Summary of Glutamine
Primary Information, Benefits, Effects, and Important Facts
Glutamine is one of the 20 naturally occurring amino acids in dietary protein, specifically it is a conditionally essential amino acid (being elevated to essential during periods of disease and muscle wasting typical of physical trauma). It is sold as an isolated amino acids as well as being found in high levels in dietary meats and eggs. It is found in very high levels in both whey and casein protein.
Glutamine is a very effective intestinal and immune system health compound, as these cells use glutamine as the preferred fuel source rather than glucose.
It is generally touted as a muscle builder, but has not been proven to enhance muscle building in healthy individuals; only those suffering from physical trauma such as burns or muscular wounds (knife wounds) or in disease states in which muscle wasting occurs, such as AIDS. In these individuals, however, glutamine is effective at building muscle and alleviating a decrease in muscle mass typical of the ailment.
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Things To Know & Note
Glutamine is non-stimulatory
How to Take Glutamine
Recommended dosage, active amounts, other details
Supplementation of L-glutamine tends to be dosed at 5 g or above, with higher doses being advised against due to excessive ammonia in serum. The lowest dose found to increase ammonia in serum has been 0.75 g/kg, or approximately 51 g for a 150 lb individual.
Due to the relative inefficacy of glutamine supplementation for increasing muscle mass, the optimal dosage is not known. The above recommended doses are sufficient for intestinal health reasons and for attenuating a possible relative glutamine deficiency (seen in instances of low protein intake or veganism).
Frequently Asked Questions about Glutamine
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Human Effect Matrix
The Human Effect Matrix looks at human studies (it excludes animal and in vitro studies) to tell you what effects glutamine has on your body, and how strong these effects are.
|Grade||Level of Evidence [show legend]|
|Robust research conducted with repeated double-blind clinical trials|
|Multiple studies where at least two are double-blind and placebo controlled|
|Single double-blind study or multiple cohort studies|
|Uncontrolled or observational studies only|
Level of Evidence
? The amount of high quality evidence. The more evidence, the more we can trust the results.
Magnitude of effect
? The direction and size of the supplement's impact on each outcome. Some supplements can have an increasing effect, others have a decreasing effect, and others have no effect.
Consistency of research results
? Scientific research does not always agree. HIGH or VERY HIGH means that most of the scientific research agrees.
|Low See all 3 studies|
|Minor||Very High See 2 studies|
|Minor||- See study|
|Minor||Moderate See 2 studies|
|Minor||- See study|
|Minor||Very High See 2 studies|
|Minor||- See study|
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|Minor||Low See all 3 studies|
Studies Excluded from Consideration
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Scientific Research on Glutamine
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White Rice at 11.1% protein
Corn at 16.2% protein
Tofu at 9.1% protein
Eggs at 4.3% protein
Average dietary intake of glutamine, according to the Nurse's Study of 70,356 women, is around 6.85+/-2.19 g glutamine daily.
It should be noted that the above percentages are based on total protein content, and not total caloric content nor weight. If assessed by weight, beef protein has 1.23g of glutamine per 100g product whereas skim milk has 0.28g glutamine per 100g product.
It is also noted that some of these levels of glutamine may be underreported, and subsequently levels of glutamate higher than expected; this is due to one of the historically used methods of amino acid analysis, hydrolysis, inducing conversion of glutamine to glutamate or pyroglutamic acid. The sequencing study cited above demonstrates the higher range of values, and it's methods are described here. Comparing results between conventional methods and gene sequencing can yield differences of up to 4% in total amino acids (influence on glutamine would be dependent on glutamine content of food).
Glutamine analysis hasn't been too accurate in the past for exact numbers (due to degradation and conversion of glutamine) but the general trend of meat and dairy being the best dietary sources of glutamine exists. Interestingly, some plant sources have a higher glutamine content on a percentage basis, but they are not the best sources of dietary glutamine due to the low overall amount of protein from plant sources relative to meat and dairy sources
Glutamine is one of the conditionally essential amino acids, with the standard amino acid backbone and a 3-carbon side-chain with a ketone group on the furthest carbon from the amine group and culminating with a nitrogen on the end of the side-chain.
