Side effects of amino acid supplements

. 2022 Mar 25 ; 71 (1) : 29-45. [epub] 20220119

Jazyk angličtina Země Česko Médium print-electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid35043647

The aim of the article is to examine side effects of increased dietary intake of amino acids, which are commonly used as a dietary supplement. In addition to toxicity, mutagenicity and carcinogenicity, attention is focused on renal and gastrointestinal tract functions, ammonia production, and consequences of a competition with other amino acids for a carrier at the cell membranes and enzymes responsible for their degradation. In alphabetic order are examined arginine, beta-alanine, branched-chain amino acids, carnosine, citrulline, creatine, glutamine, histidine, beta -hydroxy- beta -methylbutyrate, leucine, and tryptophan. In the article is shown that enhanced intake of most amino acid supplements may not be risk-free and can cause a number of detrimental side effects. Further research is necessary to elucidate effects of high doses and long-term consumption of amino acid supplements on immune system, brain function, muscle protein balance, synthesis of toxic metabolites, and tumor growth and examine their suitability under certain circumstances. These include elderly, childhood, pregnancy, nursing a baby, and medical condition, such as diabetes and liver disease. Studies are also needed to examine adaptive response to a long-term intake of any substance and consequences of discontinuation of supplementation.

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Fabresse N, Gheddar L, Kintz P, Knapp A, Larabi IA, Alvarez JC. Analysis of pharmaceutical products and dietary supplements seized from the black market among bodybuilders. Forensic Sci Int. 2021;322:110771. doi: 10.1016/j.forsciint.2021.110771. PubMed DOI

Baxter JH, Carlos JL, Thurmond J, Rehani RN, Bultman J, Frost D. Dietary toxicity of calcium beta-hydroxy-beta-methyl butyrate (CaHMB) Food Chem Toxicol. 2005;43:1731–1741. doi: 10.1016/j.fct.2005.05.016. PubMed DOI

Kim HJ, Kim CK, Carpentier A, Poortmans JR. Studies on the safety of creatine supplementation. Amino Acids. 2011;40:1409–1418. doi: 10.1007/s00726-011-0878-2. PubMed DOI

Bode BP, Kaminski DL, Souba WW, Li AP. Glutamine transport in isolated human hepatocytes and transformed liver cells. Hepatology. 1995;21:511–520. PubMed

Park KG. The Sir David Cuthbertson Medal Lecture 1992. The immunological and metabolic effects of L-arginine in human cancer. Proc Nutr Soc. 1993;52:387–401. doi: 10.1079/pns19930080. PubMed DOI

Barbul A. Arginine: biochemistry, physiology, and therapeutic implications. JPEN J Parenter Enteral Nutr. 1986;10:227–238. doi: 10.1177/0148607186010002227. PubMed DOI

Geliebter AA, Hashim SA, Van Itallie TB. Oral L-histidine fails to reduce taste and smell acuity but induces anorexia and urinary zinc excretion. Am J Clin Nutr. 1981;34:119–120. doi: 10.1093/ajcn/34.1.119. PubMed DOI

Tietze IN, S⊘rensen SS, Eiskjaer H, Thomsen K, Pedersen EB. Tubular handling of amino acids after intravenous infusion of amino acids in healthy humans. Nephrol Dial Transplant. 1992;7:493–500. PubMed

Gougoux A, Vinay P, Halperin ML. Regulation of renal ammoniagenesis in the dog with chronic metabolic acidosis: effect of a glutamine load. Am J Physiol. 1985;249:F745–F752. doi: 10.1152/ajprenal.1985.249.5.F745. PubMed DOI

Canessa-Fischer M, Shalhoub R, Glabman S, de Haas J, Pitts RF. Effects of infusions of ammonia, amides, and amino acids on excretion of ammonia. Am J Physiol. 1963;204:192–196. doi: 10.1152/ajplegacy.1963.204.2.192. PubMed DOI

Yuneva M, Zamboni N, Oefner P, Sachidanandam R, Lazebnik Y. Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells. J Cell Biol. 2007;178:93–105. doi: 10.1083/jcb.200703099. PubMed DOI PMC

Albaugh VL, Pinzon-Guzman C, Barbul A. Arginine-dual roles as an onconutrient and immunonutrient. J Surg Oncol. 2017;115:273–280. doi: 10.1002/jso.24490. PubMed DOI PMC

Evans RW, Fernstrom JD, Thompson J, Morris SM, Jr, Kuller LH. Biochemical responses of healthy subjects during dietary supplementation with L-arginine. J Nutr Biochem. 2004;15:534–539. doi: 10.1016/j.jnutbio.2004.03.005. PubMed DOI

Holecek M, Sispera L. Effects of arginine supplementation on amino acid profiles in blood and tissues in fed and overnight-fasted rats. Nutrients. 2016;8:206. doi: 10.3390/nu8040206. PubMed DOI PMC

