Who Wastes Money on Glutamine?

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  1. Who Wastes Money on Glutamine?


    Well this original thread came up missing So Im going to repost it


    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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    J Strength Cond Res 2002 Feb;16(1):157-60
    The effects of high-dose glutamine ingestion on weightlifting performance

    Antonio J, Sanders MS, Kalman D, Woodgate D, Street C.

    Sports Science Laboratory, University of Delaware, Newark, Delaware 19716, USA.

    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 x 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.

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    Int J Sports Med 2000 Jan;21(1):25-30 Related Articles, Links


    The effect of free glutamine and peptide ingestion on the rate of muscle glycogen resynthesis in man.

    van Hall G, Saris WH, van de Schoor PA, Wagenmakers AJ.

    Department of Human Biology, Maastricht University, The Netherlands. [email protected]

    The present study investigated previous claims that ingestion of glutamine and of protein-carbohydrate mixtures may increase the rate of glycogen resynthesis following intense exercise. Eight trained subjects were studied during 3 h of recovery while consuming one of four drinks in random order. Drinks were ingested in three 500 ml boluses, immediately after exercise and then after 1 and 2 h of recovery. Each bolus of the control drink contained 0.8 g x kg(-1) body weight of glucose. The other drinks contained the same amount of glucose and 0.3 g x kg(-1) body weight of 1) glutamine, 2) a wheat hydrolysate (26% glutamine) and 3) a whey hydrolysate (6.6% glutamine). Plasma glutamine, decreased by approximately 20% during recovery with ingestion of the control drink, no changes with ingestion of the protein hydrolysates drinks, and a 2-fold increase with ingestion of the free glutamine drinks. The rate of glycogen resynthesis was not significantly different in the four tests: 28 +/- 5, 26 +/- 6, 33 +/- 4, and 34 +/- 3 mmol glucosyl units x kg(-1) dry weight muscle x h(-1) for the control, glutamine, wheat- and whey hydrolysate ingestion, respectively. It is concluded that ingestion of a glutamine/carbohydrate mixture does not increase the rate of glycogen resynthesis in muscle. Glycogen resynthesis rates were higher, although not statistically significant, after ingestion of the drink containing the wheat (21 +/- 8%) and whey protein hydrolysate (20 +/- 6%) compared to ingestion of the control and free glutamine drinks, implying that further research is needed on the potential protein effect.

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    Metabolism 2000 Dec;49(12):1555-60 Related Articles, Links


    Intravenous glutamine does not stimulate mixed muscle protein synthesis in healthy young men and women.

    Zachwieja JJ, Witt TL, Yarasheski KE.

    Exercise and Nutrition Program, Pennington Biomedical Research Center, Baton Rouge, LA, USA.

    We investigated the effects of a glutamine-supplemented amino acid mixture on vastus lateralis muscle protein synthesis rate in healthy young men and women. Three men and 3 women (27.8 +/- 2.0 yr, 22.2 +/- 1.0 body mass index [BMI], 56.1 +/- 4.5 kg lean body mass [LBM]) received a 14-hour primed, constant intravenous infusion of L[1-13C]leucine to evaluate the fractional rate of mixed muscle protein synthesis. In addition to tracer administration, a clinically relevant amino acid mixture supplemented with either glutamine or glycine in amounts isonitrogenous to glutamine, was infused. Amino acid mixtures were infused on separate occasions in random order at a rate of 0.04 g/kg/h (glutamine at approximately 0.01 g/kg/h) with at least 2 weeks between treatment. For 2 days before and on the day of an infusion, dietary intake was controlled so that each subject received 1.5 g protein/kg/d. Compared with our previous report in the postabsorptive state, amino acid infusion increased the fractional rate of mixed muscle protein synthesis by 48% (P < .05); however, the addition of glutamine to the amino acid mixture did not further elevate muscle protein synthesis rate (ie, 0.071% +/- 0.008%/h for amino acids + glutamine v 0.060% +/- 0.008%/h for amino acids + glycine; P = .316). Plasma glutamine concentrations were higher (P < .05) during the glutamine-supplemented infusion, but free intramuscular glutamine levels were not increased (P = .363). Both plasma and free intramuscular glycine levels were increased when extra glycine was included in the infused amino acid mixture (both P < .0001). We conclude that intravenous infusion of amino acids increases the fractional rate of mixed muscle protein synthesis, but addition of glutamine to the amino acid mixture does not further stimulate muscle protein synthesis rate in healthy young men and women.

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    J Appl Physiol 2002 Sep;93(3):813-22 Related Articles, Links


    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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    Effect of glutamine and protein supplementation on exercise-induced decreases in salivary IgA.

    Krzywkowski K, Petersen EW, Ostrowski K, Link-Amster H, Boza J, Halkjaer-Kristensen J, Pedersen BK.

    The Copenhagen Muscle Research Centre, Rigshospitalet, 2200 Copenhagen, Denmark.

    Postexercise immune impairment has been linked to exercise-induced decrease in plasma glutamine concentration. This study examined the possibility of abolishing the exercise-induced decrease in salivary IgA through glutamine supplementation during and after intense exercise. Eleven athletes performed cycle ergometer exercise for 2 h at 75% of maximal oxygen uptake on 3 separate days. Glutamine (a total of 17.5 g), protein (a total of 68.5 g/6.2 g protein-bound glutamine), and placebo supplements were given during and up to 2 h after exercise. Unstimulated, timed saliva samples were obtained before exercise and 20 min, 140 min, 4 h, and 22 h postexercise. The exercise protocol induced a decrease in salivary IgA (IgA concentration, IgA output, and IgA relative to total protein). The plasma concentration of glutamine was decreased by 15% 2 h postexercise in the placebo group, whereas this decline was abolished by both glutamine and protein supplements.None of the supplements, however, was able to abolish the decline in salivary IgA. This study does not support that postexercise decrease in salivary IgA is related to plasma glutamine concentrations.

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    Effect of carb intake on plasma glutamine

    Int J Sport Nutr 1998 Mar;8(1):49-59 Related Articles, Links


    Effect of low- and high-carbohydrate diets on the plasma glutamine and circulating leukocyte responses to exercise.

    Gleeson M, Blannin AK, Walsh NP, Bishop NC, Clark AM.

    School of Sport and Exercise Sciences, University of Birmingham, Edgbaston, England.

    We examined the effects of a low-carbohydrate (CHO) diet on the plasma glutamine and circulating leukocyte responses to prolonged strenuous exercise. Twelve untrained male subjects cycled for 60 min at 70% of maximal oxygen uptake on two separate occasions, 3 days apart. All subjects performed the first exercise task after a normal diet; they completed the second exercise task after 3 days on either a high-CHO diet (75 +/- 8% CHO, n = 6) or a low-CHO diet (7 +/- 4% CHO, n = 6). The low-CHO diet was associated with a larger rise in plasma cortisol during exercise, a greater fall in the plasma glutamine concentration during recovery, and a larger neutrophilia during the postexercise period. Exercise on the high-CHO diet did not affect levels of plasma glutamine and circulating leukocytes. We conclude that CHO availability can influence the plasma glutamine and circulating leukocyte responses during recovery from intense prolonged exercise.

