Recent posts: Amino Acids
All About BCAAs
What are branched chain amino acids?
Amino acids are the building blocks of protein. Branched chain amino acids (BCAAs) are so called because of their structure, which includes a “side chain” of one carbon atom and three hydrogen atoms. There are three BCAAs: leucine, isoleucine, and valine. Of these, leucine is the most heavily researched, and appears to offer the biggest physiological benefit. (More on that below.)
For the science geeks, these hydrophobic (water-fearing) amino acids are referred to as “aliphatic” (from the Greek aleiphar, or oil), as their central carbon attaches to a branched non-cyclic, open carbon chain.

BCAAs provide the basis for protein synthesis and energy production (Harper AE et al 1984; Patti ME et al 1998; Xu G et al 1998; Anthony JC et al 2001). In fact, BCAAs can comprise up to one-third of muscle protein (Mero 1999). Because of their prevalence and involvement in protein synthesis and energy production, BCAAs are important to many metabolic processes.
However, if BCAAs are going to participate in these processes, they must be available to the body. This means we have to eat enough BCAAs, and at the right times, to enable such processes to occur.
Why is adequate BCAA intake so important?
The BCAAs are the only amino acids not degraded in the liver. All other amino acids are regulated by the gut and the liver before being circulated elsewhere in the body. However, BCAAs head directly into the bloodstream. This means that dietary intake of BCAAs directly influences plasma levels and concentrations in muscle tissue (Layman DK 2003). Interestingly, BCAAs are burned for energy (oxidized) during exercise, so they’re also an important exercise fuel.
Consuming BCAAs before training can increase uptake into muscle tissue (Mittleman KD et al 1998). This has many benefits:
- BCAA supplementation may lower lactate levels after resistance training and improve muscular oxidation.
- BCAAs may increase growth hormone (GH) circulation, which may be related to anabolic mechanisms causing muscle growth (De Palo EF et al 2001).
- BCAA supplementation may decrease serum concentrations of the intramuscular enzymes creatine kinase and lactate dehydrogenase following prolonged exercise. This can decrease muscle damage and improve recovery (Coombes JS, McNaughton LR 2000).
Muscle is an important site of BCAA activity. There is an increased cell concentration and breakdown of BCAAs in muscle tissue (Layman DK 2003). BCAAs are continuously released from the liver and other internal organs to skeletal muscle so that the BCAAs can assist in maintaining blood sugar levels. Indeed, BCAAs may be responsible for up to 40% of blood sugar production during exercise (Ahlborg G et al 1974; Ruberman NB 1975; see also Layman DK 2003).
What you should know
Because BCAAs are so important to muscle tissue, and because they help maintain blood sugar levels, it’s important to get enough to support your workouts. Consuming a carbohydrate, protein, and amino acid beverage during and after training can induce an insulin response, which helps transport BCAAs into cells. However, availability of leucine is more important than insulin. Within the muscle cell there’s one particular regulatory pathway for protein synthesis that’s stimulated by insulin, but dependent on leucine (Anthony et al 2000). In other words, protein synthesis (and hence muscle rebuilding) depends on how much leucine is available. And since BCAA levels decline with exercise, it makes sense to supplement with them during and/or after workouts (Mero 1999).
Because it’s so important to have leucine available for protein synthesis, if you train in a fasted state, or don’t eat after exercise, you’re going to lose more protein than you rebuild. However, if you eat adequate BCAAs during this time, especially leucine, you’ll enhance protein synthesis.
For extra credit
For the body to make new proteins, it needs an estimated daily leucine intake of between 1 to 4 grams/day (FAO/WHO/UNU 1985). That minimum intake needs to be met before leucine will be able to impact the insulin signaling pathway. But that’s just a baseline. Actual metabolic use, especially by athletes and people doing heavy resistance training, may be upwards of 12 grams/day.
There is a theory that BCAAs can limit central fatigue with endurance athletes, but it doesn’t appear to be supported by current data.
BCAA content of foods (grams of amino acids/100 g of protein)
Whey protein isolate 26%
Milk protein 21%
Muscle protein 18%
Soy protein isolate 18%
Wheat protein 15%
Source: USDA Food Composition Tables
Summary and recommendations
BCAAs play an important role in:
- Synthesis of proteins in general
- Glucose homeostasis (i.e. keeping blood sugar levels constant)
- Direct regulation of muscle protein synthesis (via insulin signaling cascade)
BCAAs’ potential impact on the aforementioned processes depends upon availability and dietary intake.
Adequate consumption of BCAAs may help manage body fat, spare muscle mass, and regulate glucose/insulin balance.
How can you put this knowledge to use?
Try adding BCAAs into your workout drink at a rate of 5 g BCAA per hour of training.
During periods of lower calorie intake, try adding a BCAA supplement every 2-4 hours during the day.
References
Anthony JC, et al. Signaling pathways involved in translational control of protein synthesis in skeletal muscle by leucine. J Nutr 2001;131:856S-860S.
Anthony JC, et al. Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation. J Nutr 2000;130:139-145.
Ahlborg G, et al. Substrate turnover during prolonged exercise in man. J Clin Invest 1974;53:1080-1090.
