesity, 8: 52-61. doi:10.1111/j.2047-6310.2012.00087.x. 
  1. Sina S Ullrich, Penelope CE Fitzgerald, Gudrun Schober, Robert E Steinert, Michael Horowitz, Christine Feinle-Bisset; Intragastric administration of leucine or isoleucine lowers the blood glucose response to a mixed-nutrient drink by different mechanisms in healthy, lean volunteers, The American Journal of Clinical Nutrition, Volume 104, Issue 5, 1 November 2016, Pages 1274-1284, https://doi.org/10.3945/ajcn.116.140640. 
  1. Haufe S. et al. Branched-chain and aromatic amino acids, insulin resistance and liver specific ectopic fat storage in overweight to obese subjects. Nutrition, Metabolism and Cardiovascular Diseases, Volume 26, Issue 7, 637-642 
  1. Li H, Xu M, Lee J, He C and Xie Z. (2012). Leucine supplementation increases SIRT1 expression and prevents mitochondrial dysfunction and metabolic disorders in high-fat diet-induced obese mice. American Journal of Physiology - Endocrinology and Metabolism, 303(10), E1234-E1244. http://doi.org/10.1152/ajpendo.00198.2012 
  1. Chunzi Liang, Benjamin J Curry, Patricia L Brown and Michael B. Zemel, Leucine Modulates Mitochondrial Biogenesis and SIRT1-AMPK Signaling in C2C12 Myotubes, Journal of Nutrition and Metabolism, vol. 2014, Article ID 239750, 11 pages, 2014. https://doi.org/10.1155/2014/239750. 
  1. Binder E, Bermúdez-Silva FJ, André C, Elie M, Romero-Zerbo SY, et al. Leucine Supplementation Protects from Insulin Resistance by Regulating Adiposity Levels (2013). Leucine Supplementation Protects from Insulin Resistance by Regulating Adiposity Levels. PLOS ONE 8(9): e74705. https://doi.org/10.1371/journal.pone.0074705
  1. Banerjee, Jheelam et al. Activation of the AMPK/Sirt1 pathway by a leucine-metformin combination increases insulin sensitivity in skeletal muscle, and stimulates glucose and lipid metabolism and increases life span in Caenorhabditis elegans. Metabolism - Clinical and Experimental, Volume 65, Issue 11, 1679-1691 
  1. Jiao J, Han S-F, Zhang W, Xu J-Y, Tong X, Yin X-B, Qin L-Q (2016). Chronic leucine supplementation improves lipid metabolism in C57BL/6J mice fed with a high-fat/cholesterol diet. Food & Nutrition Research, 60, 10.3402/fnr.v60.31304. http://doi.org/10.3402/fnr.v60.31304 
  1. Cholsoon Jang, Sungwhan F Oh, Shogo Wada, Glenn C Rowe, Laura Liu, Mun Chun Chan, James Rhee, Atsushi Hoshino, Boa Kim, Ayon Ibrahim, Luisa G Baca, Esl Kim, Chandra C Ghosh, Samir M Parikh, Aihua Jiang, Qingwei Chu, Daniel E Forman, Stewart H Lecker, Saikumari Krishnaiah, Joshua D Rabinowitz, Aalim M Weljie, Joseph A Baur, Dennis L Kasper & Zoltan Arany. Published: 07 March 2016. A branched-chain amino acid metabolite drives vascular fatty acid transport and causes insulin resistance. Nature Medicine volume 22, pages 421-426 (2016) 
  1. D’Antona G, Ragni M, Cardile A, Tedesco L, Dossena M, Bruttini F et al. (2010). Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab. 12, 362-372. doi: 10.1016/j.cmet.2010.08.016 
  1. Szmelcman S, Guggenheim K. Interference between leucine, isoleucine and valine during intestinal absorption. Biochemical Journal. 1966;100(1):7-11. 
  1. Robert R. Wolfe. Branched-chain amino acids and muscle protein synthesis in humans: myth or reality? Journal of the International Society of Sports Nutrition201714:30 https://doi.org/10.1186/s12970-017-0184-9
  1. L Deldicque, C Sanchez Canedo and S Horman. Antagonistic effects of leucine and glutamine on the mTOR pathway in myogenic C2C12 cells. Amino Acids, 2008, Volume 35, Number 1, Page 147
  1. Amy Hector, Stuart M. Phillips. Protein Recommendations for Weight Loss in Elite Athletes: A Focus on Body Composition and Performance. Int J Sport Nutr Exerc Metab 2017 
  1. Rahimi MH, Shab-Bidar S, Mollahosseini M, Djafarian K. Nutrition 2017. Leucine, Not Total Protein, Content of a Supplement Is the Primary Determinant of Muscle Protein Anabolic Responses in Healthy Older Women, The Journal of Nutrition, nxy091, June 13, 2018
  1. Branched-chain amino acid supplementation and exercise-induced muscle damage in exercise recovery: A meta-analysis of randomized clinical trials.