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    Clin Nutr 2002 Oct;21(5):423-9 Related Articles, Links


    Carbohydrate supplementation during intense exercise and the immune response of cyclists.

    Bacurau RF, Bassit RA, Sawada L, Navarro F, Martins E Jr, Costa Rosa LF.

    Department of Physiology and Biophysics, Institute of Biomedical Sciences, University of Sao Paulo, Brazil.

    OBJECTIVE: To evaluate the effect of carbohydrate supplementation upon some aspects of the immune function in athletes during intense indoor cycling. METHODS: Twelve male athletes cycled for 20 min at a velocity corresponding to 90% of that obtained at the anaerobic threshold and rested for 20 min. This protocol was repeated six times. The athletes received, during the trial, water ad libitum, or a solution of carbohydrate (95% glucose polymers and 5% fructose) at 10% (w/v), 1 g kg h every 20 min, starting at the 10th minute of the first exercise period, plus extra water ad libitum. RESULTS: Exercise induced a reduction in peripheral blood mononuclear cell proliferation (37%) as well as in the production of cytokines by cultured cells (interleukin-1 (IL-1), interleukin-2 (IL-2), tumor necrosis factor-alpha (TNF-alpha) and interferon-gamma (IFN-gamma), by 37%, 35%, 26% and 16%, respectively). All of these changes were prevented by the ingestion of a carbohydrate drink by the athletes, except that in IFN-gamma production, which was equally decreased (17%) after the second trial. The concentration of plasma glutamine, an important fuel for immune cells, was decreased in the placebo group but maintained in the group that received carbohydrate. CONCLUSION: Carbohydrate supplementation affects positively the immune response of cyclists by avoiding or minimizing changes in plasma glutamine concentration

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    An excerpt from "Appetite For Construction
    Building Results From Research"
    by John M. Berardi

    Should I Spend my Hard-Earned Money on Glutamine or Hookers?

    .... A high protein diet provides a big whack of glutamine as it is. In fact, if you follow standard bodybuilding protein recommendations, about 10% of your total dietary protein intake is composed of glutamine (milk proteins are composed of somewhere between 3 — 10% glutamine while meat is composed of about 15% glutamine). This means that a high protein diet (400g/day) already provides me with about 40g of glutamine.

    • While the theorists still cling to the idea that since glutamine helps clinical stress, it might help with exercise stress, it‚s important to note that exercise stress has got nothin‚ on surgery, cancer, sepsis, burns, etc. For example, when compared with downhill running or weight lifting, urinary nitrogen loss is 15x (1400%) greater in minor surgery, 25x (2400%) greater in major surgery, and 33x (3200%) greater in sepsis. When it comes to the immune response, it‚s about 9x (800%) greater with surgery. When it comes to metabolic increase, it‚s 7x (600%) greater with burn injury, and when it comes to creatine kinase release; it‚s about 2x (100%) greater with surgery. As I said, exercise has got nothin‚ on real, clinical stress. It‚s like trying to compare the damage inflicted by a peashooter and that inflicted by a rocket launcher.

    • The major studies examining glutamine supplementation in otherwise healthy weightlifters have shown no effect. In the study by Candow et al (2001), 0.9g of supplemental glutamine/kg/day had no impact on muscle performance, body composition, and protein degradation. Folks, that's 90g per day for some lifters.

    • The majority of the studies using glutamine supplementation in endurance athletes have shown little to no measurable benefit on performance or immune function.

    • And with respect to glycogen replenishment in endurance athletes, it's interesting to note that the first study that looked at glycogen resynthesis using glutamine missed a couple of things. Basically, the study showed that after a few glycogen depleting hours of cycling at a high percentage of VO2 max interspersed with very intense cycle sprints that were supramaximal, a drink containing 8g of glutamine replenished glycogen to the same extent as a drink containing 61g of carbohydrate.

    The problem was that during the recovery period, a constant IV infusion of labeled glucose was given (i.e., a little bit of glucose was given to both groups by IV infusion). While this isn't too big of a deal on its own since the infusion only provided a couple of grams of glucose, the other problem is that during glycogen depleting exercise, a lot of alanine, lactate, and other gluconeogenic precursors are released from the muscle.

    What this means is that there's a good amount of glucose that will be formed after such exercise, glucose that will be made in the liver from the gluconeogenic precursors and that will travel to the muscle to replenish glycogen. Therefore, without a placebo group that receives no calories, carbohydrates, or glutamine, we have no idea of knowing whether or not the placebo would have generated the same amount of glycogen replenishment as the glutamine group or the glutamine plus carbohydrate group. To say it another way, perhaps there's a normal glycogen replenishment curve that was unaffected by any of the treatments.

    • And finally, with respect to the claims that glutamine might increase cell swelling/volume (something I once believed was a reality), we decided to test this theory out in our lab using multifrequency bioelectric impedance analysis as well as magnetic resonance spectroscopy. The pilot data that's kicking around has demonstrated that glutamine supplementation has no effect on total body water, intracellular fluid volumes, or extracellular fluid volumes (as measured by mBIA) and has no effect on muscle volume (as measured by nMRS)...


  2. Do not **** with this thread. I mean it.
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  3. Nelson
    Nelson's Avatar

    YJ the anti-glutaminist
  4. Cool Money on glutamine is well spent


    Glutamine increases cell volume which increases protein synthesis, thats ideal for adding muscle mass(or bulking).

    Studies show that adding glutamine to protein supplements increases protein synthesis more than protein alone.

    For a serious bodybuilder, there is nothing non-essential about glutamine. The research is more than conclusive that the levels of glutamine (and cysteine) are chemical determinants of whether you will lose or gain muscle mass.

    Kinscherf.R et al. Low plasma glutamine in combination with high glutamine levels indicate risk for loss of body cell mass in healthy individuals: the effect of N-acetyl-cysteine. J.Mol.Med. vol 74:393-400 1996.

    when our body doesn't get enough, musle mass is lost in large amounts.

    Droge.W. and Holm.E. Role of cysteine and glutathione in HIV infection and other diseases associated with muscle wasting and immunological dysfunction.FASEB J.11:1077-1089,1997.

    Hack.V et al. Cystine levels, cystine flux, and protein catabolism in cancer cachexia, HIV/SIV infection and senescence. FASEB J. 11:84-92 1997.

    "The other 10(9 in infants) are called inessential amino acids - not because the body does not require them, buy because it CAN synthesis its own WHEN THE DIET DOES NOT SUPPLY THEM. Cells do not store surplus amino acids for later use. When a protein is to be synthesized, all of the amino acids necssary MUST be present at once, and if even on is missing, the protein cannot be made."
    -- saladin; Anatopmy & Physiology: The unity of form and function. p992

    recent research has demonstrated that adding glutamine to two isocaloric /isoprotein diets increased protein synthesis within muscle tissue. The diet without glutamine only increased rates in intestinal cells.

    You can argue whether or not the supplemental glutamine was used by the intesitine or acutally made it to muscle tissue, but the result is the same. Added glutamine increased protein synthesis, and obviously wasn't "wasted"

    Nutrition 2001 Jan;17(1):35-40

    Theres much more evidence for glutamine supplementation than there is against.


