Branched-Chain Amino Acids (BCAAs)
OVERVIEW
Branched-chain amino acids are essential nutrients that the body obtains from proteins found in food, especially meat, dairy products, and legumes. They include leucine, isoleucine, and valine. "Branched-chain" refers to the chemical structure of these amino acids. People use branched-chain amino acids for medicine.
Branched-chain amino acids are commonly taken by mouth or given intravenously (by IV) by healthcare providers for brain conditions due to liver disease (acute, chronic, and latent hepatic encephalopathy). Branched-chain amino acids are used for many other conditions and may be taken by athletes to improve athletic performance, prevent fatigue, improve concentration, and reduce muscle breakdown during intense exercise. But there is limited scientific research to support these other uses.
CLASSIFICATION
Is a Form of:
Essential nutrient obtained from proteins
Primary Function:
Brain conditions due to liver disease
Also Known As:
Acide Isovalérique de Leucine, Acides Aminés à Chaîne Ramifiée, Acides Aminés Ramifiés
HOW DOES IT WORK?
Branched-chain amino acids stimulate the building of protein in muscle and possibly reduce muscle breakdown. Branched-chain amino acids seem to prevent faulty message transmission in the brain cells of people with advanced liver disease, mania, tardive dyskinesia, and anorexia.
USES
- Poor brain function related to liver disease. Taking branched-chain amino acids by mouth seems to improve liver function in people with poor brain function caused by liver disease. Branched-chain amino acids may also improve mental function or reverse comas in people with this condition, but conflicting results exist. Branched-chain amino acids don't appear to reduce the chance of death in people with this condition.
- Consuming a drink containing branched-chain amino acids seems to reduce symptoms of mania.
- Movement disorder called tardive dyskinesia. Taking branched-chain amino acids by mouth seems to reduce symptoms of the muscle disorder called tardive dyskinesia.
RECOMMENDED DOSING
The following doses have been studied in scientific research:
BY MOUTH:
- For a brain condition due to liver disease (hepatic encephalopathy): 240 mg/kg/day up to 25 grams of branched-chain amino acids daily for three months. In some cases the dose is taken in three divided doses daily.
- For mania: a 60 gram branched-chain amino acid drink containing valine, isoleucine, and leucine in a ratio of 3:3:4 taken every morning for 7 days.
- For tardive dyskinesia: a branched-chain amino acid drink containing valine, isoleucine, and leucine at a dose of 222 mg/kg taken three times daily for 3 weeks.
FREQUENTLY ASKED QUESTIONS:
What do BCAA supplements do?
The branched-chain amino acids (BCAAs) are a group of three essential amino acids: leucine, isoleucine and valine. They are essential, meaning they can't be produced by your body and must be obtained from food. BCAA supplements have been shown to build muscle, decrease muscle fatigue and alleviate muscle soreness.
Are BCAA supplements worth it?
"During exercise, whether you're lifting weights, running or cycling, your body will start to use those BCAAs for energy," Dr Kendall explains. So, it makes sense in theory, but Dr Kendall says that studies show that BCAAs make no difference to elite performance.
When should I take BCAA supplements?
Best Time to Take BCAAs. The ideal time to take branched-chain amino acids is during workouts by adding 5-10 grams to your shake regimen, both pre-workout or post-workout, to fuel your body and repair your muscles.
What amino acids are BCAA?
BCAA refers to three of the essential amino acids: leucine, isoleucine and valine. They are different to the other essential amino acids because of their 'branched-chain' structure.
Should I take BCAA every day?
Research has shown supplemental BCAA intake to be safe for healthy adults in doses of 4-20 g per day, with prolonged intake one week or more showing greater benefits than acute (short term) intake. Aim for 2-3 g leucine between meals, before, during or after workouts to maximize muscle protein synthesis.
Does BCAA have side effects?
Branched-chain amino acids are POSSIBLY SAFE when taken by mouth appropriately for up to 2 years. Some side effects are known to occur, such as fatigue and loss of coordination.
Does BCAA burn belly fat?
Amino acids, especially BCAAs, have been shown to help athletes burn more body fat—especially belly fat.
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Can BCAAs make you gain weight?