Glutamine is not highly soluble in an aqueous environment, and thus when used in intravenous infusion it tends to be bound to the amino acid Alanine as Alanyl-glutamine.
It is the most abundant amino acid in human tissue (mostly muscle tissue) and plasma. It has various biological roles including acting as a nitrogen transport between tissues alongside alanine, acting as a precursor for the antioxidant glutathione, acting as a precursor for nucleotides, regulating acid/base metabolism and being involved as a substrate in gluconeogenesis. It can also stimulate production of L-citrulline and L-glycine via acting as substrate.
Plasma levels in healthy humans are typically 500-750 umol/L after a morning fast. Muscle concentrations are typically regulated at 20umol/kg wet weight and release 50 umol/L into plasma per hour in a fed state. This is due to muscle being a prime location for glutamine synthesis via the enzyme glutamine synthetase. These plasma levels are typically reduced in periods of critical illness due to increased usage of glutamine as substrate in various metabolic processes.
Up to 13% of circulating glutamine tends to be redirected to the splanchnic bed to be used as energy substrate by the liver and intestinal enterocytes.
The amount of glutamine devoted to intestinal and hepatic tissue (splanchic extraction) does not differ between food-bound sources and supplemental dosages.
Ischemia/reperfusion (I/R) is an injury to tissue caused by a restriction of oxygen availability (ischemia) followed by an excessive feed of oxygen to the tissue which causes large amounts of oxidative damage (reperfusion). Glutamine appears to, in vitro, be protective against I/R in cardiac tissue and this has been replicated in rats given glutamine injections either 18 hours before damage or an infusion for the immediate four hours preceding damage.
This protection is thought to be associated with enhanced cardiac glutathione concentrations (a deficiency of which exacerbates damage) or the induction of heat shock proteins, particularly HSP70.
Glutamine appears to reduce the damage associated with ischemia/reperfusion injury in cardiac cells, which may be associated with enhancing antioxidant and heat shock protein defenses
When given to humans around the time of surgery associated with I/R injury (cardiopulmonary bypass), supplementation of 500 mg/kg glutamine (as alanyl-glutamine) for three days prior to surgery is associated with less clinical and biochemical indicators of damage in three days of followup which has been previously seen with IV administration of 400 mg/kg glutamine (as Dipeptiven).
In persons with chronic stable angina a single oral dose of 80 mg/kg glutamine is able to enhance physical performance as assessed by a Bruce test, suggestive of protective effects.
Supplementation of glutamine to persons with cardiac impairments or around the time of cardiac surgery has been shown to be cardioprotective, and this has been confirmed with oral supplementation. It is not sure how this information applies to otherwise healthy individuals
Glutamine has been shown to be able to 'blunt' the blood glucose spikes in response to dietary carbohydrate, attenuating rises and Cmax values of blood glucose and insulin in response to dietary carbohydrate ingestion. When investigated as to whether this is due to non-significant delays in gastric emptying, it does not appear to be the case.
Glutamine is known to be the main energy substrate used by the immune cells called leukocytes and contributes to the proliferation of these cells, the reason for glutamine being the fuel substrate for leukocytes is the need for a quicker energy source than glucose (similar to intestinal mucosa and bone marrow). Leukocytes cannot synthesize glutamine on their own, and thus are reliant on glutamine provided from other tissues that possess the glutamine synthetase enzyme, or from dietary intake.
Leukocyte growth rates are highest at a concentration of approximately 600 umol/L, a concentration well within normal human physiology. For this reason glutamine and it's supplemental usage tends to be practically limited to times where synthesis or intake is suppressed or redirected, such as critical illness or prolonged cardiovascular exercise.