Coombes JS, McNaughton LR. Effects of branched-chain amino acid supplementation on serum creatine kinase and lactate dehydrogenase after prolonged exercise. J Sports Med Phys Fitness 2000;40:240-246.
De Palo EF, et al. Plasma lactate, GH and GH-binding protein levels in exercise following BCAA supplementation in athletes. Amino Acids 2001;20:1-11.
FAO/WHO/UNU. Energy and protein requirements. Report of joint FAO/WHO/UNU expert consultation. WHO Tech Pep Ser 1985;724:1-206.
Garlick PJ. The role of leucine in the regulation of protein metabolism. J Nutr. 2005 Jun;135(6 Suppl):1553S-6S. Review.
Harper AE, et al. Branched-chain amino acid metabolism. Annu Rev Nutr 1984;4:409-454.
Layman DK. The role of leucine in weight loss diets and glucose homeostasis. J Nutr 2003;133:261S-267S.
Mero A. Leucine supplementation and intensive training. Sports Med 1999;27:347-358.
Mittleman KD, et al. Branched chain amino acids prolong exercise during heat stress in men and women. Med Sci Sports Exerc 1998;30:83-91.
Patti ME, et al. Bidirectional modulation of insulin action by amino acids. J Clin Invest 1998;101:1519-1529.
Ruberman NB. Muscle amino acid metabolism and gluconeogenesis. Ann Rev Med 1975;26:245-258.
Xu G, et al. Branched-chain amino acids are essential in the regulation of PHAS-I and p70 S6 kinase by pancreatic beta cells. J Biol Chem 1998;273:28178-28184.
All About Glutamine
What is glutamine?
Glutamine is the most abundant free amino acid in the human body, making up about 60% of the skeletal muscle amino acid pool. (For more on amino acids, see All About BCAAs and All About Protein sections.)
Glutamine is a conditionally essential amino acid, which means that normally our bodies don’t need it from our diet. Exogeneous glutamine (in other words, glutamine we supplement or consume in food) is essential only under certain conditions, which include stress, trauma, muscular dystrophy, and illness, which can decrease glutamine levels by up to 50% (in severe cases). Because glutamine is a precursor for the structural unit of DNA and RNA, rapidly dividing cells are most likely to suffer from a shortage.
When we aren’t experiencing stress, trauma, muscular dystrophy or illness, our body produces enough glutamine on its own to supply our needs. The major part of endogenously produced (in other words, stuff our body makes) glutamine comes from skeletal muscle. Vitamin B3 and B6 are necessary for the production of glutamine from glutamic acid.

Why is glutamine so important?
Glutamine is a vital fuel source for the intestines and immune system that helps to keep defenses up against microbes. By nourishing these cells, it maintains the integrity of the GI tract.
Since the immune system is necessary for recovery from stress, glutamine may help during intense bouts of training. It may play a role in:
- Normalizing growth hormone
- Promoting glucose uptake after workouts
- Enhancing the hydration state of a muscle
- Reducing acid buildup with exercise
Yet it doesn’t seem that exercise decreases glutamine concentrations enough to compromise regular immune functions. This makes sense, since those who consume adequate energy from their diet tend to have a high glutamine intake. However, some people whose training and diet causes physical stress may benefit, e.g. people who are eating less food than necessary to modify body composition (in other words, dieting) or people whose training is extremely strenuous (such as elite athletes).
What you should know about glutamine
Where to find it
Cabbage and beets contain high concentrations of glutamine. (Eastern European grandmothers everywhere, rejoice! You have one more reason to encourage your “too skinny” grandchildren to eat the buraczki, borscht and holubtsi!) Other food sources include fish, beans and dairy.

Glutamine supplementation and dose
Typically, the consumption of any solo amino acid in high doses may hinder the assimilation of other amino acids. High doses of single amino acids can also result in bloating and diarrhea since they have osmotic properties. Yet glutamine supplements appear to be absorbed adequately and don’t create GI distress.
Glutamine supplementation has become routine to promote gut health in those with GI disorders, or those with HIV/AIDS, cancer, and other severe illnesses. Because glutamine has a rapid turnover rate, even high amounts (up to 30 grams each day) can be given without side effects. Most people will have a normalized plasma glutamine concentration by adding 20-25 grams over a 24 hour period.
In studies, glutamine supplement dosages have varied, including:
- 18 to 30 grams per day, by mouth
- 10 grams three times per day, by mouth
- 0.6 grams per kg of body weight per day (thus a 100 kg/220 lb person would consume 60 g daily)
- 14 grams of glutamine per day in combination with arginine and HMB for up to 24 weeks
Glutamine side effects and long-term use
There is little data regarding long-term usage (more than a few weeks) of glutamine supplements. No reported adverse effects have been attributed to short-term supplementation at less than 30 grams per day. Still, in some studies using high-dose intravenous administration of glutamine, patients developed elevated liver enzymes (indicating liver stress).
Other groups at risk:
- Those with diabetes should use caution when supplementing with glutamine because they tend to metabolize glutamine abnormally.
- Those who are sensitive to MSG (monosodium glutamate) may want to avoid glutamine supplements, due to glutamate inter-conversion.