  1. Jiao J, Han S.F, Zhang W, Xu JY, Tong X, Yin XB, Yuan LX, Qin LQ (2016). Chronic leucine supplementation improves lipid metabolism in C57BL/6J mice fed with a high-fat/cholesterol diet. Food & nutrition research, 60, 31304. doi:10.3402/fnr.v60.31304 
  1. Macotela Y, Emanuelli B, Ba˚ng AM, Espinoza DO, Boucher J, Beebe K, et al. Dietary leucine an environmental modifier of insulin resistance acting on multiple levels of metabolism. PLoS One 2011; 6: e21187. 
  1. Zhang Y, Guo K, LeBlanc RE, Loh D, Schwartz GJ, Yu YH. Increasing dietary leucine intake reduces diet-induced obesity and improves glucose and cholesterol metabolism in mice via multimechanisms. Diabetes 2007; 56: 164754. 
  1. Khan M, Joseph F. Adipose tissue and adipokines: the association with and application of adipokines in obesity. Scientifica (Cairo) 2014; 2014: 328592 
  1. Zemel MB, Bruckbauer A. Effects of a leucine and pyridoxine containing nutraceutical on fat oxidation, and oxidative and inflammatory stress in overweight and obese subjects. Nutrients 2012; 4: 52941 
  1. Ricoult SJ, Manning BD. The multifaceted role of mTORC1 in the control of lipid metabolism. EMBO Rep 2013; 14: 24251 
  1. Freudenberg A, Petzke KJ, Klaus S. Comparison of high protein diets and leucine supplementation in the prevention of metabolic syndrome and related disorders in mice. J Nutr Biochem 2012; 3: 152430. 
  1. Vaughan RA, Garcia-Smith R, Gannon NP, Bisoffi M, Trujillo KA, Conn CA. Leucine treatment enhances oxidative capacity through complete carbohydrate oxidation and increased mitochondrial density in skeletal muscle cells. Amino Acids 2013; 45: 90111. 
  1. Zhang Y et al. (2007) Increasing dietary leucine intake reduces diet-induced obesity and improves glucose and cholesterol metabolism in mice via multimechanisms. Diabetes 56(6):1647-1654
  1. Okekunle AP, Zhang M, Wang Z. et al. Dietary branched-chain amino acids intake exhibited a different relationship with type 2 diabetes and obesity risk: a meta-analysis. Acta Diabetol (2018). https://doi.org/10.1007/s00592-018-1243-7
  1. Binder E, Bermúdez-Silva FJ, André C, Elie M, Romero-Zerbo SY, et al. Leucine Supplementation Protects from Insulin Resistance by Regulating Adiposity Levels (2013) Leucine Supplementation Protects from Insulin Resistance by Regulating Adiposity Levels. PLOS ONE 8(9): e74705. https://doi.org/10.1371/journal.pone.0074705
  1. Binder E, Bermúdez‐Silva FJ, Elie M, Leste‐Lasserre T, Belluomo I, Clark S, Duchampt A, Mithieux G and Cota D. (2014) Leucine supplementation modulates fuel substrates utilization and glucose metabolism in previously obese mice. Obesity, 22: 713-720. doi:10.1002/oby.20578 
  1. Li H, Xu M, Lee J, He C and Xie Z (2012). Leucine supplementation increases SIRT1 expression and prevents mitochondrial dysfunction and metabolic disorders in high-fat diet-induced obese mice. American journal of physiology. Endocrinology and metabolism, 303(10), E1234-44.
  1. Pedroso JA, Zampieri TT and and Donato J. (2015). Reviewing the Effects of L-Leucine Supplementation in the Regulation of Food Intake, Energy Balance, and Glucose Homeostasis. Nutrients, 7 (5), 3914-37. https://dx.doi.org/10.3390%2Fnu705391
  1. Caoileann H Murphy, Nelson I Saddler, Michaela C Devries, Chris McGlory, Steven K Baker and Stuart M Phillips. Leucine supplementation enhances integrative myofibrillar protein synthesis in free-living older men consuming lower- and higher-protein diets: a parallel-group crossover study, The American Journal of Clinical Nutrition, Volume 104, Issue 6, 1 December 2016, Pages 1594-1606, https://doi.org/10.3945/ajcn.116.136424 
  1. Yadao DR, MacKenzie S and Bergdahl A. (2018) Reducing branched‐chain amino acid intake to reverse metabolic complications in obesity and type 2 diabetes. J Physiol, 596: 3455-3456. doi:10.1113/JP276274