Schulze F, Glos S, Petruschka D, Altenburg C, Maas R, Benndorf R, Schwedhelm E, Beil U, Böger RH. L-Arginine enhances the triglyceride-lowering effect of simvastatin in patients with elevated plasma triglycerides. Nutr Res. 2009;29:291–297. doi: 10.1016/j.nutres.2009.04.004. PubMed DOI

Flynn NE, Knabe DA, Mallick BK, Wu G. Postnatal changes of plasma amino acids in suckling pigs. J Anim Sci. 2000;7:2369–2375. doi: 10.2527/2000.7892369x. PubMed DOI

Luiking YC, Poeze M, Deutz NE. Arginine infusion in patients with septic shock increases nitric oxide production without haemodynamic instability. Clin Sci (Lond) 2015;128:57–67. doi: 10.1042/CS20140343. PubMed DOI

Oka RK, Szuba A, Giacomini JC, Cooke JP. A pilot study of L-arginine supplementation on functional capacity in peripheral arterial disease. Vasc Med. 2005;10:265–274. doi: 10.1191/1358863x05vm637oa. PubMed DOI

Bednarz B, Jaxa-Chamiec T, Maciejewski P, Szpajer M, Janik K, Gniot J, Kawka-Urbanek T, Drozdowska D, Gessek J, Laskowski H. Efficacy and safety of oral l-arginine in acute myocardial infarction. Results of the multicenter, randomized, double-blind, placebo-controlled ARAMI pilot trial. Kardiol Pol. 2005;62:421–427. PubMed

Balasubramanian A, Thirumavalavan N, Srivatsav A, Yu J, Hotaling JM, Lipshultz LI, Pastuszak AW. An analysis of popular online erectile dysfunction supplements. J Sex Med. 2019;16:843–852. doi: 10.1016/j.jsxm.2019.03.269. PubMed DOI PMC

Liu P, Shen WQ, Chen HL. Efficacy of arginine-enriched enteral formulas for the healing of pressure ulcers: A systematic review. J Wound Care. 2017;26:319–323. doi: 10.12968/jowc.2017.26.6.319. PubMed DOI

Tan B, Li X, Yin Y, Wu Z, Liu C, Tekwe CD, Wu G. Regulatory roles for L-arginine in reducing white adipose tissue. Front Biosci (Landmark Ed) 2012;17:2237–2246. doi: 10.2741/4047. PubMed DOI PMC

Mehta S, Stewart DJ, Levy RD. The hypotensive effect of L-arginine is associated with increased expired nitric oxide in humans. Chest. 1996;109:1550–555. doi: 10.1378/chest.109.6.1550. PubMed DOI

Wilson AM, Harada R, Nair N, Balasubramanian N, Cooke JP. L-arginine supplementation in peripheral arterial disease: no benefit and possible harm. Circulation. 2007;116:188–195. doi: 10.1161/CIRCULATIONAHA.106.683656. PubMed DOI

Schulman SP, Becker LC, Kass DA, Champion HC, Terrin ML, Forman S, Ernst KV, Kelemen MD, Townsend SN, Capriotti A, Hare JM, Gerstenblith G. L-arginine therapy in acute myocardial infarction: the Vascular Interaction With Age in Myocardial Infarction (VINTAGE MI) randomized clinical trial. JAMA. 2006;295:58–64. doi: 10.1001/jama.295.1.58. PubMed DOI

Mohan S, Wu CC, Shin S, Fung HL. Continuous exposure to L-arginine induces oxidative stress and physiological tolerance in cultured human endothelial cells. Amino Acids. 2012;43:1179–1188. doi: 10.1007/s00726-011-1173-y. PubMed DOI PMC

Huang J, Ladeiras D, Yu Y, Ming XF, Yang Z. Detrimental effects of chronic L-arginine rich food on aging kidney. Front Pharmacol. 2021;11:582155. doi: 10.3389/fphar.2020.582155. PubMed DOI PMC

del Favero S, Roschel H, Solis MY, Hayashi AP, Artioli GG, Otaduy MC, Benatti FB, Harris RC, Wise JA, Leite CC, Pereira RM, de Sá-Pinto AL, Lancha-Junior AH, Gualano Beta-alanine (Carnosyn™) supplementation in elderly subjects (60–80 years): effects on muscle carnosine content and physical capacity. Amino Acids. 2012;43:49–56. doi: 10.1007/s00726-011-1190-x. PubMed DOI PMC

Blancquaert L, Everaert I, Missinne M, Baguet A, Stegen S, Volkaert A, Petrovic M, Vervaet C, Achten E, De Maeyer M, De Henauw S, Derave W. Effects of histidine and β-alanine supplementation on human muscle carnosine storage. Med Sci Sports Exerc. 2017;49:602–609. doi: 10.1249/MSS.0000000000001213. PubMed DOI

Holeček M. Histidine in health and disease: Metabolism, physiological importance, and use as a supplement. Nutrients. 2020;12:848. doi: 10.3390/nu12030848. PubMed DOI PMC