Branched-chain amino acids may help prevent weight gain and enhance fat loss. In another study, weightlifters given 14 grams of BCAAs per day lost 1% more body fat over the eight-week study period than those given 28 grams of whey protein per day. The BCAA group also gained 4.4 lbs (2 kg) more muscle.
Is BCAA better than whey protein?
BCAA stands for Branched Chain Amino Acid. As a rule, BCAAs have a lower caloric content than whey protein, which makes them better if you are trying to cut weight while still maintaining muscle. They are also more readily available than whey protein is, and can help premature fatigue when training fasted.
Which is better BCAA or amino acids?
BCAAs are essential amino acids, but they have a branched-chain structure that sets them apart from the other EAAs. They are the building blocks of protein. Although branched-chain amino acids are in EAAs, the quantity is higher in pure BCAA supplements. Protein helps to promote muscle maintenance and growth.
Should I take BCAA and amino acids?
Use anytime – before, during, and after workouts.
BCAAs can be taken before, during, and after workouts to rapidly increase amino acid levels in the bloodstream, promote protein synthesis, and prevent muscle protein breakdown.
Can you drink BCAAs all day?
Our trainers and nutritionists recommend that you take BCAAs during your workouts, throughout the day on non-training days, and between meals. In short, you can be pretty flexible about when you take BCAAs, as long as you're not forcing them to compete with other nutrients in your digestive system to get absorbed.
Do I need BCAAs if I take protein?
That's because BCAA supplements don't contain all nine of the essential amino acids, while whey protein does. As a result, your muscle response won't be as high as it could be. In fact, it's unlikely that you even need BCAAs if you're already taking in enough protein, as we reported.
Is BCAA bad for liver?
Increased intake of branched chain amino acids (BCAA, essential amino acids compromising 20% of total protein intake) reduces body weight. However, elevated circulating BCAA is associated with non-alcoholic fatty liver disease and injury.
Does BCAA cause hair loss?
BCAAs have been shown to help retain muscle mass and maximize fat loss in conjunction with a calorie-restricted diet. Can BCAAs cause hair loss? Hair loss can point to amino acid deficiencies (as well as iron and vitamin deficiencies), so actually the opposite is true.
What do BCAA supplements do?
Our trainers and nutritionists recommend that you take BCAAs during your workouts, throughout the day on non-training days, and between meals. In short, you can be pretty flexible about when you take BCAAs, as long as you're not forcing them to compete with other nutrients in your digestive system to get absorbed.
Should I take BCAAs before bed?
BCAAs can be taken at any time—before, during, or after exercise, as well as throughout the day and before bed. Many people believe that taking BCAAs at bedtime can help with overnight muscle-protein synthesis.
Do BCAAs affect hormones?
Amino acids (AAs), especially BCAAs, play pivotal roles in hormonal secretion and action as well as in intracellular signaling. There is emerging data showing that BCAAs regulate gene transcription and translation. AAs stimulate protein synthesis and inhibit protein breakdown in skeletal muscle and liver.
Is too much BCAAs bad?
Research from the University of Sydney concluded that relying too heavily on BCAAs (branched chain amino acids, which are found in protein shakes) may reduce lifespan, and cause weight gain and a lower mood.
CLINICAL STUDIES
- ^ A multi-nutrient supplement reduced markers of inflammation and improved physical performance in active individuals of middle to older age: a randomized, double-blind, placebo-controlled study.
- ^ a b c Consuming a supplement containing branched-chain amino acids during a resistance-training program increases lean mass, muscle strength and fat loss.
- ^ Combination of branched-chain amino acids and angiotensin-converting enzyme inhibitor suppresses the cumulative recurrence of hepatocellular carcinoma: a randomized control trial.
- ^ Yoshizawa F. New therapeutic strategy for amino acid medicine: notable functions of branched chain amino acids as biological regulators. J Pharmacol Sci. (2012)
- ^ Dietary Protein Impact on Glycemic Control during Weight Loss.
- ^ a b Riazi R, et al. The total branched-chain amino acid requirement in young healthy adult men determined by indicator amino acid oxidation by use of L-{1-13C}phenylalanine. J Nutr. (2003)
- ^ a b c d e f g Nutraceutical Effects of Branched-Chain Amino Acids on Skeletal Muscle.
