Glutamine, Worthless For Recovery, Worthless For Immune System, Worthless for Supplementation
Glutamine serves as a gluconeogenic precursor when muscle glycogen is depleted by approximately 90%; however, resistance training typically produces approximately 40% depletion in muscle glycogen, which may not be severe enough to benefit from glutamine supplementation. Than again, 99.9% of the human population will never reach a state where it is necessitated. There is a vast amount of data to prove and conclude its ineffectiveness.
With the exception of supplemental glutamine's beneficial role in gastrointestinal disorders (and general gut health), sepsis, and for the recovery from trauma and or surgery.... there's not much sense in administering a product that is very much limited in it's availability for physiological uptake, due to the fact that it's endogenous levels (prior to supplementation) are double the concentration of any other amino acid within the human body (1). Additionally, free form glutamine is unstable in solution at physiological pH.
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Facts and fallacies of purported ergogenic amino acid supplements.
Williams MH.
Department of Exercise Science, Physical Education, and Recreation, Old Dominion University, Norfolk, Virginia, USA. mwilliam@odu.edu
Although current research suggests that individuals involved in either high-intensity resistance or endurance exercise may have an increased need for dietary protein, the available research is either equivocal or negative relative to the ergogenic effects of supplementation with individual amino acids. Although some research suggests that the induction of hyperaminoacidemia via intravenous infusion of a balanced amino acid mixture may induce an increased muscle protein synthesis after exercise, no data support the finding that oral supplementation with amino acids, in contrast to dietary protein, as the source of amino acids is more effective. Some well-controlled studies suggest that aspartate salt supplementation may enhance endurance performance, but other studies do not, meriting additional research. Current data, including results for several well-controlled studies, indicated that supplementation with arginine, ornithine, or lysine, either separately or in combination, does not enhance the effect of exercise stimulation on either hGH or various measures of muscular strength or power in experienced weightlifters. Plasma levels of BCAA and tryptophan may play important roles in the cause of central fatigue during exercise, but the effects of BCAA or tryptophan supplementation do not seem to be effective ergogenics for endurance exercise performance, particularly when compared with carbohydrate supplementation, a more natural choice. Although glutamine supplementation may increase plasma glutamine levels, its effect on enhancement of the immune system and prevention of adverse effects of the overtraining syndrome are equivocal. Glycine, a precursor for creatine, does not seem to possess the ergogenic potential of creatine supplementation. Research with metabolic by-products of amino acid metabolism is in its infancy, and current research findings are equivocal relative to ergogenic applications. In general, physically active individuals are advised to obtain necessary amino acids through consumption of natural, high-quality protein foods.
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Glutamine: commercially essential or conditionally essential? A critical appraisal of the human data.
Am J Clin Nutr. 2001 Jul;74(1):25-32. Buchman AL.
Division of Gastroenterology and Hepatology, Northwestern University, Chicago, IL 60611, USA. a-buchman@nwu.edu
Glutamine is a nonessential amino acid that can be synthesized from glutamate and glutamic acid by glutamate-ammonia ligase. Glutamine is an important fuel source for the small intestine. It was proposed that glutamine is necessary for the maintenance of normal intestinal morphology and function in the absence of luminal nutrients. However, intestinal morphologic and functional changes related to enteral fasting and parenteral nutrition are less significant in humans than in animal models and may not be clinically significant. Therefore, it is unclear whether glutamine is necessary for the preservation of normal intestinal morphology and function in humans during parenteral nutrition. It was suggested that both glutamine-supplemented parenteral nutrition and enteral diets may pre-vent bacterial translocation via the preservation and augmentation of small bowel villus morphology, intestinal permeability, and intestinal immune function. However, it is unclear whether clinically relevant bacterial translocation even occurs in humans, much less whether there is any value in the prevention of such occurrences. Results of the therapeutic use of glutamine in humans at nonphysiologic doses indicate limited efficacy. Although glutamine is generally recognized to be safe on the basis of relatively small studies, side effects in patients receiving home parenteral nutrition and in those with liver-function abnormalities have been described. Therefore, on the basis of currently available clinical data, it is inappropriate to recommend glutamine for therapeutic use in any condition.
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Effect of glutamine supplementation combined with resistance training in young adults.
Candow DG, Chilibeck PD, Burke DG, Davison KS, Smith-Palmer T.
College of Kinesiology, University of Saskatchewan, Saskatoon, Canada.