Saunders B, Franchi M, De Oliveira LF, Da Eira Silva V, Da Silva RP, De Salles Painelli V, Costa LAR, Sale C, Harris RC, Roschel H, Artioli GG, Gualano B. 24-Week β-alanine ingestion does not affect muscle taurine or clinical blood parameters in healthy males. Eur J Nutr. 2020;59:57–65. doi: 10.1007/s00394-018-1881-0. PubMed DOI

Dolan E, Swinton PA, Painelli VS, Stephens Hemingway B, Mazzolani B, Infante Smaira F, Saunders B, Artioli GG, Gualano B. A systematic risk assessment meta-analysis on the use of oral β-alanine supplementation. Adv Nutr. 2019;10:452–463. doi: 10.1093/advances/nmy115. PubMed DOI PMC

Floyd JC, Jr, Fajans SS, Conn JW, Knopf RF, Rull J. Stimulation of insulin secretion by amino acids. J Clin Invest. 1966;45:1487–1502. doi: 10.1172/JCI105456. PubMed DOI PMC

Nair KS, Short KR. Hormonal and signaling role of branched-chain amino acids. J Nutr. 2005;135(6 Suppl):1547S–1552S. doi: 10.1093/jn/135.6.1547S. PubMed DOI

Holeček M. The role of skeletal muscle in the pathogenesis of altered concentrations of branched-chain amino acids (valine, leucine, and isoleucine) in liver cirrhosis, diabetes, and other diseases. Physiol Res. 2021;70:293–305. doi: 10.33549/physiolres.934648. PubMed DOI PMC

Holeček M. Why are branched-chain amino acids increased in starvation and diabetes? Nutrients. 2020;12:3087. doi: 10.3390/nu12103087. PubMed DOI PMC

Holeček M. Branched-chain amino acids in health and disease: metabolism, alterations in blood plasma, and as supplements. Nutr Metab (Lond) 2018;15:33. doi: 10.1186/s12986-018-0271-1. PubMed DOI PMC

Strüder HK, Hollmann W, Platen P, Donike M, Gotzmann A, Weber K. Influence of paroxetine, branched-chain amino acids and tyrosine on neuroendocrine system responses and fatigue in humans. Horm Metab Res. 1998;30:188–194. doi: 10.1055/s-2007-978864. PubMed DOI

Gijsman HJ, Scarnà A, Harmer CJ, McTavish SB, Odontiadis J, Cowen PJ, Goodwin GM. A dose-finding study on the effects of branch chain amino acids on surrogate markers of brain dopamine function. Psychopharmacology (Berl) 2002;160:192–197. doi: 10.1007/s00213-001-0970-5. PubMed DOI

Rose WC, Wixom RL, Lockhart HB, Lambert GF. The amino acid requirements of man. XV. The valine requirement; summary and final observations. J Biol Chem. 1955;217:987–995. PubMed

Heger J, Van Phung T, Krízová L, Sustala M, Simecek K. Efficiency of amino acid utilization in the growing pig at suboptimal levels of intake: branched-chain amino acids, histidine and phenylalanine + tyrosine. J Anim Physiol Anim Nutr (Berl) 2003;87:52–65. doi: 10.1046/j.1439-0396.2003.00406.x. PubMed DOI

Bikker P, Verstegen MW, Bosch MW. Amino acid composition of growing pigs is affected by protein and energy intake. J Nutr. 1994;124:1961–1969. doi: 10.1093/jn/124.10.1961. PubMed DOI

Holecek M, Siman P, Vodenicarovova M, Kandar R. Alterations in protein and amino acid metabolism in rats fed a branched-chain amino acid- or leucine-enriched diet during postprandial and postabsorptive states. Nutr Metab (Lond) 2016;13:12. doi: 10.1186/s12986-016-0072-3. PubMed DOI PMC

Harper AE, Miller RH, Block KP. Branched-chain amino acid metabolism. Annu Rev Nutr. 1984;4:409–454. doi: 10.1146/annurev.nu.04.070184.002205. PubMed DOI

Davuluri G, Allawy A, Thapaliya S, Rennison JH, Singh D, Kumar A, Sandlers Y, Van Wagoner DR, Flask CA, Hoppel C, Kasumov T, Dasarathy S. Hyperammonaemia-induced skeletal muscle mitochondrial dysfunction results in cataplerosis oxidative stress. J Physiol. 2016;594:7341–7360. doi: 10.1113/JP272796. PubMed DOI PMC

Wagenmakers AJ, Coakley JH, Edwards RH. Metabolism of branched-chain amino acids and ammonia during exercise: clues from McArdle’s disease. Int J Sports Med. 1990;11(Suppl 2):S101–S113. doi: 10.1055/s-2007-1024861. PubMed DOI