Glutamine is an amino acid intimately linked in vitro with muscle homeostasis and muscle protein synthesis, in which a surplus causes anabolism and prevents breakdown while a deficit causes catabolism. This correlation has been seen in vivo when glutamine is infused (some counter evidence) and appears to be specific for glutamine.
When looking at cellular cultures and isolated cells, glutamine appears to dose-dependently increase muscle protein synthesis. When glutamine is increased in the blood via injections, this relationship is still observed
Studies using glutamine in otherwise healthy persons and investigating either muscle protein synthesis or lean mass gains have noted a failure with 900 mg/kg lean mass (placbo being 900mg/kg maltodextrin) in youth paired with resistance training.
The addition of glutamine to creatine or extra glutamine (300 mg/kg bodyweight) to a protein and carbohydrate shake or amino acid and carbohydrate shake have also failed to outperform the supplements ingested without glutamine, suggesting no role as a synergistic.
In studies of otherwise healthy humans given glutamine supplementation, it does not appear to enhance the rates of muscle protein synthesis
Plasma glutamine levels are either increased or unchanged in short term, high intensity activities and tend to be unchanged with eccentric muscle damage suggesting that extra glutamine supplementation will not benefit short term intensity exercise or weightlifting by any means which act through serum glutamine levels (such as immunosuppression or catabolism).
In contrast to this, endurance events exceeding 2 hours do tend to show decreases in serum glutamine levels. Both supplementation of glutamine and increasing protein intake from food (in the dose of 20-30g animal source protein) can alleviate this decline in serum glutamine and potentially can reduce damage to immune cells associated with prolonged cardiovascular exercise. This decrease in serum glutamine levels may also suppress release of interleukin-6 (IL-6) from muscle tissue, and supplementation of glutamine can preserve IL-6 levels.
Supplementation with glutamine during longer duration cardiovascular exercise, via decreasing ammonia, has also been noted to increase performance. The decrease in ammonia per se is also seen as desirable.
An oral load of 2 g glutamine has been shown to increase plasma bicarbonate levels in vivo. This has been shown to not affect high intensity exercise to any noticeable degree, whether it aids in endurance events or not is not known.
By attenuating or otherwise preventing glutamine depletion in exericse lasting for more than one hour, performance may indirectly increase relative to the glutamine depleted state. This is not so much performance 'enhancement' as it is performance 'preservation'
Glutamine ingestion, at 0.5 g/kg daily, has been shown in a small study on hypercortisolemic patients (induced be prednisone at a dose to induce muscle protein breakdown) noted less of a catabolic state via reducing essential amino acid conversion into glutamine, and less of a leucine expenditure.
There is some evidence that oral glutamine can increase glycogen replishment rates when consumed alongside carbohydrates but more studies are needed to see whether this method holds benefit over food sources of glutamine or holds true with higher carbohydrate intakes.
Glutamine itself, in the absence of carbohydrates, may enhance muscle glycogen stores.
Glutamine supplementation has been shown to stimulate protein synthesis in the gut of healthy humans to a similar potency as mixed amino acids.
Glutamine is investigated to aiding a 'leaky gut' as it is a regulator of intestinal tight junction barriers. Intentional depletion of intracellular glutamine and inhibition of glutamine synthesis in vitro leads to rapid increases in gut permeability. In the absence of dietary glutamine, de novo synthesis via glutamine synthetase is the main source of glutamine.
Glutamine has been implicated in also alleviating the increased permeability done to the gut by acetaldehyde, the metabolite of alcohol as well as chemotherapy and radiation therapy. Glutamine can alleviate the increase in permeability associated with sepsis in vivo, but not prevent it.
In an intervention study on preterm infants, it was demonstrated that glutamine supplementation at 0.3g/kg could aid in intestinal integrity and reduce the occurrence of septicemia and increase recovery; and these results have been replicated with both positive and negative results.
A study with 15g oral glutamine on critically ill patients did not find significant decreases in intestinal permeability.
At least one study has shown glutamine, in adults, to confer protection from adverse chemotherapy induced changes in intestinal permeability.