    Bowtell, J. L., K. Gelly, M. L. Jackman, A. Patel, M.
    Simeoni, and M. J. Rennie. Effect of oral glutamine on
    whole body carbohydrate storage during recovery from exhaustive
    exercise. J. Appl. Physiol. 86(6): 1770–1777, 1999.—The
    purpose of this study was to determine the efficacy of glutamine
    in promoting whole body carbohydrate storage and
    muscle glycogen resynthesis during recovery from exhaustive
    exercise. Postabsorptive subjects completed a glycogendepleting
    exercise protocol, then consumed 330 ml of one of
    three drinks, 18.5% (wt/vol) glucose polymer solution, 8 g
    glutamine in 330 ml glucose polymer solution, or 8 g glutamine
    in 330 ml placebo, and also received a primed constant
    infusion of [1-13C]glucose for 2 h. Plasma glutamine concentration
    was increased after consumption of the glutamine drinks
    (0.7–1.1 mM, P , 0.05). In the second hour of recovery, whole
    body nonoxidative glucose disposal was increased by 25%
    after consumption of glutamine in addition to the glucose
    polymer (4.48 6 0.61 vs. 3.59 6 0.18 mmol/kg, P , 0.05). Oral
    glutamine alone promoted storage of muscle glycogen to an
    extent similar to oral glucose polymer. Ingestion of glutamine
    and glucose polymer together promoted the storage of carbohydrate
    outside of skeletal muscle, the most feasible site
    being the liver.


    <<< Strength Cond Res 2002 Feb;16(1):157-60
    The effects of high-dose glutamine ingestion on weightlifting performance>>


    Effect of glutamine supplementation of the diet on tissue protein synthesis rate of glucocorticoid-treated rats.

    Boza JJ, Turini M, Moennoz D, Montigon F, Vuichoud J, Gueissaz N, Gremaud G, Pouteau E, Piguet-Welsch C, Finot PA, Ballevre O.

    Nestle Research Center, Vers-chez-les-Blanc, 1000 Lausanne 26, Switzerland. [email protected]

    Although glutamine status in the critically ill patient can be improved by nutritional means, the most effective way of effecting such supplementation has received little attention. We evaluated two different ways of supplementing clinical nutrition products with glutamine, either with free glutamine or by providing a glutamine-rich protein source, in acute glucocorticoid-treated (intraperitoneal dexamethasone, 120 mg/kg) rats. During the recovery period, the animals received isonitrogenous and isoenergetic diets containing either casein, mixed whey proteins with or without glutamine, or carob protein plus essential amino acids. Plasma and tissue amino acids and glutathione as well as tissue protein synthesis were measured. Dexamethasone treatment lowered weight gain, muscle glutamine, and muscle and jejunal protein synthetic rate. Muscle protein synthesis was increased (from 15.9% to 24.2%/d) only when glutamine was included in the diet as a free amino acid. This increase paralleled a rise in plasma glutamine. We speculate that glutamine provided in dietary protein is extensively metabolized by the splanchnic tissues and does not influence peripheral glutamine status to the same extent as glutamine provided in a free amino acid form. However, both forms of glutamine supplementation were equally effective in increasing protein synthesis in the jejunum (by 25%). This is likely the main benefit of glutamine supplementation of enteral nutrition formulas.



    Kinscherf R, Hack V, Fischbach T, Friedmann B, Weiss C, Edler L, Bartsch P, Droge W.
    Low plasma glutamine in combination with high glutamate levels indicate risk for loss of body cell mass in healthy individuals: the effect of N-acetyl-cysteine.



    Division of Immunochemistry, Deutsches Krebsforschungszentrum, Heidelberg, Germany.

    Skeletal muscle catabolism, low plasma glutamine, and high venous glutamate levels are common among patients with cancer or human immunodeficiency virus infection. In addition, a high glycolytic activity is commonly found in muscle tissue of cachectic cancer patients, suggesting insufficient mitochondrial energy metabolism. We therefore investigated (a) whether an "an-aerobic physical exercise" program causes similar changes in plasma amino acid levels,
    and (b) whether low plasma glutamine or high glutamate levels are risk factors for loss of body cell mass (BCM) in healthy human subjects, i.e., in the absence of a tumor or virus infection. Longitudinal measurements from healthy subjects over longer periods suggest that the age-related loss of BCM occur mainly during episodes with high venous glutamate levels, indicative of decreased muscular transport activity for glutamate. A significant increase in venous glutamate levels from 25 to about 40 microM was seen after a program of "anaerobic physical exercise." This was associated with changes in T lymphocyte numbers. Under these conditions persons with low baseline levels of plasma glutamine, arginine, and cystine levels also showed a loss of BCM. This loss of BCM was correlated not only with the amino acid levels at baseline examination, but also with an increase in plasma glutamine, arginine, and cystine levels during the observation period, suggesting that a loss of BCM in healthy individuals terminates itself by adjusting these amino acids to higher levels that stabilize BCM. To test a possible regulatory role of cysteine in this context we determined the effect of N-acetyl-cysteine on BCM in a group of subjects with relatively low glutamine levels. The placebo group of this study showed a loss of BCM and an increase in body fat, suggesting that body protein had been converted into other forms of chemical energy. The decrease in mean BCM/body fat ratios was prevented by N-acetyl-cysteine, indicating that cysteine indeed plays a regulatory role in the physiological control of BCM.



    Julio J. Boza, Martial Dangin, Denis Moënnoz, Franck Montigon, Jacques Vuichoud, Andrée Jarret, Etienne Pouteau, Gerard Gremaud, Sylviane Oguey-Araymon, Didier Courtois, Alfred Woupeyi, Paul-André Finot, and Olivier Ballèvre
    Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers
    Am J Physiol Gastrointest Liver Physiol 281: G267-G274, 2001

    The objectives of the present study were to determine the splanchnic extraction of glutamine after ingestion of glutamine-rich protein (15N-labeled oat proteins) and to compare it with that of free glutamine and to determine de novo glutamine synthesis before and after glutamine consumption. Eight healthy adults were infused intravenously in the postabsorptive state with L-[1-13C]glutamine (3 µmol · kg-1 · h-1) and L-[1-13C]lysine (1.5 µmol · kg-1 · h-1) for 8 h. Four hours after the beginning of the infusion, subjects consumed (every 20 min) a liquid formula providing either 2.5 g of protein from 15N-labeled oat proteins or a mixture of free amino acids that mimicked the oat-amino acid profile and contained L-[2,5-15N2]glutamine and L-[2-15N]lysine. Splanchnic extraction of glutamine reached 62.5 ± 5.0% and 66.7 ± 3.9% after administration of 15N-labeled oat proteins and the mixture of free amino acids, respectively. Lysine splanchnic extraction was also not different (40.9 ± 11.9% and 34.9 ± 10.6% for 15N-labeled oat proteins and free amino acids, respectively). The main conclusion of the present study is that glutamine is equally bioavailable when given enterally as a free amino acid and when protein bound. Therefore, and taking into consideration the drawbacks of free glutamine supplementation of ready-to-use formulas for enteral nutrition, protein sources naturally rich in this amino acid are the best option for providing stable glutamine.