Holecek M. Evidence of a vicious cycle in glutamine synthesis and breakdown in pathogenesis of hepatic encephalopathy-therapeutic perspectives. Metab Brain Dis. 2014;29:9–17. doi: 10.1007/s11011-013-9428-9. PubMed DOI PMC

Holeček M. Branched-chain amino acid supplementation in treatment of liver cirrhosis: Updated views on how to attenuate their harmful effects on cataplerosis and ammonia formation. Nutrition. 2017;41:80–5. doi: 10.1016/j.nut.2017.04.003. PubMed DOI

MacLean DA, Graham TE. Branched-chain amino acid supplementation augments plasma ammonia responses during exercise in humans. J Appl Physiol (1985) 1993;74:2711–2717. doi: 10.1152/jappl.1993.74.6.2711. PubMed DOI

MacLean DA, Graham TE, Saltin B. Stimulation of muscle ammonia production during exercise following branched-chain amino acid supplementation in humans. J Physiol. 1996;493:909–922. doi: 10.1113/jphysiol.1996.sp021433. PubMed DOI PMC

Gibson EL. Tryptophan supplementation and serotonin function: genetic variations in behavioural effects. Proc Nutr Soc. 2018;77:174–188. doi: 10.1017/S0029665117004451. PubMed DOI

Bloomgarden Z. Diabetes and branched-chain amino acids: What is the link? J Diabetes. 2018;10:350–52. doi: 10.1111/1753-0407.12645. PubMed DOI

Yoon MS. The emerging role of branched-chain amino acids in insulin resistance and metabolism. Nutrients. 2016;8:405. doi: 10.3390/nu8070405. PubMed DOI PMC

Abe H. Role of histidine-related compounds as intracellular proton buffering constituents in vertebrate muscle. Biochemistry (Mosc) 2000;65:757–765. PubMed

Liu Y, Cotillard A, Vatier C, Bastard JP, Fellahi S, Stévant M, Allatif O, Langlois C, Bieuvelet S, Brochot A, Guilbot A, Clément K, Rizkalla SW. A dietary supplement containing cinnamon, chromium and carnosine decreases fasting plasma glucose and increases lean mass in overweight or obese pre-diabetic subjects: A randomized, placebo-controlled trial. PLoS One. 2015;10:e0138646. doi: 10.1371/journal.pone.0138646. PubMed DOI PMC

Park YJ, Volpe SL, Decker EA. Quantitation of carnosine in humans plasma after dietary consumption of beef. J Agric Food Chem. 2005;53:4736–4739. doi: 10.1021/jf047934h. PubMed DOI

Crenn P, Coudray-Lucas C, Cynober L, Messing B. Post-absorptive plasma citrulline concentration: a marker of intestinal failure in humans. Transplant Proc. 1998;30:2528. doi: 10.1016/s0041-1345(98)00711-8. PubMed DOI

Allerton TD, Proctor DN, Stephens JM, Dugas TR, Spielmann G, Irving BA. L-Citrulline supplementation: Impact on cardiometabolic health. Nutrients. 2018;10:921. doi: 10.3390/nu10070921. PubMed DOI PMC

Osowska S, Moinard C, Neveux N, Loï C, Cynober L. Citrulline increases arginine pools and restores nitrogen balance after massive intestinal resection. Gut. 2004;53:1781–1786. doi: 10.1136/gut.2004.042317. PubMed DOI PMC

Buford TW, Kreider RB, Stout JR, Greenwood M, Campbell B, Spano M, Ziegenfuss T, Lopez H, Landis J, Antonio J. International Society of Sports Nutrition position stand: creatine supplementation and exercise. J Int Soc Sports Nutr. 2007;4:6. doi: 10.1186/1550-2783-4-6. PubMed DOI PMC

Hall M, Trojian TH. Creatine supplementation. Curr Sports Med Rep. 2013;12:240–44. doi: 10.1249/JSR.0b013e31829cdff2. PubMed DOI

Juhn MS, O’Kane JW, Vinci DM. Oral creatine supplementation in male collegiate athletes: a survey of dosing habits and side effects. J Am Diet Assoc. 1999;99:593–595. doi: 10.1016/s0002-8223(99)00145-5. PubMed DOI

Kreider RB, Kalman DS, Antonio J, Ziegenfuss TN, Wildman R, Collins R, Candow DG, Kleiner SM, Almada AL, Lopez HL. International Society of Sports Nutrition position stand: safety and efficacy of creatine supplementation in exercise, sport, and medicine. J Int Soc Sports Nutr. 2017;14:18. doi: 10.1186/s12970-017-0173-z. PubMed DOI PMC

Antonio J, Candow DG, Forbes SC, Gualano B, Jagim AR, Kreider RB, Rawson ES, Smith-Ryan AE, VanDusseldorp TA, Willoughby DS, Ziegenfuss TN. Common questions and misconceptions about creatine supplementation: what does the scientific evidence really show? J Int Soc Sports Nutr. 2021;18:13. doi: 10.1186/s12970-021-00412-w. PubMed DOI PMC