Crohn's disease is a disease characterized by increased intestinal permeability as well as an inflammatory response in the intestinal membrane.
One study using 21g oral glutamine daily in a small sample size noted that glutamine was not effective in reducing intestinal permeability associated with Crohn's Disease. A response to this study concurred with reports of a study done on children with Crohn's having the same results and hypothesized that the benefits of glutamine on the intestinal wall could be getting negated by glutamine enhancing T-cell and Nitric Oxide function, of which are adverse pathology associated with Crohn's disease. These results are supported by one study using intravenous glutamine at 0.3 g/kg finding no apparent benefit.
In contrast to the null effects, a more recent study found improvements in intestinal permeability associated with both glutamine and the active control of whey protein, both at 0.5 g/kg bodyweight daily for 2 months, and one intravenous study has noted improvements in intestinal permeability. It is hypothesized that this may be due to the higher dosage of glutamine used.
In the critically ill (hospitalized) glutamine has an elevated importance. Demand for glutamine is increased in the kidneys, immune cells, and the intestinal mucosa during these periods in response to cachexia, infection, and trauma. It is common, however, for glutamine need during these states to exceed the capacity of skeletal muscle to synthesis glutamine; this results in a reduction of the free (intra-cellular) glutamine pool in the body. With this reduction in glutamine comes a reduction in protein economy and alterations in metabolism (increase in protein catabolism, decreased levels of enzymes and hormones using glutamine as a building block). Due to these reasons, one of the main interventions for glutamine is rehabilitative and in response to sickness rather than merely preventative.
Due to the ubiquitous nature of glutamine in the body, bodily stores of glutamine are depleted in an attempt to counter the increased metabolic activity typical of critical illness. Since skeletal muscle is largely glutamine it is at a higher risk for catabolism during periods of illness. Supplementing with glutamine in the critically ill alleviates the decline in muscle mass significantly, although it does not necessarily prolong life or survivial outcomes.
Glutathione, an important endogenous anti-oxidant that is created from glutamine, also is decreased in situations of critical illness and trauma. As provision of glutamine becomes the rate-limiting step, administration of 0.5 g/kg bodyweight glutamine intravenously increases glutathione levels in this population.
The Observed Safety Limit of glutamine supplementation, of which is the highest amount one can take and be assured of no side effects, has been suggested as being 14g/d in supplemental form (above food intake). Higher levels than this have been tested and well tolerated, but there is not enough evidence to suggest that higher doses are completely free from harm over a lifetime of supplementation nor enough evidence to assume harm exists. Limited evidence suggests that 50-60g for a period of a few weeks is not associated with significant adverse effects.
Acutely, doses of around 0.75g/kg bodyweight have been implicated in increasing plasma ammonia levels above the tolerated safety limit. A study in elderly persons (69+/-8.8 years) with 0.5g/kg oral glutamine has shown no effects on plasma ammonia levels, but was associated with an increase in serum urea and creatinine that was deemed not clinically relevant. A transient decrease in the kidney's glomerular filtration rate was seen.
- Lehmkuhl M, et al. The effects of 8 weeks of creatine monohydrate and glutamine supplementation on body composition and performance measures. J Strength Cond Res. (2003)
- Wilkinson SB, et al. Addition of glutamine to essential amino acids and carbohydrate does not enhance anabolism in young human males following exercise. Appl Physiol Nutr Metab. (2006)
- Lenders CM, et al. Evaluation of a novel food composition database that includes glutamine and other amino acids derived from gene sequencing data. Eur J Clin Nutr. (2009)
- Amino Acid Analysis (AAARG).
- Quantitative Analyses of Glutamine in Peptides and Proteins.
- Baxter JH, et al. Glutamine in commercial liquid nutritional products. J Agric Food Chem. (2004)
- Swails WS, et al. Glutamine content of whole proteins: implications for enteral formulas. Nutr Clin Pract. (1992)
- Alanyl-glutamine counteracts the depletion of free glutamine and the postoperative decline in protein synthesis in skeletal muscle.