    Mittendorfer, E. Volpi, and R. R. Wolfe
    Whole body and skeletal muscle glutamine metabolism in healthy subjects
    Am J Physiol Endocrinol Metab 280: E323-E333, 2001.

    We measured glutamine kinetics using L-[5-15N]glutamine and L-[ring-2H5]phenylalanine infusions in healthy subjects in the postabsorptive state and during ingestion of an amino acid mixture that included glutamine, alone or with additional glucose. Ingestion of the amino acid mixture increased arterial glutamine concentrations by ~20% (not by 30%; P < 0.05), irrespective of the presence or absence of glucose. Muscle free glutamine concentrations remained unchanged during ingestion of amino acids alone but decreased from 21.0 ± 1.0 to 16.4 ± 1.6 mmol/l (P < 0.05) during simultaneous ingestion of glucose due to a decrease in intramuscular release from protein breakdown and glutamine synthesis (0.82 ± 0.10 vs. 0.59 ± 0.06 µmol · 100 ml leg-1 · min-1; P < 0.05). In both protocols, muscle glutamine inward and outward transport and muscle glutamine utilization for protein synthesis increased during amino acid ingestion; leg glutamine net balance remained unchanged. In summary, ingestion of an amino acid mixture that includes glutamine increases glutamine availability and uptake by skeletal muscle in healthy subjects without causing an increase in the intramuscular free glutamine pool. Simultaneous ingestion of glucose diminishes the intramuscular glutamine concentration despite increased glutamine availability in the blood due to decreased glutamine production.
    Last edited by John Benz; 03-19-2003 at 10:03 PM.
  5. Re: Money on glutamine is well spent


    Originally posted by John Benz


    when our body doesn't get enough, musle mass is lost in large amounts.
    LMAO! Losti n large amounts huh? Like what? 3lbs a minute?

    Droge.W. and Holm.E. Role of cysteine and glutathione in HIV infection and other diseases associated with muscle wasting and immunological dysfunction.FASEB J.11:1077-1089,1997.

    Hack.V et al. Cystine levels, cystine flux, and protein catabolism in cancer cachexia, HIV/SIV infection and senescence. FASEB J. 11:84-92 1997.
    Do these have attached articles? or are they randon citations?

    &quot;The other 10(9 in infants) are called inessential amino acids - not because the body does not require them, buy because it CAN synthesis its own WHEN THE DIET DOES NOT SUPPLY THEM. Cells do not store surplus amino acids for later use. When a protein is to be synthesized, all of the amino acids necssary MUST be present at once, and if even on is missing, the protein cannot be made.&quot;
    -- saladin; Anatopmy &amp; Physiology: The unity of form and function. p992
    Not much relevance to support glutamine supplementation. After all, cottage cheese, beans, milk, protein powder, etc. all contain solid amounts of glutamine.

    recent research has demonstrated that adding glutamine to two isocaloric /isoprotein diets increased protein synthesis within muscle tissue. The diet without glutamine only increased rates in intestinal cells.
    Sorry, this was dismissed above.

    You can argue whether or not the supplemental glutamine was used by the intesitine or acutally made it to muscle tissue, but the result is the same. Added glutamine increased protein synthesis, and obviously wasn't &quot;wasted&quot;
    Says who? some random guy? Im sure he works for EAS though.



    Theres much more evidence for glutamine supplementation than there is against.
    Sorry once again, afraid not.


    Bowtell, J. L., K. Gelly, M. L. Jackman, A. Patel, M.
    Simeoni, and M. J. Rennie. Effect of oral glutamine on
    whole body carbohydrate storage during recovery from exhaustive
    exercise. J. Appl. Physiol. 86(6): 1770–1777, 1999.—The
    purpose of this study was to determine the efficacy of glutamine
    in promoting whole body carbohydrate storage and
    muscle glycogen resynthesis during recovery from exhaustive
    exercise. Postabsorptive subjects completed a glycogendepleting
    exercise protocol, then consumed 330 ml of one of
    three drinks, 18.5% (wt/vol) glucose polymer solution, 8 g
    glutamine in 330 ml glucose polymer solution, or 8 g glutamine
    in 330 ml placebo, and also received a primed constant
    infusion of [1-13C]glucose for 2 h. Plasma glutamine concentration
    was increased after consumption of the glutamine drinks
    (0.7–1.1 mM, P , 0.05). In the second hour of recovery, whole
    body nonoxidative glucose disposal was increased by 25%
    after consumption of glutamine in addition to the glucose
    polymer (4.48 6 0.61 vs. 3.59 6 0.18 mmol/kg, P , 0.05). Oral
    glutamine alone promoted storage of muscle glycogen to an
    extent similar to oral glucose polymer. Ingestion of glutamine
    and glucose polymer together promoted the storage of carbohydrate
    outside of skeletal muscle, the most feasible site
    being the liver.
    This was dismissed above also, but this is for LIVER glycogen replacement, no where near as essential as muscle glycogen replacement.




    Effect of glutamine supplementation of the diet on tissue protein synthesis rate of glucocorticoid-treated rats.

    Boza JJ, Turini M, Moennoz D, Montigon F, Vuichoud J, Gueissaz N, Gremaud G, Pouteau E, Piguet-Welsch C, Finot PA, Ballevre O.

    Nestle Research Center, Vers-chez-les-Blanc, 1000 Lausanne 26, Switzerland. [email protected]

    Although glutamine status in the critically ill patient can be improved by nutritional means, the most effective way of effecting such supplementation has received little attention. We evaluated two different ways of supplementing clinical nutrition products with glutamine, either with free glutamine or by providing a glutamine-rich protein source, in acute glucocorticoid-treated (intraperitoneal dexamethasone, 120 mg/kg) rats. During the recovery period, the animals received isonitrogenous and isoenergetic diets containing either casein, mixed whey proteins with or without glutamine, or carob protein plus essential amino acids. Plasma and tissue amino acids and glutathione as well as tissue protein synthesis were measured. Dexamethasone treatment lowered weight gain, muscle glutamine, and muscle and jejunal protein synthetic rate. Muscle protein synthesis was increased (from 15.9% to 24.2%/d) only when glutamine was included in the diet as a free amino acid. This increase paralleled a rise in plasma glutamine. We speculate that glutamine provided in dietary protein is extensively metabolized by the splanchnic tissues and does not influence peripheral glutamine status to the same extent as glutamine provided in a free amino acid form. However, both forms of glutamine supplementation were equally effective in increasing protein synthesis in the jejunum (by 25%). This is likely the main benefit of glutamine supplementation of enteral nutrition formulas.
    This was also dismissed above. It says in the article that nutritonal provided glutamine is a good way to replace lost glutamine stores, no need buy extra and get robbed.

    Kinscherf R, Hack V, Fischbach T, Friedmann B, Weiss C, Edler L, Bartsch P, Droge W.
    Low plasma glutamine in combination with high glutamate levels indicate risk for loss of body cell mass in healthy individuals: the effect of N-acetyl-cysteine.

    Division of Immunochemistry, Deutsches Krebsforschungszentrum, Heidelberg, Germany.