Davani-Davari D, Karimzadeh I, Ezzatzadegan-Jahromi S, Sagheb MM. Potential adverse effects of creatine supplement on the kidney in athletes and bodybuilders. Iran J Kidney Dis. 2018;12:253–260. PubMed

Poortmans JR, Kumps A, Duez P, Fofonka A, Carpentier A, Francaux M. Effect of oral creatine supplementation on urinary methylamine, formaldehyde, and formate. Med Sci Sports Exerc. 2005;37:1717–1720. doi: 10.1249/01.mss.0000176398.64189.e6. PubMed DOI

Ziegler TR, Szeszycki EE, Estívariz CF, Puckett AB, Leader LM. Glutamine: from basic science to clinical applications. Nutrition. 1996;12(11–12 Suppl):S68–S70. doi: 10.1016/s0899-9007(96)00019-6. PubMed DOI

Décombaz J, Reinhardt P, Anantharaman K, von Glutz G, Poortmans JR. Biochemical changes in a 100 km run: free amino acids, urea, and creatinine. Eur J Appl Physiol Occup Physiol. 1979;41:61–72. doi: 10.1007/BF00424469. PubMed DOI

Brodan V, Kuhn E, Pechar J, Tomková D. Changes of free amino acids in plasma of healthy subjects induced by physical exercise. Eur J Appl Physiol Occup Physiol. 1976;35:69–77. doi: 10.1007/BF00444658. PubMed DOI

Roth E, Funovics J, Mühlbacher F, Schemper M, Mauritz W, Sporn P, Fritsch A. Metabolic disorders in severe abdominal sepsis: glutamine deficiency in skeletal muscle. Clin Nutr. 1982;1:25–41. doi: 10.1016/0261-5614(82)90004-8. PubMed DOI

Holecek M, Sispera L. Glutamine deficiency in extracellular fluid exerts adverse effects on protein and amino acid metabolism in skeletal muscle of healthy, laparotomized, and septic rats. Amino Acids. 2014;46:1377–1384. doi: 10.1007/s00726-014-1701-7. PubMed DOI

Stehle P, Zander J, Mertes N, Albers S, Puchstein C, Lawin P, Fürst P. Effect of parenteral glutamine peptide supplements on muscle glutamine loss and nitrogen balance after major surgery. Lancet. 1989;1:231–233. doi: 10.1016/s0140-6736(89)91254-3. PubMed DOI

Wernerman J, Hammarqvist F, Vinnars E. Alpha-ketoglutarate and postoperative muscle catabolism. Lancet. 1990;335:701–703. doi: 10.1016/0140-6736(90)90811-i. PubMed DOI

Newsholme E, Hardy G. Supplementation of diets with nutritional pharmaceuticals. Nutrition. 1997;13:837–839. doi: 10.1016/s0899-9007(97)00253-0. PubMed DOI

Hardy G, Hardy IJ. Can glutamine enable the critically ill to cope better with infection? JPEN J Parenter Enteral Nutr. 2008;32:489–491. doi: 10.1177/0148607108319796. PubMed DOI

Ziegler TR, Benfell K, Smith RJ, Young LS, Brown E, Ferrari-Baliviera E, Lowe DK, Wilmore DW. Safety and metabolic effects of L-glutamine administration in humans. JPEN J Parenter Enteral Nutr. 1990;14(4 Suppl):137S–146S. doi: 10.1177/0148607190014004201. PubMed DOI

Tsubuku S, Hatayama K, Mawatari K, Smriga M, Kimura T. Thirteen-week oral toxicity study of L-glutamine in rats. Int J Toxicol. 2004;23:107–112. doi: 10.1080/10915810490435677. PubMed DOI

Wong AW, Magnuson BA, Nakagawa K, Bursey RG. Oral subchronic and genotoxicity studies conducted with the amino acid, L-glutamine. Food Chem Toxicol. 2011;49:2096–2102. doi: 10.1016/j.fct.2011.05.023. PubMed DOI

Holeček M. Adverse effects of chronic intake of glutamine-supplemented diet on amino acid concentrations and protein metabolism in rat: effect of short-term starvation. Clin Nutr ESPEN. 2011;6:E190–E196. doi: 10.1016/j.eclnm.2011.05.002. DOI

Galera SC, Fechine FV, Teixeira MJ, Coelho ZC, de Vasconcelos RC, de Vasconcelos PR. The safety of oral use of L-glutamine in middle-aged and elderly individuals. Nutrition. 2010;26:375–381. doi: 10.1016/j.nut.2009.05.013. PubMed DOI

Holecek M. Side effects of long-term glutamine supplementation. JPEN J Parenter Enteral Nutr. 2013;37:607–616. doi: 10.1177/0148607112460682. PubMed DOI

Matsuno T, Satoh T. Glutamine metabolism in the avian host bearing transplantable hepatomatous growth induced by MC-29 virus. Int J Biochem. 1986;18:187–189. doi: 10.1016/0020-711x(86)90155-2. PubMed DOI