- Those with epilepsy or bipolar disorder should be extremely cautious if considering glutamine and discuss it with their doctor first. Many anti-seizure medications work to block glutamate stimulation in the brain. And since the body metabolizes glutamine to glutamate, glutamine may interact negatively with anti-seizure medication.
Summary
Will it harm you in doses of less than 30 grams per day? Probably not.
If all of your bases are covered with nutrition, exercise and recovery, and you have the money to spend each month on more supplements, then adding glutamine is good. If you are undergoing a period of food restriction, then glutamine supplementation may improve nitrogen retention, decrease infection, and promote recovery from illness. Other situations that may benefit from glutamine supplementation include GI disorders, HIV/AIDS, and cancer.
Extra credit
Glutamine is a precursor for arginine.
A supplement blend containing glutamine has been shown to lower body fat, increase muscle mass, and increase strength when combined with 12 weeks of resistance training.
References
Wernerman J. Clinical use of glutamine supplementation. J Nutr 2008;138:2040S-2044S.
Choi SH et al. Glutamine on the luminal microbial environment after massive small bowel resection. J Korean Med Sci 2002;17:778-783.
Darmaun D. Role of glutamine depletion in severe illness. Diabetes Nutr Metab 2000;13:25-30.
Goodman MJ, et al. Abnormalities in the apparently normal bowel mucosa in Crohn’s disease. Lancet 1976;7:275-278.
Bertolo RF & Burrin DG. Comparative aspects of tissue glutamine and proline metabolism. J Nutr 2008;138:2032S-2039S.
Roth E. Nonnutritive effects of glutamine. J Nutr 2008;138:2025S-2031S.
Carvalho-Peixoto J, et al. Glutamine and carbohydrate supplements reduce ammonemia increase during endurance field exercise. Appl Physiol Nutr Metab 2007;32:1186-1190.
Groff JL, Gropper SS, Hunt SM. Advanced Nutrition and Human Metabolism. West Publishing Company, New York, 1995.
Institute of Medicine. The Role of Protein and Amino Acids in Sustaining and Enhancing Performance. National Academy Press: Washington DC, 1999.
Mack G. Glutamine synthetase isoenzymes, oligomers and subunits from hairy roots of Beta Vulgaris L. var. lutea. Planta 1998;205:113-20.
DiPasquale M. Amino Acids and Proteins for the Athlete: The Anabolic Edge. CRC Press: Boca Raton, FL, 1997.
Lohaus G. & Moellers C. Phloem transport of amino acids in two Brassica napus L. genotypes and one B. carinata genotype in relation to their seed protein content. Planta 2000;211:833-840.
Ziegler TR, et al. Glutamine and the gastrointestinal tract. Curr Opin Clin Nutr Metab Care 2000;3:355-362.
Ochs G. Complexity and expression of the glutamine synthetase multigene family in the amphidiploid crop Brassica napus. Plant Mol Biol 1999;39:395-405.
Labow BI & Souba WW. Glutamine. World J Surg 2000;24:1503-1513.
Gleeson M. Dosing and efficacy of glutamine supplementation in human exercise and sport training. J Nutr 2008;138:2045S-2049S.
Lininger SW, et al. A-Z guide to drug-herb-vitamin interactions. Prima Health, Rocklin, CA, 2000.
Mahan K, Escott-Stump S. Krause’s Food, Nutrition, and Diet Therapy. WB Saunders Company; Philadelphia, 2004.
Iwashita S, et al. Impact of glutamine supplementation on glucose homeostasis during and after exercise. J Appl Physiol 2005;99:1858-1865.
Scarpignato C, Pelosini I. Management of irritable bowel syndrome: novel approaches to the pharmacology of gut motility. Can J Gastroenterol 1999;13 Supp A:50A-65A.
Medina MA. Glutamine and cancer. J Nutr 2001;131:2539S-2542S.
Mithieux G. New data and concepts on glutamine and glucose metabolism in the gut. Curr Opin Clin Nutr Metab Care 2001;4:267-271.
Noyer CM, et al. A double-blind placebo-controlled pilot study of glutamine therapy for abnormal intestintal permeability in patients with AIDS. Am J Gastroenterol 1998;93:972–975.
Shabert JK, Wilmore DW. Glutamine deficiency as a cause of human immunodeficiency virus wasting. Med Hypotheses 1996;46:252–256.
Reeds PJ, Burrin DG. Glutamine and the bowel. J Nutr 2001;131:2505S-2508S.
Melis GC, et al. Glutamine: recent developments in research on the clinical significance of glutamine. Curr Opin Clin Nutr Metab Care 2004;7:59-70.
Vardimon L. Neuroprotection by glutamine synthetase. Isr Med Assoc J 2000;2 Supp:46-51.
Kraemer WJ, et al. Effects of amino acids supplement on physiological adaptations to resistance training. Med Sci Sports Exerc 2009 Apr 3 [Epub ahead of print]
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Ligthart-Melis GC, et al. Glutamine is an important precursor for de novo synthesis of arginine in humans. Am J Clin Nutr 2008;87:1282-1289.