    Skeletal muscle catabolism, low plasma glutamine, and high venous glutamate levels are common among patients with cancer or human immunodeficiency virus infection. In addition, a high glycolytic activity is commonly found in muscle tissue of cachectic cancer patients, suggesting insufficient mitochondrial energy metabolism. We therefore investigated (a) whether an &quot;an-aerobic physical exercise&quot; program causes similar changes in plasma amino acid levels,
    and (b) whether low plasma glutamine or high glutamate levels are risk factors for loss of body cell mass (BCM) in healthy human subjects, i.e., in the absence of a tumor or virus infection. Longitudinal measurements from healthy subjects over longer periods suggest that the age-related loss of BCM occur mainly during episodes with high venous glutamate levels, indicative of decreased muscular transport activity for glutamate. A significant increase in venous glutamate levels from 25 to about 40 microM was seen after a program of &quot;anaerobic physical exercise.&quot; This was associated with changes in T lymphocyte numbers. Under these conditions persons with low baseline levels of plasma glutamine, arginine, and cystine levels also showed a loss of BCM. This loss of BCM was correlated not only with the amino acid levels at baseline examination, but also with an increase in plasma glutamine, arginine, and cystine levels during the observation period, suggesting that a loss of BCM in healthy individuals terminates itself by adjusting these amino acids to higher levels that stabilize BCM. To test a possible regulatory role of cysteine in this context we determined the effect of N-acetyl-cysteine on BCM in a group of subjects with relatively low glutamine levels. The placebo group of this study showed a loss of BCM and an increase in body fat, suggesting that body protein had been converted into other forms of chemical energy. The decrease in mean BCM/body fat ratios was prevented by N-acetyl-cysteine, indicating that cysteine indeed plays a regulatory role in the physiological control of BCM.
    Once again, this is based around sick, or immunodepressive individuals, how comparable are the immune systems of a weight training athlete to an AIDS patient? Hmm



    Julio J. Boza, Martial Dangin, Denis Moënnoz, Franck Montigon, Jacques Vuichoud, Andrée Jarret, Etienne Pouteau, Gerard Gremaud, Sylviane Oguey-Araymon, Didier Courtois, Alfred Woupeyi, Paul-André Finot, and Olivier Ballèvre
    Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers
    Am J Physiol Gastrointest Liver Physiol 281: G267-G274, 2001

    The objectives of the present study were to determine the splanchnic extraction of glutamine after ingestion of glutamine-rich protein (15N-labeled oat proteins) and to compare it with that of free glutamine and to determine de novo glutamine synthesis before and after glutamine consumption. Eight healthy adults were infused intravenously in the postabsorptive state with L-[1-13C]glutamine (3 µmol · kg-1 · h-1) and L-[1-13C]lysine (1.5 µmol · kg-1 · h-1) for 8 h. Four hours after the beginning of the infusion, subjects consumed (every 20 min) a liquid formula providing either 2.5 g of protein from 15N-labeled oat proteins or a mixture of free amino acids that mimicked the oat-amino acid profile and contained L-[2,5-15N2]glutamine and L-[2-15N]lysine. Splanchnic extraction of glutamine reached 62.5 ± 5.0% and 66.7 ± 3.9% after administration of 15N-labeled oat proteins and the mixture of free amino acids, respectively. Lysine splanchnic extraction was also not different (40.9 ± 11.9% and 34.9 ± 10.6% for 15N-labeled oat proteins and free amino acids, respectively).The main conclusion of the present study is that glutamine is equally bioavailable when given enterally as a free amino acid and when protein bound. Therefore, and taking into consideration the drawbacks of free glutamine supplementation of ready-to-use formulas for enteral nutrition, protein sources naturally rich in this amino acid are the best option for providing stable glutamine.
    I agree. So why not get a decent protein supplement rich in glutamine and not waste your money on extra glutamine that your body doesnt even absorb?



    Mittendorfer, E. Volpi, and R. R. Wolfe
    Whole body and skeletal muscle glutamine metabolism in healthy subjects
    Am J Physiol Endocrinol Metab 280: E323-E333, 2001.

    We measured glutamine kinetics using L-[5-15N]glutamine and L-[ring-2H5]phenylalanine infusions in healthy subjects in the postabsorptive state and during ingestion of an amino acid mixture that included glutamine, alone or with additional glucose. Ingestion of the amino acid mixture increased arterial glutamine concentrations by ~20% (not by 30%; P &lt; 0.05), irrespective of the presence or absence of glucose. Muscle free glutamine concentrations remained unchanged during ingestion of amino acids alone but decreased from 21.0 ± 1.0 to 16.4 ± 1.6 mmol/l (P &lt; 0.05) during simultaneous ingestion of glucose due to a decrease in intramuscular release from protein breakdown and glutamine synthesis (0.82 ± 0.10 vs. 0.59 ± 0.06 µmol · 100 ml leg-1 · min-1; P &lt; 0.05). In both protocols, muscle glutamine inward and outward transport and muscle glutamine utilization for protein synthesis increased during amino acid ingestion; leg glutamine net balance remained unchanged. In summary, ingestion of an amino acid mixture that includes glutamine increases glutamine availability and uptake by skeletal muscle in healthy subjects without causing an increase in the intramuscular free glutamine pool. Simultaneous ingestion of glucose diminishes the intramuscular glutamine concentration despite increased glutamine availability in the blood due to decreased glutamine production.

    LoL...thats a shrewd observation. But again, this is why a protein supplement is needed. Whey protein covers each and every factor here, and then some...


    All in all Im very proud of you for getting away from T-Mag articles, this is certainly a step up, still way off, but coming along.
    •   
       


  6. Your stating your opinion, which is worthless. Refute me with proof. None of your statements disprove anything. Nor do your articles on "young adults." Try harder, you aren't even close.

  7. Originally posted by John Benz
    Your stating your opinion, which is worthless. Refute me with proof. None of your statements disprove anything. Nor do your articles on &quot;young adults.&quot; Try harder, you aren't even close.
    Umm... yea. I think you know better. You must have forgotten to read the articles in this thread aye? They refute everything you posted....and then some. You're far behind, you're battling a lost cause.
  8. Talking


    If you say so, sonny.

  9. Glutamine seems kind of like ZMA to me. It sounds great on paper but after weeks of use I did not notice any difference whatsoever. I'm gonna lean towards Yellowjacket here, only from personal experience. Even if either of them did anything, I probably wont be buying them again because they are not worth the money to me. Not that what I said disproves/proves anything though.

  10. L.R. BRILLA AND VICTOR CONTE. Effects of a Novel Zinc-Magnesium Formulation on Hormones and Strength. JEPonline, 3(4): 26-36, 2000. Muscle attributes and selected blood hormones of football players were assessed in response to a nightly supplementation regimen during spring football, over an 8-week period, with pre-post measures. A double-blind randomized study was conducted with ZMA (30 mg zinc monomethionine aspartate, 450 mg magnesium aspartate, and 10.5 mg of vitamin B-6) and placebo (P), n=12 and n=15, respectively. Plasma zinc and magnesium levels were ZMA (0.80 to 1.04 g/ml; 19.43 to 20.63 mcg/ml ) and P (0.84 to 0.80 g/ml ; 19.68 to 18.04 g/ml), respectively (P<0.001). Free testosterone increased with ZMA (132.1 to 176.3 pg/mL), compared to P (141.0 to 126.6 pg/mL) (P<0.001); IGF-I increased in the ZMA group (424.2 to 439.3 ng/mL) and decreased in P (437.3 to 343.3 ng/mL) (P<0.001). Muscle strength via torque measurements and functional power were assessed with a Biodex dynamometer. Differences were noted between the groups (P<0.001): ZMA (189.9 to 211 Nm at 180º/s and 316.5 to 373.7 Nm at 300º/s) and P (204.2 to 209.1 Nm at 180º/s and 369.5 to 404.3 Nm at 300º/s). The results demonstrate the efficacy of a Zn-Mg preparation (ZMA) on muscle attributes and selected hormones in strength-trained, competitive athletes.