McGivan JD, Bungard CI. The transport of glutamine into mammalian cells. Front Biosci. 2007;12:874–882. doi: 10.2741/2109. PubMed DOI

Bungard CI, McGivan JD. Glutamine availability up-regulates expression of the amino acid transporter protein ASCT2 in HepG2 cells and stimulates the ASCT2 promoter. Biochem J. 2004;382:27–32. doi: 10.1042/BJ20040487. PubMed DOI PMC

Gao P, Tchernyshyov I, Chang TC, Lee Y-S, Kita K, Ochi T, Zeller KI, De Marzo AM, Van Eyk JE, Mendell JT, Dang CV. c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism. Nature. 2009;458:762–765. doi: 10.1038/nature07823. PubMed DOI PMC

Kaadige MR, Looper RE, Kamalanaadhan S, Ayer DE. Glutamine-dependent anapleurosis dictates glucose uptake and cell growth by regulating MondoA transcriptional activity. Proc Natl Acad Sci U S A. 2009;106:14878–14883. doi: 10.1073/pnas.0901221106. PubMed DOI PMC

Le Bricon T. Effect of glutamine supplementation on protein metabolism and glutathione in tumor-bearing rats. Clin Nutr. 1996;15:211. doi: 10.1016/s0261-5614(96)80244-5. PubMed DOI

Kaibara A, Yoshida S, Yamasaki K, Ishibashi N, Kakegawa T. Effect of glutamine and chemotherapy on protein metabolism in tumor-bearing rats. J Surg Res. 1994;57:143–149. doi: 10.1006/jsre.1994.1122. PubMed DOI

Fahr MJ, Kornbluth J, Blossom S, Schaeffer R, Klimberg VS, Harry M. Vars Research Award. Glutamine enhances immunoregulation of tumor growth. JPEN J Parenter Enteral Nutr. 1994;18:471–476. doi: 10.1177/0148607194018006471. PubMed DOI

Yoshida S, Kaibara A, Yamasaki K, Ishibashi N, Noake T, Kakegawa T. Effect of glutamine supplementation on protein metabolism and glutathione in tumor-bearing rats. JPEN J Parenter Enteral Nutr. 1995;19:492–497. doi: 10.1177/0148607195019006492. PubMed DOI

Klimberg VS, Souba WW, Salloum RM, Plumley DA, Cohen FS, Dolson DJ, Bland KI, Copeland EM. Glutamine-enriched diets support muscle glutamine metabolism without stimulating tumor growth. J Surg Res. 1990;48:319–323. doi: 10.1016/0022-4804(90)90066-b. PubMed DOI

Austgen TR, Dudrick PS, Sitren H, Bland KI, Copeland E, Souba WW. The effects of glutamine-enriched total parenteral nutrition on tumor growth and host tissues. Ann Surg. 1992;215:107–113. doi: 10.1097/00000658-199202000-00003. PubMed DOI PMC

Albrecht J, Zielińska M, Norenberg MD. Glutamine as a mediator of ammonia neurotoxicity: A critical appraisal. Biochem Pharmacol. 2010;80:1303–1308. doi: 10.1016/j.bcp.2010.07.024. PubMed DOI PMC

Oppong KN, Al-Mardini H, Thick M, Record CO. Oral glutamine challenge in cirrhotics pre- and post-liver transplantation: a psychometric and analyzed EEG study. Hepatology. 1997;26:870–76. doi: 10.1002/hep.510260411. PubMed DOI

Ortiz M, Jacas C, Córdoba J. Minimal hepatic encephalopathy: diagnosis, clinical significance and recommendations. J Hepatol. 2005;42(Suppl 1):S45–S53. doi: 10.1016/j.jhep.2004.11.028. PubMed DOI

Kopple JD, Swendseid ME. Evidence that histidine is an essential amino acid in normal and chronically uremic man. J Clin Invest. 1975;55:881–891. doi: 10.1172/JCI108016. PubMed DOI PMC

Edelman JJ, Seco M, Dunne B, Matzelle SJ, Murphy M, Joshi P, Yan TD, Wilson MK, Bannon PG, Vallely MP, Passage J. Custodiol for myocardial protection and preservation: a systematic review. Ann Cardiothorac Surg. 2013;2:717–728. doi: 10.3978/j.issn.2225-319X.2013.11.10. PubMed DOI PMC

Sheiner JB, Morris P, Anderson GH. Food intake suppression by histidine. Pharmacol Biochem Behav. 1985;23:721–726. doi: 10.1016/0091-3057(85)90061-9. PubMed DOI

Yoshimatsu H, Chiba S, Tajima D, Akehi Y, Sakata T. Histidine suppresses food intake through its conversion into neuronal histamine. Exp Biol Med (Maywood) 2002;227:63–68. doi: 10.1177/153537020222700111. PubMed DOI