The purpose of this study was to assess the effect of oral glutamine supplementation combined with resistance training in young adults. A group of 31 subjects, aged 18-24 years, were randomly allocated to groups (double blind) to receive either glutamine (0.9 g x kg lean tissue mass(-1) x day(-1); n = 17) or a placebo (0.9 g maltodextrin x kg lean tissue mass(-1) x day(-1); n = 14 during 6 weeks of total body resistance training. Exercises were performed for four to five sets of 6-12 repetitions at intensities ranging from 60% to 90% 1 repetition maximum (1 RM). Before and after training, measurements were taken of 1 RM squat and bench press strength, peak knee extension torque (using an isokinetic dynamometer), lean tissue mass (dual energy X-ray absorptiometry) and muscle protein degradation (urinary 3-methylhistidine by high performance liquid chromatography). Repeated measures ANOVA showed that strength, torque, lean tissue mass and 3-methylhistidine increased with training (P < 0.05), with no significant difference between groups. Both groups increased their 1 RM squat by approximately 30% and 1 RM bench press by approximately 14%. The glutamine group showed increases of 6% for knee extension torque, 2% for lean tissue mass and 41% for urinary levels of 3-methylhistidine. The placebo group increased knee extension torque by 5%, lean tissue mass by 1.7% and 3-methylhistidine by 56%. We conclude that glutamine supplementation during resistance training has no significant effect on muscle performance, body composition or muscle protein degradation in young healthy adults.
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Exercise-induced immunodepression- plasma glutamine is not the link.
Hiscock N, Pedersen BK.
Copenhagen Muscle Research Centre and Department of Infectious Diseases, Rigshospitalet, University of Copenhagen, DK-2100 Copenhagen, Denmark.
The amino acid glutamine is known to be important for the function of some immune cells in vitro. It has been proposed that the decrease in plasma glutamine concentration in relation to catabolic conditions, including prolonged, exhaustive exercise, results in a lack of glutamine for these cells and may be responsible for the transient immunodepression commonly observed after acute, exhaustive exercise. It has been unclear, however, whether the magnitude of the observed decrease in plasma glutamine concentration would be great enough to compromise the function of immune cells. In fact, intracellular glutamine concentration may not be compromised when plasma levels are decreased postexercise. In addition, a number of recent intervention studies with glutamine feeding demonstrate that, although the plasma concentration of glutamine is kept constant during and after acute, strenuous exercise, glutamine supplementation does not abolish the postexercise decrease in in vitro cellular immunity, including low lymphocyte number, impaired lymphocyte proliferation, impaired natural killer and lymphokine-activated killer cell activity, as well as low production rate and concentration of salivary IgA. It is concluded that, although the glutamine hypothesis may explain immunodepression related to other stressful conditions such as trauma and burn, plasma glutamine concentration is not likely to play a mechanistic role in exercise-induced immunodepression.
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Addition of glutamine to essential amino acids and carbohydrate does not enhance anabolism in young human males following exercise.
Wilkinson SB, Kim PL, Armstrong D, Phillips SM.
Exercise Metabolism Research Group, Department of Kinesiology, McMaster University, 1280 Main St. West, Hamilton, ON L8S 4K1, Canada.
We examined the effect of a post-exercise oral carbohydrate (CHO, 1 g.kg(-1).h(-1)) and essential amino acid (EAA, 9.25 g) solution containing glutamine (0.3 g/kg BW; GLN trial) versus an isoenergetic CHO-EAA solution without glutamine (control, CON trial) on muscle glycogen resynthesis and whole-body protein turnover following 90 min of cycling at 65% VO2 peak. Over the course of 3 h of recovery, muscle biopsies were taken to measure glycogen resynthesis and mixed muscle protein synthesis (MPS), by incorporation of [ring-2H5] phenylalanine. Infusion of [1-13C] leucine was used to measure whole-body protein turnover. Exercise resulted in a significant decrease in muscle glycogen (p < 0.05) with similar declines in each trial. Glycogen resynthesis following 3 h of recovery indicated no difference in total accumulation or rate of repletion. Leucine oxidation increased 2.5 fold (p < 0.05) during exercise, returned to resting levels immediately post-exercise,and was again elevated at 3 h post-exercise (p < 0.05). Leucine flux, an index of whole-body protein breakdown rate, was reduced during exercise, but increased to resting levels immediately post-exercise, and was further increased at 3 h post-exercise (p < 0.05), but only during the CON trial. Exercise resulted in a marked suppression of whole-body protein synthesis (50% of rest; p < 0.05), which was restored post-exercise; however, the addition of glutamine did not affect whole-body protein synthesis post-exercise. The rate of MPS was not different between trials. The addition of glutamine to a CHO + EAA beverage had no effect on post-exercise muscle glycogen resynthesis or muscle protein synthesis, but may suppress a rise in whole-body proteolysis during the later stages of recovery.