- ^ Ahlborg G, et al. Substrate turnover during prolonged exercise in man. Splanchnic and leg metabolism of glucose, free fatty acids, and amino acids. J Clin Invest. (1974)
- ^ Wahren J, Felig P, Hagenfeldt L. Effect of protein ingestion on splanchnic and leg metabolism in normal man and in patients with diabetes mellitus. J Clin Invest. (1976)
- ^ Yoshiji H, et al. Combination of branched-chain amino acid and angiotensin-converting enzyme inhibitor improves liver fibrosis progression in patients with cirrhosis. Mol Med Report. (2012)
- ^ Reynolds B, et al. Amino acid transporters and nutrient-sensing mechanisms: new targets for treating insulin-linked disorders. Biochem Soc Trans. (2007)
- ^ Boado RJ, et al. Selective expression of the large neutral amino acid transporter at the blood-brain barrier. Proc Natl Acad Sci U S A. (1999)
- ^ Pardridge WM, Choi TB. Neutral amino acid transport at the human blood-brain barrier. Fed Proc. (1986)
- ^ Effects of leucine on intestinal absorption of tryptophan in rats.
- ^ a b c d Harris RA, et al. Regulation of the branched-chain alpha-ketoacid dehydrogenase and elucidation of a molecular basis for maple syrup urine disease. Adv Enzyme Regul. (1990)
- ^ a b c Shimomura Y, et al. Branched-chain alpha-keto acid dehydrogenase complex in rat skeletal muscle: regulation of the activity and gene expression by nutrition and physical exercise. J Nutr. (1995)
- ^ a b c Kobayashi R, et al. Hepatic branched-chain alpha-keto acid dehydrogenase complex in female rats: activation by exercise and starvation. J Nutr Sci Vitaminol (Tokyo). (1999)
- ^ a b c Shimomura Y, et al. Suppression of glycogen consumption during acute exercise by dietary branched-chain amino acids in rats. J Nutr Sci Vitaminol (Tokyo). (2000)
- ^ a b c Howarth KR, et al. Exercise training increases branched-chain oxoacid dehydrogenase kinase content in human skeletal muscle. Am J Physiol Regul Integr Comp Physiol. (2007)
- ^ a b Harper AE, Miller RH, Block KP. Branched-chain amino acid metabolism. Annu Rev Nutr. (1984)
- ^ Damuni Z, Reed LJ. Purification and properties of the catalytic subunit of the branched-chain alpha-keto acid dehydrogenase phosphatase from bovine kidney mitochondria. J Biol Chem. (1987)
- ^ Popov KM, et al. Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases. J Biol Chem. (1992)
- ^ Shimomura Y, et al. Purification and partial characterization of branched-chain alpha-ketoacid dehydrogenase kinase from rat liver and rat heart. Arch Biochem Biophys. (1990)
- ^ Shimomura Y, et al. Regulation of branched-chain amino acid catabolism: nutritional and hormonal regulation of activity and expression of the branched-chain alpha-keto acid dehydrogenase kinase. Curr Opin Clin Nutr Metab Care. (2001)
- ^ Suryawan A, et al. A molecular model of human branched-chain amino acid metabolism. Am J Clin Nutr. (1998)
- ^ a b c Xu M, et al. Mechanism of activation of branched-chain alpha-keto acid dehydrogenase complex by exercise. Biochem Biophys Res Commun. (2001)
- ^ a b c Paxton R, Harris RA. Regulation of branched-chain alpha-ketoacid dehydrogenase kinase. Arch Biochem Biophys. (1984)
- ^ Kobayashi R, et al. Clofibric acid stimulates branched-chain amino acid catabolism by three mechanisms. Arch Biochem Biophys. (2002)
- ^ Teräväinen H, Larsen A, Hillbom M. Clofibrate-induced myopathy in the rat. Acta Neuropathol. (1977)
- ^ Paul HS, Adibi SA. Paradoxical effects of clofibrate on liver and muscle metabolism in rats. Induction of myotonia and alteration of fatty acid and glucose oxidation. J Clin Invest. (1979)
- ^ Shiraki M, et al. Activation of hepatic branched-chain alpha-keto acid dehydrogenase complex by tumor necrosis factor-alpha in rats. Biochem Biophys Res Commun. (2005)
- ^ a b Shimomura Y, et al. Branched-chain 2-oxo acid dehydrogenase complex activation by tetanic contractions in rat skeletal muscle. Biochim Biophys Acta. (1993)
- ^ Wagenmakers AJ, et al. Exercise-induced activation of the branched-chain 2-oxo acid dehydrogenase in human muscle. Eur J Appl Physiol Occup Physiol. (1989)
- ^ a b Ament W, Verkerke GJ. Exercise and fatigue. Sports Med. (2009)