Holeček M. Influence of histidine administration on ammonia and amino acid metabolism: A review. Physiol Res. 2020;69:555–564. doi: 10.33549/physiolres.934449. PubMed DOI PMC

Solomon JK, Geison RL. Effect of excess dietary L-histidine on plasma cholesterol levels in weanling rats. J Nutr. 1978;108:936–943. doi: 10.1093/jn/108.6.936. PubMed DOI

Harvey PW, Hunsaker HA, Allen KG. Dietary L-histidine-induced hypercholesterolemia and hypocupremia in the rat. J Nutr. 1981;111:639–647. doi: 10.1093/jn/111.4.639. PubMed DOI

Hitomi-Ohmura E, Amano N, Aoyama Y, Yoshida A. The effect of a histidine-excess diet on cholesterol synthesis and degradation in rats. Lipids. 1992;27:755–760. doi: 10.1007/BF02535845. PubMed DOI

Holeček M, Vodeničarovová V. Effects of histidine supplementation on amino acid metabolism in rats. Physiol Res. 2020;69:99–111. doi: 10.33549/physiolres.934296. PubMed DOI PMC

Holeček M. Beta-hydroxy-beta-methylbutyrate supplementation and skeletal muscle in healthy and muscle-wasting conditions. J Cachexia Sarcopenia Muscle. 2017;8:529–541. doi: 10.1002/jcsm.12208. PubMed DOI PMC

Hsieh LC, Chow CJ, Chang WC, Liu TH, Chang CK. Effect of beta-hydroxy-beta-methylbutyrate on protein metabolism in bed-ridden elderly receiving tube feeding. Asia Pac J Clin Nutr. 2010;19:200–208. PubMed

Vukovich MD, Stubbs NB, Bohlken RM. Body composition in 70-year-old adults responds to dietary beta-hydroxy-beta-methylbutyrate similarly to that of young adults. J Nutr. 2001;131:2049–2052. doi: 10.1093/jn/131.7.2049. PubMed DOI

Singh SS, Kumar A, Welch N, Sekar J, Mishra S, Bellar A, Gangadhariah M, Attaway A, Al Khafaji H, Wu X, Pathak V, Agrawal V, McMullen MR, Hornberger TA, Nagy LE, Davuluri G, Dasarathy S. Multiomics-identified intervention to restore ethanol-induced dysregulated proteostasis and secondary sarcopenia in alcoholic liver disease. Cell Physiol Biochem. 2021;55:91–116. doi: 10.33594/000000327. PubMed DOI PMC

Nissen S, Sharp RL, Panton L, Vukovich M, Trappe S, Fuller JC., Jr Beta-hydroxy-beta-methylbutyrate (HMB) supplementation in humans is safe and may decrease cardiovascular risk factors. J Nutr. 2000;130:1937–1945. doi: 10.1093/jn/130.8.1937. PubMed DOI

Rathmacher JA, Nissen S, Panton L, Clark RH, Eubanks May P, Barber AE, D’Olimpio J, Abumrad NN. Supplementation with a combination of beta-hydroxy-beta-methylbutyrate (HMB), arginine, and glutamine is safe and could improve hematological parameters. JPEN J Parenter Enteral Nutr. 2004;28:65–75. doi: 10.1177/014860710402800265. PubMed DOI

Holecek M, Muthny T, Kovarik M, Sispera L. Effect of beta-hydroxy-beta-methylbutyrate (HMB) on protein metabolism in whole body and in selected tissues. Food Chem Toxicol. 2009;47:255–259. doi: 10.1016/j.fct.2008.11.021. PubMed DOI

Holeček M, Vodeničarovová M, Fingrová R. Dual effects of beta-hydroxy-beta-methylbutyrate (HMB) on amino acid, energy, and protein metabolism in the liver and muscles of rats with streptozotocin-induced type 1 diabetes. Biomolecules. 2020;10:1475. doi: 10.3390/biom10111475. PubMed DOI PMC

Garlick PJ. The role of leucine in the regulation of protein metabolism. J Nutr. 2005;135(6 Suppl):1553S–1556S. doi: 10.1093/jn/135.6.1553S. PubMed DOI

Katsanos CS, Kobayashi H, Sheffield-Moore M, Aarsland A, Wolfe RR. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol. 2006;291:E381–E387. doi: 10.1152/ajpendo.00488.2005. PubMed DOI

Rieu I, Balage M, Sornet C, Giraudet C, Pujos E, Grizard J, Mosoni L, Dardevet D. Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidaemia. J Physiol. 2006;575:305–315. doi: 10.1113/jphysiol.2006.110742. PubMed DOI PMC

Guo K, Yu YH, Hou J, Zhang Y. Chronic leucine supplementation improves glycemic control in etiologically distinct mouse models of obesity and diabetes mellitus. Nutr Metab (Lond) 2010;7:57. doi: 10.1186/1743-7075-7-57. PubMed DOI PMC