- Lacey JM, Wilmore DW. Is glutamine a conditionally essential amino acid. Nutr Rev. (1990)
- Is Glutamine a Conditionally Essential Amino Acid?.
- Gleeson M. Dosing and efficacy of glutamine supplementation in human exercise and sport training. J Nutr. (2008)
- Fujita T, Yanaga K. Association between glutamine extraction and release of citrulline and glycine by the human small intestine. Life Sci. (2007)
- Lightfoot A, McArdle A, Griffiths RD. Muscle in defense. Crit Care Med. (2009)
- Souba WW. Glutamine: a key substrate for the splanchnic bed. Annu Rev Nutr. (1991)
- Response of glutamine metabolism to exogenous glutamine in humans.
- Effect of glutamine on leucine metabolism in humans.
- Boza JJ, et al. Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers. Am J Physiol Gastrointest Liver Physiol. (2001)
- Khogali SE, et al. Is glutamine beneficial in ischemic heart disease. Nutrition. (2002)
- Wischmeyer PE, et al. Glutamine preserves cardiomyocyte viability and enhances recovery of contractile function after ischemia-reperfusion injury. JPEN J Parenter Enteral Nutr. (2003)
- Wischmeyer PE, et al. Single dose of glutamine enhances myocardial tissue metabolism, glutathione content, and improves myocardial function after ischemia-reperfusion injury. JPEN J Parenter Enteral Nutr. (2003)
- Bolotin G, et al. Glutamine improves myocardial function following ischemia-reperfusion injury. Asian Cardiovasc Thorac Ann. (2007)
- Leichtweis S, Ji LL. Glutathione deficiency intensifies ischaemia-reperfusion induced cardiac dysfunction and oxidative stress. Acta Physiol Scand. (2001)
- Wischmeyer PE. Glutamine: the first clinically relevant pharmacological regulator of heat shock protein expression. Curr Opin Clin Nutr Metab Care. (2006)
- Domanski MJ, et al. Association of myocardial enzyme elevation and survival following coronary artery bypass graft surgery. JAMA. (2011)
- Sufit A, et al. Pharmacologically dosed oral glutamine reduces myocardial injury in patients undergoing cardiac surgery: a randomized pilot feasibility trial. JPEN J Parenter Enteral Nutr. (2012)
- Lomivorotov VV, et al. Glutamine is cardioprotective in patients with ischemic heart disease following cardiopulmonary bypass. Heart Surg Forum. (2011)
- Awad S, et al. A randomized cross-over study of the metabolic and hormonal responses following two preoperative conditioning drinks. Nutrition. (2011)
- Ardawi MS, Newsholme EA. Glutamine metabolism in lymphocytes of the rat. Biochem J. (1983)
- Parry-Billings M, et al. Does glutamine contribute to immunosuppression after major burns. Lancet. (1990)
- Kim H. Glutamine as an immunonutrient. Yonsei Med J. (2011)
- MacLennan PA, et al. Inhibition of protein breakdown by glutamine in perfused rat skeletal muscle. FEBS Lett. (1988)
- MacLennan PA, Brown RA, Rennie MJ. A positive relationship between protein synthetic rate and intracellular glutamine concentration in perfused rat skeletal muscle. FEBS Lett. (1987)
- Zhou X, Thompson JR. Regulation of protein turnover by glutamine in heat-shocked skeletal myotubes. Biochim Biophys Acta. (1997)
- Millward DJ, Jepson MM, Omer A. Muscle glutamine concentration and protein turnover in vivo in malnutrition and in endotoxemia. Metabolism. (1989)
- Januszkiewicz A, et al. Effect of a short-term infusion of glutamine on muscle protein metabolism postoperatively. Clin Nutr. (1996)
- Wusteman M, Elia M. Effect of glutamine infusions on glutamine concentration and protein synthetic rate in rat muscle. JPEN J Parenter Enteral Nutr. (1991)
- Relationship between glutamine concentration and protein synthesis in rat skeletal muscle.