- ^ a b Davis JM, Alderson NL, Welsh RS. Serotonin and central nervous system fatigue: nutritional considerations. Am J Clin Nutr. (2000)
- ^ a b c Blomstrand E. A role for branched-chain amino acids in reducing central fatigue. J Nutr. (2006)
- ^ Blomstrand E. Amino acids and central fatigue. Amino Acids. (2001)
- ^ Blomstrand E, Celsing F, Newsholme EA. Changes in plasma concentrations of aromatic and branched-chain amino acids during sustained exercise in man and their possible role in fatigue. Acta Physiol Scand. (1988)
- ^ Fernstrom JD, Wurtman RJ. Brain serotonin content: physiological regulation by plasma neutral amino acids. Science. (1972)
- ^ Fernstrom JD, Faller DV. Neutral amino acids in the brain: changes in response to food ingestion. J Neurochem. (1978)
- ^ Pardridge WM. Blood-brain barrier carrier-mediated transport and brain metabolism of amino acids. Neurochem Res. (1998)
- ^ Blomstrand E, et al. Effect of carbohydrate ingestion on brain exchange of amino acids during sustained exercise in human subjects. Acta Physiol Scand. (2005)
- ^ Nybo L, et al. Neurohumoral responses during prolonged exercise in humans. J Appl Physiol. (2003)
- ^ Meeusen R, et al. Effects of tryptophan and/or acute running on extracellular 5-HT and 5-HIAA levels in the hippocampus of food-deprived rats. Brain Res. (1996)
- ^ a b c d Falavigna G, et al. Effects of diets supplemented with branched-chain amino acids on the performance and fatigue mechanisms of rats submitted to prolonged physical exercise. Nutrients. (2012)
- ^ Gomez-Merino D, et al. Evidence that the branched-chain amino acid L-valine prevents exercise-induced release of 5-HT in rat hippocampus. Int J Sports Med. (2001)
- ^ Armon C. Sports and trauma in amyotrophic lateral sclerosis revisited. J Neurol Sci. (2007)
- ^ Chiò A, et al. Severely increased risk of amyotrophic lateral sclerosis among Italian professional football players. Brain. (2005)
- ^ a b Belli S, Vanacore N. Proportionate mortality of Italian soccer players: is amyotrophic lateral sclerosis an occupational disease. Eur J Epidemiol. (2005)
- ^ Valenti M, et al. Amyotrophic lateral sclerosis and sports: a case-control study. Eur J Neurol. (2005)
- ^ a b c Carunchio I, et al. Increased levels of p70S6 phosphorylation in the G93A mouse model of Amyotrophic Lateral Sclerosis and in valine-exposed cortical neurons in culture. Exp Neurol. (2010)
- ^ Vucic S, Kiernan MC. Cortical excitability testing distinguishes Kennedy's disease from amyotrophic lateral sclerosis. Clin Neurophysiol. (2008)
- ^ Zanette G, et al. Changes in motor cortex inhibition over time in patients with amyotrophic lateral sclerosis. J Neurol. (2002)
- ^ Pieri M, et al. Increased persistent sodium current determines cortical hyperexcitability in a genetic model of amyotrophic lateral sclerosis. Exp Neurol. (2009)
- ^ van Zundert B, et al. Neonatal neuronal circuitry shows hyperexcitable disturbance in a mouse model of the adult-onset neurodegenerative disease amyotrophic lateral sclerosis. J Neurosci. (2008)
- ^ Hinault C, et al. Amino acids and leucine allow insulin activation of the PKB/mTOR pathway in normal adipocytes treated with wortmannin and in adipocytes from db/db mice. FASEB J. (2004)
- ^ Uberall F, et al. Evidence that atypical protein kinase C-lambda and atypical protein kinase C-zeta participate in Ras-mediated reorganization of the F-actin cytoskeleton. J Cell Biol. (1999)
- ^ a b c d e Nishitani S, et al. Leucine promotes glucose uptake in skeletal muscles of rats. Biochem Biophys Res Commun. (2002)
- ^ a b c Chang TW, Goldberg AL. Leucine inhibits oxidation of glucose and pyruvate in skeletal muscles during fasting. J Biol Chem. (1978)
- ^ a b Tessari P, et al. Hyperaminoacidaemia reduces insulin-mediated glucose disposal in healthy man. Diabetologia. (1985)
- ^ a b c Flakoll PJ, et al. Short-term regulation of insulin-mediated glucose utilization in four-day fasted human volunteers: role of amino acid availability. Diabetologia. (1992)
- ^ a b Du M, et al. Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase. J Anim Sci. (2007)