    The study had them take nothing but ZMA, no other supps. So, it could be assumed that getting it from a multi should be just as effective. Here is the full text of the study:

    http://www.css.edu/users/tboone2/asep/Brilla1ColV2.doc

  11. One more...

    J Appl Physiol 2002 Sep;93(3):813-22 Related Articles, Links


    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.

  12. Yep, another

    Am J Physiol Cell Physiol 2001 Oct;281(4):C1259-65 Related Articles, Links


    Effect of glutamine supplementation on exercise-induced changes in lymphocyte function.

    Krzywkowski K, Petersen EW, Ostrowski K, Kristensen JH, Boza J, Pedersen BK.

    Copenhagen Muscle Research Centre and Department of Infectious Diseases, Rigshospitalet, 2200 Copenhagen N, Denmark.

    The purpose of this study was to investigate the possible role of glutamine in exercise-induced impairment of lymphocyte function. Ten male athletes participated in a randomized, placebo-controlled, double-blind crossover study. Each athlete performed bicycle exercise for 2 h at 75% of maximum O(2) consumption on 2 separate days. Glutamine or placebo supplements were given orally during and up to 2 h postexercise. The trial induced postexercise neutrocytosis that lasted at least 2 h. The total lymphocyte count increased by the end of exercise due to increase of both CD3(+)TCR alpha beta(+) and CD3(+)TCR gamma delta(+) T cells as well as CD3(-)CD16(+)CD56(+) natural killer (NK) cells. Concentrations of CD8(+) and CD4(+) T cells lacking CD28 and CD95 on their surface increased more than those of cells expressing these receptors. Within the CD4(+) cells, only CD45RA(-) memory cells, but not CD45RA(+) naive cells, increased in response to exercise. Most lymphocyte subpopulations decreased 2 h after exercise. Glutamine supplementation abolished the postexercise decline in plasma glutamine concentration but had no effect on lymphocyte trafficking, NK and lymphokine-activated killer cell activities, T cell proliferation, catecholamines, growth hormone, insulin, or glucose. Neutrocytosis was less pronounced in the glutamine-supplemented group, but it is unlikely that this finding is of any clinical significance. This study does not support the idea that glutamine plays a mechanistic role in exercise-induced immune changes.

  13. Beautiful........


    Clin Nutr 2002 Oct;21(5):423-9 Related Articles, Links


    Carbohydrate supplementation during intense exercise and the immune response of cyclists.

    Bacurau RF, Bassit RA, Sawada L, Navarro F, Martins E Jr, Costa Rosa LF.

    Department of Physiology and Biophysics, Institute of Biomedical Sciences, University of Sao Paulo, Brazil.

    OBJECTIVE: To evaluate the effect of carbohydrate supplementation upon some aspects of the immune function in athletes during intense indoor cycling. METHODS: Twelve male athletes cycled for 20 min at a velocity corresponding to 90% of that obtained at the anaerobic threshold and rested for 20 min. This protocol was repeated six times. The athletes received, during the trial, water ad libitum, or a solution of carbohydrate (95% glucose polymers and 5% fructose) at 10% (w/v), 1 g kg h every 20 min, starting at the 10th minute of the first exercise period, plus extra water ad libitum. RESULTS: Exercise induced a reduction in peripheral blood mononuclear cell proliferation (37%) as well as in the production of cytokines by cultured cells (interleukin-1 (IL-1), interleukin-2 (IL-2), tumor necrosis factor-alpha (TNF-alpha) and interferon-gamma (IFN-gamma), by 37%, 35%, 26% and 16%, respectively). All of these changes were prevented by the ingestion of a carbohydrate drink by the athletes, except that in IFN-gamma production, which was equally decreased (17%) after the second trial. The concentration of plasma glutamine, an important fuel for immune cells, was decreased in the placebo group but maintained in the group that received carbohydrate. CONCLUSION: Carbohydrate supplementation affects positively the immune response of cyclists by avoiding or minimizing changes in plasma glutamine concentration

  14. MUSCLE EFFLUX OF GLUTAMINE
    IN ORAL CREATINE OVERSUPPLIED SPORTSMEN
    CAN MIMIC STRESS CONDITIONS
    WITH INCREASED RISKS OF ATHLETIC TRAUMAS

    By Renato COCCHI MD, neurologist and medical psychologist


    During the 2nd World Congress on Stress (Melbourne, 1998) Dr G. Tassani and I asserted that stress, even the first phase of overtraining syndrome, induces an increased supply of peripheral Acetylcholine (ACh) for increased availability of its precursor, the choline. This happens because brain reduced turnover of ACh reduces the blood-barrier transport into the brain of choline, but also by an increased efflux of choline from the brain. As for the vagal district, an increasing of ACh during stress had experimental evidence (Hata et al. 1986; Kita et al., 1986).

    The vagal stimulation grows because the direct link between hypothalamic glutamate hyperfunction, and stimulation of some vagal brain nuclei like Nucleus Dorsalis Vagi and Nucleus Tracti Solitarii. (Kunos et al., 1995; Pluzhnichenko, 1997; Yoneda and Tache', 1995).

    As for heart, if the sympathetic system is unable to compensate the increased vagal stimulation, one person could have vagal syncope or an irreversible fatal collapse. Since many physicians have a poor understanding of the dynamic of that mechanism, often we erroneously heard about heart infarcts in such cases. Luckily these are rare events as spontaneous ones.

    Out of the body districts under the vagal control we maintain that it happens the same increasing of the peripheral ACh (ours are only clinical data, now). That drives to postures unbalance and to a power magnification of the athletic gesture. This is the result of a magnified but wrong setting of postures, when they usually set according to their brain kinetic memory mirroring normal conditions. So postures can play at their excursion's limits, with reduced margins for recovery. In that state a provoked athletic trauma could be heavier, because the postures do not easily allow the balance to reset, being at work with poor compensating margins.

    In the same time the voluntary athletic gesture becomes magnified and powerful because of muscular fibres increased stimulation due to a larger amount of ACh into the end-plate.

    The loose of synchronism between postures working at their limits and magnified athletic gesture can end to a spontaneous athletic trauma. In other terms, in a stress situation like that, one can reach an increased easiness to spontaneous athletic traumas and more severity in provoked athletic traumas.

    Which role could play a creatine excess diet in this mechanism?

    Creatine's function is to favour the resynthesis of phospho-creatine, and so the muscular ATP production. The increasing of the body muscular mass could be due to the extra work the larger amount of ATP lets doing, since physical fatigue appears later.