- Candow DG, et al. Effect of glutamine supplementation combined with resistance training in young adults. Eur J Appl Physiol. (2001)
- Robson PJ, et al. Effects of exercise intensity, duration and recovery on in vitro neutrophil function in male athletes. Int J Sports Med. (1999)
- Babij P, Matthews SM, Rennie MJ. Changes in blood ammonia, lactate and amino acids in relation to workload during bicycle ergometer exercise in man. Eur J Appl Physiol Occup Physiol. (1983)
- Gleeson M, et al. The effect of severe eccentric exercise-induced muscle damage on plasma elastase, glutamine and zinc concentrations. Eur J Appl Physiol Occup Physiol. (1998)
- Parry-Billings M, et al. Plasma amino acid concentrations in the overtraining syndrome: possible effects on the immune system. Med Sci Sports Exerc. (1992)
- Rennie MJ, et al. Effect of exercise on protein turnover in man. Clin Sci (Lond). (1981)
- Contrasting plasma free amino acid patterns in elite athletes: association with fatigue and infection.
- Cury-Boaventura MF, et al. Effects of exercise on leukocyte death: prevention by hydrolyzed whey protein enriched with glutamine dipeptide. Eur J Appl Physiol. (2008)
- Hiscock N, et al. Glutamine supplementation further enhances exercise-induced plasma IL-6. J Appl Physiol. (2003)
- Parry-Billings M, et al. A communicational link between skeletal muscle, brain, and cells of the immune system. Int J Sports Med. (1990)
- Antonio J, et al. The effects of high-dose glutamine ingestion on weightlifting performance. J Strength Cond Res. (2002)
- Carvalho-Peixoto J, Alves RC, Cameron LC. Glutamine and carbohydrate supplements reduce ammonemia increase during endurance field exercise. Appl Physiol Nutr Metab. (2007)
- Increased plasma bicarbonate and growth hormone after an oral glutamine load.
- Haub MD, et al. Acute L-glutamine ingestion does not improve maximal effort exercise. J Sports Med Phys Fitness. (1998)
- Claeyssens S, et al. Effect of enteral glutamine on leucine, phenylalanine and glutamine metabolism in hypercortisolemic subjects. Am J Physiol Endocrinol Metab. (2000)
- Effect of oral glutamine on whole body carbohydrate storage during recovery from exhaustive exercise.
- Bowtell JL, et al. Effect of oral glutamine on whole body carbohydrate storage during recovery from exhaustive exercise. J Appl Physiol. (1999)
- Coëffier M, et al. Enteral glutamine stimulates protein synthesis and decreases ubiquitin mRNA level in human gut mucosa. Am J Physiol Gastrointest Liver Physiol. (2003)
- Li N, et al. Glutamine regulates Caco-2 cell tight junction proteins. Am J Physiol Gastrointest Liver Physiol. (2004)
- Potsic B, et al. Glutamine supplementation and deprivation: effect on artificially reared rat small intestinal morphology. Pediatr Res. (2002)
- Glutamine and Barrier Function in Cultured Caco-2 Epithelial Cell Monolayers.
- Glutamine Synthetase: A Key Enzyme for Intestinal Epithelial Differentiation?.