- ^ Hardie DG. Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism. Proc Nutr Soc. (2011)
- ^ O'Neill HM. AMPK and Exercise: Glucose Uptake and Insulin Sensitivity. Diabetes Metab J. (2013)
- ^ Tremblay F, Marette A. Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells. J Biol Chem. (2001)
- ^ Takano A, et al. Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin. Mol Cell Biol. (2001)
- ^ Haruta T, et al. A rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1. Mol Endocrinol. (2000)
- ^ a b Newgard CB, et al. A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistance. Cell Metab. (2009)
- ^ a b Wang TJ, et al. Metabolite profiles and the risk of developing diabetes. Nat Med. (2011)
- ^ a b c Doi M, et al. Isoleucine, a potent plasma glucose-lowering amino acid, stimulates glucose uptake in C2C12 myotubes. Biochem Biophys Res Commun. (2003)
- ^ Doi M, et al. Hypoglycemic effect of isoleucine involves increased muscle glucose uptake and whole body glucose oxidation and decreased hepatic gluconeogenesis. Am J Physiol Endocrinol Metab. (2007)
- ^ Doi M, et al. Isoleucine, a blood glucose-lowering amino acid, increases glucose uptake in rat skeletal muscle in the absence of increases in AMP-activated protein kinase activity. J Nutr. (2005)
- ^ a b Peyrollier K, et al. L-leucine availability regulates phosphatidylinositol 3-kinase, p70 S6 kinase and glycogen synthase kinase-3 activity in L6 muscle cells: evidence for the involvement of the mammalian target of rapamycin (mTOR) pathway in the L-leucine-induced up-regulation of system A amino acid transport. Biochem J. (2000)
- ^ Armstrong JL, et al. Regulation of glycogen synthesis by amino acids in cultured human muscle cells. J Biol Chem. (2001)
- ^ Letto J, Brosnan ME, Brosnan JT. Valine metabolism. Gluconeogenesis from 3-hydroxyisobutyrate. Biochem J. (1986)
- ^ van Hall G, et al. Mechanisms of activation of muscle branched-chain alpha-keto acid dehydrogenase during exercise in man. J Physiol. (1996)
- ^ Gibala MJ, Young ME, Taegtmeyer H. Anaplerosis of the citric acid cycle: role in energy metabolism of heart and skeletal muscle. Acta Physiol Scand. (2000)
- ^ a b c Gualano AB, et al. Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. J Sports Med Phys Fitness. (2011)
- ^ a b c Blomstrand E, et al. Influence of ingesting a solution of branched-chain amino acids on perceived exertion during exercise. Acta Physiol Scand. (1997)
- ^ Marchesini G, et al. Nutritional supplementation with branched-chain amino acids in advanced cirrhosis: a double-blind, randomized trial. Gastroenterology. (2003)
- ^ Kawamura-Yasui N, et al. Evaluating response to nutritional therapy using the branched-chain amino acid/tyrosine ratio in patients with chronic liver disease. J Clin Lab Anal. (1999)
- ^ Nishitani S, et al. Branched-chain amino acids improve glucose metabolism in rats with liver cirrhosis. Am J Physiol Gastrointest Liver Physiol. (2005)
- ^ Takeshita Y, et al. Beneficial effect of branched-chain amino acid supplementation on glycemic control in chronic hepatitis C patients with insulin resistance: implications for type 2 diabetes. Metabolism. (2012)
- ^ Felig P, Marliss E, Cahill GF Jr. Plasma amino acid levels and insulin secretion in obesity. N Engl J Med. (1969)
- ^ Caballero B, Finer N, Wurtman RJ. Plasma amino acids and insulin levels in obesity: response to carbohydrate intake and tryptophan supplements. Metabolism. (1988)
- ^ Shah SH, et al. Branched-chain amino acid levels are associated with improvement in insulin resistance with weight loss. Diabetologia. (2012)
- ^ Tai ES, et al. Insulin resistance is associated with a metabolic profile of altered protein metabolism in Chinese and Asian-Indian men. Diabetologia. (2010)
- ^ She P, et al. Disruption of BCATm in mice leads to increased energy expenditure associated with the activation of a futile protein turnover cycle. Cell Metab. (2007)
- ^ Pietiläinen KH, et al. Global transcript profiles of fat in monozygotic twins discordant for BMI: pathways behind acquired obesity. PLoS Med. (2008)