    Red muscles are the greater producers of glutamine and it comes out by means of ATP (Meister, 1956 and 1969; Graham and MacLean, 1998; Yoo, Field and McBurney, 1997).

    There is a key point. There is an efflux of l-glutamine from muscles during extended muscular exercise (Graham and McLean, 1998).

    This fact deals to suggest that the induced fatigue, due to ATP decreasing, be a defense mechanism to avoid muscular fibres' damages like sprains, when muscular work extends.

    Athletes with overtraining stress have low levels of glutamine for months or years (Rowbottom, Keast and Morton, 1996).

    Glutamine is the main precursor of the brain glutamate (Baxter, 1975; Ward, Thanki and Bradford, 1983; Laake et al., 1995; Shuplakow et al., 1977). In all stress conditions at all origin they have, there is growing of the brain glutamate, the more spread excitatory neurotransmitter that produces cascade negative reactions when in excess. (See: Friedman MJ, Charney DS and Deutch AY. Neurobiologcal and clinical consequences of stress, Philadelphia, Lippicott-Raven 1995).

    Sometimes athletes tried to increase their own athletic performances with high doses' creatine diet (up to 20-30 g daily = 5.0-7.5 kg of red meat). If so they set off also an up efflux of muscular glutamine into blood, according to the increased muscular synthesis of glutamine.

    Blood glutamine easily crosses the blood-brain barrier and so makes the brain glutamate increasing. In absence of stress this fact could be not neurochemically relevant although some symptoms of the increased brain glutamate could arise, like in stress. When in a stressed condition, the oversupply of creatine diet in athletes could increase the harmful followings of the stress itself.

    By analogy it is about the same of giving sugar to a diabetic person.

    I use creatine in the form of creatine-phosphate as an anti-fatigue drug since more than 20 years and glutamine since at least 22 years (Cocchi, 1976). Daily doses do not reach more than 2g for creatine-phosphate and 500mg for glutamine.

    In athletes excess creatine diet without considering stress conditions or even to fight stress conditions at muscular level is surely a hazardous practice._

    References

    Baxter FC. Some recent advances in studies of GABA metabolism and compartmentation. In: Roberts E, Chase TN, Tower DB (eds). GABA in nervous system function. New York, Raven 1976: 61-87.

    Cocchi R. Antidepressive properties of l-glutamine. Preliminary report. Acta psychiat belg 1976, 76: 658-666.

    Cocchi R, Tassani G. Spontaneous athletic trauma as the result of overtraining stress. Paper presented during the 2nd World Congress on Stress, Melbourne 25-29 Oct. 1998

    Graham TE, MacLean DA: Ammonia and aminoacid metabolism in skeletal muscle: human, rodent and canine models. Med Sci. Sport Exerc 1998, 30: 34-46.

    Hata T, Kita T, Higashiguchi T, Ichida S. Total Ach content, and activities of choline acetyltransferase and acetylcholinesterase in brain and duodenum of SART-stressed (repeated cold-stressed) rat. Japan. J Pharmacol 1986, 41: 475-485.

    Horger BA, Roth RH. Stress and central amino acid system. In: Friedman MJ, Charney DS, Deutch AJ. (eds). Neurobiological and clinical consequences of stress: From normal adaptation to PTSD. Philadelphia, Lippincott-Raven 1995: 61-81.

    Kita T, Hata T, Higashiguchi T, Itoh E., Kavabata A. Changes of total acetylcholine and the activity of related enzymes in SART-(repeated cold)-stressed rat brain and duodenum. Japan. J Pharmacol 1986, 40: 174-177

    Kunos G, Varga K. The tachycardia associated with the defense reaction involves activation of both GABA A and GABA B receptors in the nucleus tracti solitarii. Clin Exper Hhypertens 1995, 17: 91-100.

    Laake J.H. et al.: Glutamine from glial cells is essential for the maintenance of the nerve terminal pool of glutamate: Immunogold evidence from hippocampal slice cultures. J. Neurochem. 1995, 65: 871-881.

    Meister A. Metabolism of l-glutamine. Physiol Rev 1956, 36: 103-126.

    Meister A. On the synthesis and utilisation of l-glutamine. Harvey Lect. 1969, 63: 139-168.

    Pluzhnichenko EB. Spatial organization of hypothalamic neurons projecting to the "gastric region" of the vagosolitary complex. Neurosci Behav Physiol 1997, 27: 688-691.

    Rowbottom DG, Keast D, Morton AR. The emerging role of glutamine as an indicator of exercise stress and overtraining. Sports Med 1996, 21: 80-97.

    Shuplakow O. et al.: Glial and neuronal glutamine pools at glutamergic synapses with distinct properties. Neuroscience 1977, 77: 1201-1212.

    Ward HK, Thanki CM, Bradford HF. Glutamine and glucose as precursors of transmitter amino acids: Ex vivo studies. J Neurochem 1983, 40: 855-860

    Yoneda M, Tache' Y. SMS 201-995-induced stimulation of gastric acid via the dorsal vagal complex and inhibition via the hypothalamus in anaesthetized rats. Br J Pharmacol 1995, 116: 2303-2309.

    Yoo S.S., Field C.J., McBurney M.I.: Glutamine supplementation maintains intramuscular glutamine concentrations and normalizes lymphocyte function in infected early weaned pigs. J. Nutr. 1997, 127: 2253-2259..

    Presented at the 6th International Congress on Amino Acid, Bonn August 3-7, 1999_
    Author's address: dr Renato COCCHI, via Mercalli 10
    42100 Reggio Emilia (Italy)

  15. Canadian Journal of Physiology and Pharmacology
    Contents | Sample Issue | For Authors | Information | Services |

    Glutamine and the effects of exhaustive exercise upon the immune response
    Linda M. Castell and Eric A. Newsholme
    Can. J. Physiol. Pharmacol./Rev. Can. Physiol. Pharmacol. 76(5): 524-532 (1998)

    Abstract: There is a high incidence of infections in athletes undergoing intense, prolonged training or participating in endurance races (e.g., the marathon), in particular, upper respiratory tract infections. Prolonged, exhaustive exercise can lower the plasma level of the amino acid, glutamine, which is an important fuel for some cells of the immune system and may have specific immunostimulatory effects. This could therefore be an important factor in the event of an impaired response of immune cells to opportunistic infections. The effects of feeding glutamine to sedentary individuals and to marathon and ultramarathon runners before and after prolonged, exhaustive exercise has been investigated in a series of studies that monitored the incidence of infections and some acute-phase response markers. Oral glutamine, compared with a placebo, appeared to have a beneficial effect on the incidence of infections reported by runners after a marathon.

  16. Thats a great article showing the benefits of creatine, may save that one.....

  17. That's a lot of anti-glutamine research. Me thinks I'll finish out the rest of my supply then discontinue it.

    That leaves me with...creatine, multivitamins, zma, and sometimes guggulsterones taken with thermogenics.

  18. Ok, I can see how free form L-Glutamine supplementation might be of little value, but I still value in glutamine peptides, especially combined in and augmenting a good protein blend. For myself I have been ordering a custom blend from ProteinCustomizer that is 30% CFM Whey Isolate, 20% Milk Protein Isolate, 20% Micellular Casein, 20% Egg Protein Isolate, 9% Soy Isolate and 1% Glutamine Peptides. I plan on playing with the % of Glutamine Peptides up to 5% with a corresponding decrease in Soy Isolate. I feel glutamine in this form has helped me tremendously in recovery, unfortunately I don't have hard science to back it up, just my personal observations.