Yang J, Chi Y, Burkhardt BR, Guan Y, Wolf BA. Leucine metabolism in regulation of insulin secretion from pancreatic beta cells. Nutr Rev. 2010;68:270–79. doi: 10.1111/j.1753-4887.2010.00282.x. PubMed DOI PMC

Dardevet D, Sornet C, Bayle G, Prugnaud J, Pouyet C, Grizard J. Postprandial stimulation of muscle protein synthesis in old rats can be restored by a leucine-supplemented meal. J Nutr. 2002;132:95–100. doi: 10.1093/jn/132.1.95. PubMed DOI

Xu ZR, Tan ZJ, Zhang Q, Gui QF, Yang YM. The effectiveness of leucine on muscle protein synthesis, lean body mass and leg lean mass accretion in older people: a systematic review and meta-analysis. Br J Nutr. 2015;113:25–34. doi: 10.1017/S0007114514002475. PubMed DOI

Crozier SJ, Kimball SR, Emmert SW, Anthony JC, Jefferson LS. Oral leucine administration stimulates protein synthesis in rat skeletal muscle. J Nutr. 2005;135:376–382. doi: 10.1093/jn/135.3.376. PubMed DOI

Verhoeven S, Vanschoonbeek K, Verdijk LB, et al. Long-term leucine supplementation does not increase muscle mass or strength in healthy elderly men. Am J Clin Nutr. 2009;89:1468–1475. doi: 10.3945/ajcn.2008.26668. PubMed DOI

Leenders M, Verdijk LB, van der Hoeven L, van Kranenburg J, Hartgens F, Wodzig WK, Saris WH, van Loon LJ. Prolonged leucine supplementation does not augment muscle mass or affect glycemic control in elderly type 2 diabetic men. J Nutr. 2011;141:1070–076. doi: 10.3945/jn.111.138495. PubMed DOI

Koopman R, Verdijk LB, Beelen M, Gorselink M, Kruseman AN, Wagenmakers AJ, Kuipers H, van Loon LJ. Co-ingestion of leucine with protein does not further augment post-exercise muscle protein synthesis rates in elderly men. Br J Nutr. 2008;99:571–580. doi: 10.1017/S0007114507812013. PubMed DOI

May RC, Piepenbrock N, Kelly RA, Mitch WE. Leucine-induced amino acid antagonism in rats: muscle valine metabolism and growth impairment. J Nutr. 1991;121:293–301. doi: 10.1093/jn/121.3.293. PubMed DOI

Block KP, Harper AE. Valine metabolism in vivo: effects of high dietary levels of leucine and isoleucine. Metabolism. 1984;33:559–566. doi: 10.1016/0026-0495(84)90012-x. PubMed DOI

Aftring RP, Block KP, Buse MG. Leucine and isoleucine activate skeletal muscle branched-chain alpha-keto acid dehydrogenase in vivo. Am J Physiol. 1986;250:E599–E604. doi: 10.1152/ajpendo.1986.250.5.E599. PubMed DOI

Jones SM, Yeaman SJ. Phosphorylation of branched-chain 2-oxo acid dehydrogenase complex in isolated adipocytes. Effects of 2-oxo acids. Biochem J. 1986;236:209–213. doi: 10.1042/bj2360209. PubMed DOI PMC

Frick GP, Tai LR, Blinder L, Goodman HM. L-Leucine activates branched chain alpha-keto acid dehydrogenase in rat adipose tissue. J Biol Chem. 1981;256:2618–2620. PubMed

Hertzman PA, Blevins WL, Mayer J, Greenfield B, Ting M, Gleich GJ. Association of the eosinophilia-myalgia syndrome with the ingestion of tryptophan. N Engl J Med. 1990;322:869–873. doi: 10.1056/NEJM199003293221301. PubMed DOI

Fernstrom JD. Effects and side effects associated with the non-nutritional use of tryptophan by humans. J Nutr. 2012;142:2236S–2244S. doi: 10.3945/jn.111.157065. PubMed DOI

Scotton WJ, Hill LJ, Williams AC, Barnes NM. Serotonin syndrome: Pathophysiology, clinical features, management, and potential future directions. Int J Tryptophan Res. 2019;12:1178646919873925. doi: 10.1177/1178646919873925. PubMed DOI PMC

Xue P, Fu J, Zhou Y. The aryl hydrocarbon receptor and tumor immunity. Front Immunol. 2018;9:286. doi: 10.3389/fimmu.2018.00286. PubMed DOI PMC

Valente-Silva P, Cervenka I, Ferreira DMS, Correia JC, Edman S, Horwath O, Heng B, Chow S, Jacobs KR, Guillemin GJ, Blomstrand E, Ruas JL. Effects of tryptophan supplementation and exercise on the fate of kynurenine metabolites in mice and humans. Metabolites. 2021;11:508. doi: 10.3390/metabo11080508. PubMed DOI PMC

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