- ^ Lefort N, et al. Increased reactive oxygen species production and lower abundance of complex I subunits and carnitine palmitoyltransferase 1B protein despite normal mitochondrial respiration in insulin-resistant human skeletal muscle. Diabetes. (2010)
- ^ Lu J, et al. Insulin resistance and the metabolism of branched-chain amino acids. Front Med. (2013)
- ^ Xiao F, et al. Leucine deprivation increases hepatic insulin sensitivity via GCN2/mTOR/S6K1 and AMPK pathways. Diabetes. (2011)
- ^ Dietary Leucine - An Environmental Modifier of Insulin Resistance Acting on Multiple Levels of Metabolism.
- ^ Anthony JC, et al. Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J Nutr. (2000)
- ^ Drummond MJ, et al. Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis. J Physiol. (2009)
- ^ Phosphorylation and Activation of p70s6k by PDK1.
- ^ a b c Blomstrand E, et al. Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. J Nutr. (2006)
- ^ Wang X, Proud CG. The mTOR pathway in the control of protein synthesis. Physiology (Bethesda). (2006)
- ^ Proud CG. mTOR-mediated regulation of translation factors by amino acids. Biochem Biophys Res Commun. (2004)
- ^ a b Kimball SR, Jefferson LS. Regulation of global and specific mRNA translation by oral administration of branched-chain amino acids. Biochem Biophys Res Commun. (2004)
- ^ Resistance exercise increases AMPK activity and reduces 4E-BP1 phosphorylation and protein synthesis in human skeletal muscle.
- ^ Resistance Exercise Increases Muscle Protein Synthesis and Translation of Eukaryotic Initiation Factor 2Bϵ mRNA in a Mammalian Target of Rapamycin-dependent Manner.
- ^ Hornberger TA, Chien S. Mechanical stimuli and nutrients regulate rapamycin-sensitive signaling through distinct mechanisms in skeletal muscle. J Cell Biochem. (2006)
- ^ Corradetti MN, Inoki K, Guan KL. The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway. J Biol Chem. (2005)
- ^ a b Vander Haar E, et al. Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40. Nat Cell Biol. (2007)
- ^ Elmadhun NY, et al. Metformin alters the insulin signaling pathway in ischemic cardiac tissue in a swine model of metabolic syndrome. J Thorac Cardiovasc Surg. (2013)
- ^ Louard RJ, Barrett EJ, Gelfand RA. Effect of infused branched-chain amino acids on muscle and whole-body amino acid metabolism in man. Clin Sci (Lond). (1990)
- ^ Nair KS, Schwartz RG, Welle S. Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. Am J Physiol. (1992)
- ^ Alvestrand A, et al. Influence of leucine infusion on intracellular amino acids in humans. Eur J Clin Invest. (1990)
- ^ Liu Z, et al. Branched chain amino acids activate messenger ribonucleic acid translation regulatory proteins in human skeletal muscle, and glucocorticoids blunt this action. J Clin Endocrinol Metab. (2001)
- ^ a b Greiwe JS, et al. Leucine and insulin activate p70 S6 kinase through different pathways in human skeletal muscle. Am J Physiol Endocrinol Metab. (2001)
- ^ Navé BT, et al. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem J. (1999)
- ^ Inoki K, et al. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat Cell Biol. (2002)
- ^ Manning BD, et al. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol Cell. (2002)
- ^ Glass DJ. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat Cell Biol. (2003)
- ^ Browne GJ, Proud CG. Regulation of peptide-chain elongation in mammalian cells. Eur J Biochem. (2002)
- ^ Jones SW, et al. Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass. FASEB J. (2004)
- ^ Bodine SC, et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. (2001)
- ^ Sandri M, et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell. (2004)
- ^ Stitt TN, et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell. (2004)
- ^ Borgenvik M, Apró W, Blomstrand E. Intake of branched-chain amino acids influences the levels of MAFbx mRNA and MuRF-1 total protein in resting and exercising human muscle. Am J Physiol Endocrinol Metab. (2012)
- ^ Newsholme P, et al. New insights into amino acid metabolism, beta-cell function and diabetes. Clin Sci (Lond). (2005)
- ^ Co-Ingestion of a Protein Hydrolysate with or without Additional Leucine Effectively Reduces Postprandial Blood Glucose Excursions in Type 2 Diabetic Men.