PMID: 17111006 [PubMed - indexed for MEDLINE]
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Amino acids and endurance exercise.
Hargreaves MH, Snow R.
School of Health Sciences, Deakin University, Burwood, 3125, Australia.
Although skeletal muscle is capable of oxidizing selected amino acids, exercise in the fed and carbohydrate-replete condition results in only a small increase in amino acid utilization. Nevertheless, it may be important to increase the dietary protein requirements of active individuals. There is ongoing debate as to whether the amino acids for oxidation are derived from the free amino acid pool, from net protein breakdown, or a combination of both. There has been interest in the potential ergogenic benefits of amino acid ingestion; however, BCAA ingestion does not appear to affect fatigue during prolonged exercise, there is little support from controlled studies to recommend glutamine ingestion for enhanced immune function, and although glutamine stimulates muscle glycogen synthesis, its addition to carbohydrate supplements provides no additional benefit over ingestion of carbohydrate alone.
PMID: 11255141 [PubMed - indexed for MEDLINE]
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The Effects of High-Dose Glutamine Ingestion on Weightlifting Performance
JOSE ANTONIO1, 3, MICHAEL S. SANDERS1, DOUGLAS KALMAN2, DEREK WOODGATE1, and CHRIS STREET1
1. Sports Science Laboratory, University of Delaware, Newark, Delaware 19716, 2. Peak Wellness, Greenwich, Connecticut 06830, 3. Address correspondence to Jose Antonio, Scientific Affairs Department, Nutricia, 6111 Broken Sound Parkway NW, Boca Raton, FL 33487
The purpose of this study was to determine if high-dose glutamine ingestion affected weightlifting performance. In a double-blind, placebo-controlled, crossover study, 6 resistance-trained men (mean ? SE: age, 21.5 ? 0.3 years; weight, 76.5 ? 2.8 kg−1) performed weightlifting exercises after the ingestion of glutamine or glycine (0.3 g?kg−1) mixed with calorie-free fruit juice or placebo (calorie-free fruit juice only). Each subject underwent each of the 3 treatments in a randomized order. One hour after ingestion, subjects performed 4 total sets of exercise to momentary muscular failure (2 sets of leg presses at 200% of body weight, 2 sets of bench presses at 100% of body weight). There were no differences in the average number of maximal repetitions performed in the leg press or bench press exercises among the 3 groups. These data indicate that the short-term ingestion of glutamine does not enhance weightlifting performance in resistance-trained men.
Reference Data:Antonio, J., M.S. Sanders, D. Kalman, D. Woodgate, and C. Street. The effects of high-dose glutamine ingestion on weightlifting performance.
Keywords: amino acid, supplement, nutrition, protein
DOI: 10.1519/1533-4287(2002)016[0157:TEOHDG]2.0.CO;2
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Clin Nutr. 1996 Oct ;15 (5):267-73 16844055
Effect of a short-term infusion of glutamine on muscle protein metabolism postoperatively.
[My paper] A Januszkiewicz , P Ess?n , M A McNurlan , G A Calder , K Andersson , J Wernerman , P J Garlick
The acute effect of a short-term postoperative infusion of glucose supplemented withglutamine (0.285 g/kg body weight), on muscle protein metabolism, was studied by analyses of free amino acid concentrations and determinations of protein synthesis. A glutamine-glucose infusion was given for 5.5 h to 6 patients 2-3 days after elective surgery for colon cancer. The free glutamine concentration was 5.72 +/- 0.96 mmol/kg wet weight (ww) before and 6.14 +/- 1.10 mmol/kg ww 4 h after the glutamine infusion. The rate of protein synthesis was 1.26 +/- 0.15%/24 h before the infusion and 1.12 +/- 0.16%/24 h during its latter part. The percentage of polyribosomes was 42.2 +/- 3.4% before and 40.9 +/- 1.3% after the infusion. The results showed no difference in these biochemical parameters, indicating that a short-term infusion of glutamine given postoperatively is insufficient to affect protein metabolism in human skeletal muscle.