- Seth A, et al. L-Glutamine ameliorates acetaldehyde-induced increase in paracellular permeability in Caco-2 cell monolayer. Am J Physiol Gastrointest Liver Physiol. (2004)
- Bai M, Jiang Z, Liu Y. Glutamine dipeptide attenuate mucosal atrophic changes and preservation of gut barrier function following 5-FU intervention. Zhonghua Wai Ke Za Zhi. (1996)
- Chun H, et al. Effect of enteral glutamine on intestinal permeability and bacterial translocation after abdominal radiation injury in rats. J Gastroenterol. (1997)
- Dugan ME, McBurney MI. Luminal glutamine perfusion alters endotoxin-related changes in ileal permeability of the piglet. JPEN J Parenter Enteral Nutr. (1995)
- Sevastiadou S, et al. The impact of oral glutamine supplementation on the intestinal permeability and incidence of necrotizing enterocolitis/septicemia in premature neonates. J Matern Fetal Neonatal Med. (2011)
- Lima NL, et al. Wasting and intestinal barrier function in children taking alanyl-glutamine-supplemented enteral formula. J Pediatr Gastroenterol Nutr. (2007)
- van den Berg A, et al. The effect of glutamine-enriched enteral nutrition on intestinal permeability in very-low-birth-weight infants: a randomized controlled trial. JPEN J Parenter Enteral Nutr. (2006)
- Luo M, et al. Metabolic effects of enteral versus parenteral alanyl-glutamine dipeptide administration in critically ill patients receiving enteral feeding: a pilot study. Clin Nutr. (2008)
- Li Y, et al. Oral glutamine ameliorates chemotherapy-induced changes of intestinal permeability and does not interfere with the antitumor effect of chemotherapy in patients with breast cancer: a prospective randomized trial. Tumori. (2006)
- Den Hond E, et al. Effect of long-term oral glutamine supplements on small intestinal permeability in patients with Crohn's disease. JPEN J Parenter Enteral Nutr. (1999)
- Akobeng AK, et al. Glutamine supplementation and intestinal permeability in Crohn's disease. JPEN J Parenter Enteral Nutr. (2000)
- Glutamine-supplemented total parenteral nutrition enhances T-lymphocyte response in surgical patients undergoing colorectal resection.
- Ockenga J, et al. Glutamine-enriched total parenteral nutrition in patients with inflammatory bowel disease. Eur J Clin Nutr. (2005)
- Benjamin J, et al. Glutamine and whey protein improve intestinal permeability and morphology in patients with Crohn's disease: a randomized controlled trial. Dig Dis Sci. (2012)
- van der Hulst RR, et al. Glutamine and the preservation of gut integrity. Lancet. (1993)
- Silva AC, et al. Efficacy of a glutamine-based oral rehydration solution on the electrolyte and water absorption in a rabbit model of secretory diarrhea induced by cholera toxin. J Pediatr Gastroenterol Nutr. (1998)
- Stinnett JD, et al. Plasma and skeletal muscle amino acids following severe burn injury in patients and experimental animals. Ann Surg. (1982)
- Griffiths RD. Outcome of critically ill patients after supplementation with glutamine. Nutrition. (1997)
- Neu J, Shenoy V, Chakrabarti R. Glutamine nutrition and metabolism: where do we go from here ?. FASEB J. (1996)
- Mittendorfer B, et al. Accelerated glutamine synthesis in critically ill patients cannot maintain normal intramuscular free glutamine concentration. JPEN J Parenter Enteral Nutr. (1999)
- Sacks GS. Effect of glutamine-supplemented parenteral nutrition on mortality in critically ill patients. Nutr Clin Pract. (2011)
- Eroglu A. The effect of intravenous alanyl-glutamine supplementation on plasma glutathione levels in intensive care unit trauma patients receiving enteral nutrition: the results of a randomized controlled trial. Anesth Analg. (2009)
- Fan YP, et al. Effects of glutamine supplementation on patients undergoing abdominal surgery. Chin Med Sci J. (2009)
- Shao A, Hathcock JN. Risk assessment for the amino acids taurine, L-glutamine and L-arginine. Regul Toxicol Pharmacol. (2008)
- Garlick PJ. Assessment of the safety of glutamine and other amino acids. J Nutr. (2001)