- ^ Lynch CJ, et al. Leucine is a direct-acting nutrient signal that regulates protein synthesis in adipose tissue. Am J Physiol Endocrinol Metab. (2002)
- ^ Lynch CJ, et al. Tissue-specific effects of chronic dietary leucine and norleucine supplementation on protein synthesis in rats. Am J Physiol Endocrinol Metab. (2002)
- ^ Lynch CJ, et al. Regulation of amino acid-sensitive TOR signaling by leucine analogues in adipocytes. J Cell Biochem. (2000)
- ^ Jin G, et al. Changes in plasma and tissue amino acid levels in an animal model of complex fatigue. Nutrition. (2009)
- ^ a b c Shimomura Y, et al. Branched-chain amino acid supplementation before squat exercise and delayed-onset muscle soreness. Int J Sport Nutr Exerc Metab. (2010)
- ^ Ispoglou T, et al. Daily L-leucine supplementation in novice trainees during a 12-week weight training program. Int J Sports Physiol Perform. (2011)
- ^ Portier H, et al. Effects of branched-chain amino acids supplementation on physiological and psychological performance during an offshore sailing race. Eur J Appl Physiol. (2008)
- ^ Bigard AX, et al. Branched-chain amino acid supplementation during repeated prolonged skiing exercises at altitude. Int J Sport Nutr. (1996)
- ^ Shimizu M, et al. Energy expenditure during 2-day trail walking in the mountains (2,857 m) and the effects of amino acid supplementation in older men and women. Eur J Appl Physiol. (2012)
- ^ van Hall G, et al. Ingestion of branched-chain amino acids and tryptophan during sustained exercise in man: failure to affect performance. J Physiol. (1995)
- ^ Blomstrand E, et al. Administration of branched-chain amino acids during sustained exercise--effects on performance and on plasma concentration of some amino acids. Eur J Appl Physiol Occup Physiol. (1991)
- ^ Effect of branched-chain amino acid supplementation on mental performance.
- ^ Wiśnik P, et al. The effect of branched chain amino acids on psychomotor performance during treadmill exercise of changing intensity simulating a soccer game. Appl Physiol Nutr Metab. (2011)
- ^ Shimomura Y, et al. Effects of squat exercise and branched-chain amino acid supplementation on plasma free amino acid concentrations in young women. J Nutr Sci Vitaminol (Tokyo). (2009)
- ^ Bradley WG1, Mash DC. Beyond Guam: the cyanobacteria/BMAA hypothesis of the cause of ALS and other neurodegenerative diseases. Amyotroph Lateral Scler. (2009)
- ^ Cox PA1, Sacks OW. Cycad neurotoxins, consumption of flying foxes, and ALS-PDC disease in Guam. Neurology. (2002)
- ^ Abel EL. Football increases the risk for Lou Gehrig's disease, amyotrophic lateral sclerosis. Percept Mot Skills. (2007)
- ^ Manuel M1, Heckman CJ. Stronger is not always better: could a bodybuilding dietary supplement lead to ALS. Exp Neurol. (2011)
- ^ Elango R, et al. Determination of the tolerable upper intake level of leucine in acute dietary studies in young men. Am J Clin Nutr. (2012)
- Blomstrand E, Hassmén P, Newsholme EA. Effect of branched-chain amino acid supplementation on mental performance. Acta Physiol Scand. (1991)