- Roth E. Nonnutritive effects of glutamine. J Nutr. (2008)
- Ward E, et al. Oral glutamine in paediatric oncology patients: a dose finding study. Eur J Clin Nutr. (2003)
- Galera SC, et al. The safety of oral use of L-glutamine in middle-aged and elderly individuals. Nutrition. (2010)
- Marwood S, et al. No effect of glutamine ingestion on indices of oxidative metabolism in stable COPD. Respir Physiol Neurobiol. (2011)
- Rotovnik Kozjek N, et al. Oral glutamine supplementation during preoperative radiochemotherapy in patients with rectal cancer: a randomised double blinded, placebo controlled pilot study. Clin Nutr. (2011)
- Marton S, et al. Effect of glutamine in patients with esophagus resection. Dis Esophagus. (2010)
- Bassini-Cameron A, et al. Glutamine protects against increases in blood ammonia in football players in an exercise intensity-dependent way. Br J Sports Med. (2008)
- Mok E, et al. Lack of functional benefit with glutamine versus placebo in Duchenne muscular dystrophy: a randomized crossover trial. PLoS One. (2009)
- Yalçin SS, et al. Effect of glutamine supplementation on lymphocyte subsets in children with acute diarrhea. Turk J Pediatr. (2010)
- Antonio J, Street C. Glutamine: a potentially useful supplement for athletes. Can J Appl Physiol. (1999)
- Finn KJ, Lund R, Rosene-Treadwell M. Glutamine Supplementation did not Benefit Athletes During Short-Term Weight Reduction. J Sports Sci Med. (2003)
- Ramezani Ahmadi A, et al. The effect of glutamine supplementation on athletic performance, body composition, and immune function: A systematic review and a meta-analysis of clinical trials. Clin Nutr. (2018)
- Bernfeld E, et al. Phospholipase D-Dependent mTORC1 Activation by Glutamine. Journal of Biological Chemistry. (2018)
- Street B, Byrne C, Eston R. Glutamine Supplementation in Recovery From Eccentric Exercise Attenuates Strength Loss and Muscle Soreness. Journal of Exercise Science and Fitness. (2011)
- Rahmani Nia F, et al. Effect of L-glutamine supplementation on electromyographic activity of the quadriceps muscle injured by eccentric exercise. Iran J Basic Med Sci. (2013)
- Waldron M, et al. The effects of acute leucine or leucine-glutamine co-ingestion on recovery from eccentrically biased exercise. Amino Acids. (2018)
- Legault Z, Bagnall N, Kimmerly DS. The Influence of Oral L-Glutamine Supplementation on Muscle Strength Recovery and Soreness Following Unilateral Knee Extension Eccentric Exercise. Int J Sport Nutr Exerc Metab. (2015)
- Li P, et al. Amino acids and immune function. Br J Nutr. (2007)
- Castell LM. Can glutamine modify the apparent immunodepression observed after prolonged, exhaustive exercise?. Nutrition. (2002)
- Castell LM, Poortmans JR, Newsholme EA. Does glutamine have a role in reducing infections in athletes?. Eur J Appl Physiol Occup Physiol. (1996)
- Krzywkowski K, et al. Effect of glutamine supplementation on exercise-induced changes in lymphocyte function. Am J Physiol Cell Physiol. (2001)
- Walsh NP, et al. Effect of oral glutamine supplementation on human neutrophil lipopolysaccharide-stimulated degranulation following prolonged exercise. Int J Sport Nutr Exerc Metab. (2000)
- Krzywkowski K, et al. Effect of glutamine and protein supplementation on exercise-induced decreases in salivary IgA. J Appl Physiol (1985). (2001)
- Hiscock N, Pedersen BK. Exercise-induced immunodepression- plasma glutamine is not the link. J Appl Physiol (1985). (2002)
- Dokladny K, Zuhl MN, Moseley PL. Intestinal epithelial barrier function and tight junction proteins with heat and exercise. J Appl Physiol (1985). (2016)
- Pugh JN, et al. Glutamine supplementation reduces markers of intestinal permeability during running in the heat in a dose-dependent manner. Eur J Appl Physiol. (2017)
- Zuhl M, et al. The effects of acute oral glutamine supplementation on exercise-induced gastrointestinal permeability and heat shock protein expression in peripheral blood mononuclear cells. Cell Stress Chaperones. (2015)