  19. Effect of oral glutamine on whole-body carbohydrate storage during recovery from exhaustive exercise.. Bowtell, J. L., K. Gelly, M. L. Jackman, A. Patel, M. Simeoni, M. J. Rennie. Department of Anatomy and Physiology, University of Dundee, Dundee, Scotland, DD1 4HN and * Department of Electronics and Informatics, University of Padova, Padova, Italy

    APStracts 5:0541A, 1998.
    The aim of this study was to determine the efficacy of glutamine in promoting whole-body carbohydrate storage and muscle glycogen resynthesis during recovery from exhaustive exercise. Post-absorptive subjects completed a glycogen-depleting exercise protocol then consumed 330 ml of one of three drinks 18.5 % (w:v) glucose polymer solution, 8 g glutamine in 330 ml glucose polymer solution or 8 g glutamine in 330 ml placebo and also received a primed constant infusion of [1-13C]glucose for 2 h. Plasma glutamine concentration was increased after consumption of the glutamine drinks (0.7 mM to 1.1 mM, P < 0.05). In the second hour of recovery, whole body non -oxidative glucose disposal was increased by 25 % after consumption of glutamine in addition to the glucose polymer (4.48 +/- 0.61 vs 3.59 +/- 0.18 mmol.kg-1, P < 0.05).
    Oral glutamine alone promoted storage of muscle glycogen to an extent similar to glucose polymer. Ingestion of glutamine and glucose polymer together promoted the storage of carbohydrate outside of skeletal muscle, the most feasible site being the liver.
    Received 22 October 1977; accepted in final form 23 November
    1998.
    APS Manuscript Number A967-7.
    Article publication pending Journal of Applied Physiology.
    ISSN 1080-4757 Copyright 1998 The American Physiological Society.
    Published in APStracts on 18 December 1998

  20. Glutamine and the effects of exhaustive exercise upon the immune response.
    Castell LM, Newsholme EA.
    University Department of Biochemistry, Oxford, U.K. [email protected]
    There is a high incidence of infections in athletes undergoing intense, prolonged training or participating in endurance races (e.g., the marathon), in particular, upper respiratory tract infections. Prolonged, exhaustive exercise can lower the plasma level of the amino acid, glutamine, which is an important fuel for some cells of the immune system and may have specific immunostimulatory effects. This could therefore be an important factor in the event of an impaired response of immune cells to opportunistic infections. The effects of feeding glutamine to sedentary individuals and to marathon and ultramarathon runners before and after prolonged, exhaustive exercise has been investigated in a series of studies that monitored the incidence of infections and some acute-phase response markers.Oral glutamine, compared with a placebo, appeared to have a beneficial effect on the incidence of infections reported by runners after a marathon.
    Publication Types: Review
    Review, Tutorial

    PMID: 9839078 [PubMed - indexed for MEDLINE].

  21. Glutamine as an immunoenhancing nutrient.
    Saito H, Furukawa S, Matsuda T.
    Surgical Center, Faculty of Medicine, University of Tokyo, Japan.
    New strategies for immunonutritional support include administration of special nutrients such as glutamine. Glutamine is important in several key metabolic processes of immune cells and enterocytes. Exogenous glutamine augments the functions of lymphocytes and macrophages. Neutrophils also reportedly utilize glutamine at a significant rate. Our recent studies demonstrated that glutamine enhances neutrophil function. This article focuses on the effects of glutamine on neutrophil function in surgical stress. Enteral glutamine administration enhanced peritoneal and hepatic bacterial clearance in our rat peritonitis model. Furthermore, IV glutamine supplementation improved the outcome of animals with severe surgical stress. Our in vitro study revealed that supplemental glutamine augmented the bacterial killing function of neutrophils from postoperative patients. Glutamine increased phagocytosis of the neutrophils. In addition, glutamine dose-dependently increased production of reactive oxygen intermediates (ROI) by neutrophils. Thus, our studies suggest that glutamine supplementation may improve bactericidal function of neutrophils by increasing both phagocytosis and ROI production. In conclusion, glutamine plays an important role in neutrophil function.Glutamine may be useful for the prevention, and treatment, of severe infection in critical illness and trauma.
    Publication Types: Review
    Review, Tutorial

    PMID: 10483897 [PubMed - indexed for MEDLINE]

  22. You're posting repeat articles. None of which mean anything to a bodybuilder.

  23. Stimulatory effect of glutamine on glycogen accumulation in human skeletal muscle.
    Varnier M, Leese GP, Thompson J, Rennie MJ.
    Department of Anatomy and Physiology, University of Dundee, Scotland, United Kingdom.
    To determine whether glutamine can stimulate human muscle glycogen synthesis, we studied in groups of six subjects the effect after exercise of infusion of glutamine, alanine+glycine, or saline. The subjects cycled for 90 min at 70-140% maximal oxygen consumption to deplete muscle glycogen; then primed constant infusions of glutamine (30 mg/kg; 50 mg.kg-1.h-1) or an isonitrogenous, isoenergetic mixture of alanine+glycine or NaCl (0.9%) were administered. Muscle glutamine remained constant during saline infusion, decreased 18% during alanine+glycine infusion (P < 0.001), but rose 16% during glutamine infusion (P < 0.001). By 2 h after exercise, muscle glycogen concentration had increased more in the glutamine-infused group than in the saline or alanine+glycine controls (+2.8 +/- 0.6, +0.8 +/- 0.4, and +0.9 +/- 0.4 mumol/g wet wt, respectively, P < 0.05, glutamine vs. saline or alanine+glycine). Labeling of glycogen by tracer [U-13C]glucose was similar in glutamine and saline groups, suggesting no effect of glutamine on the fractional rate of blood glucose incorporation into glycogen.The results suggest that, after exercise, increased availability of glutamine promotes muscle glycogen accumulation by mechanisms possibly including diversion of glutamine carbon to glycogen.
    PMID: 7653548 [PubMed - indexed for MEDLINE]

  24. Another repeat article, which was refuted and dismissed above, but thanks for trying.

  25. The first abstract and the last one can be applied to a bodybuilder, the others are the way glutamine can possibly enhance the immune system YellowJacket.

  26. Originally posted by RaulJimenez
    The first abstract and the last one can be applied to a bodybuilder, the others are the way glutamine can possibly enhance the immune system YellowJacket.
    Yes and marathon runner and a bodybuilder are very comparable

    The second one is related to treatment of trauma victims. This was posted several times on various boards and soon deleted once everyone realizes a intense training weight lifter's immune system can not be compared to an AIDS patient or surgery victim, come on, you should know better than that.

  27. Yeah I know, I was doing some research on my own before coming to harsh YES and NO conclusions, and my conclusion from reading all those abstract I could find is that if you have the (money) to afford it then get it as insurance , if not then don't buy it , you get glutamine from supplements and food.

  28. Originally posted by RaulJimenez
    Yeah I know, I was doing some research on my own before coming to harsh YES and NO conclusions, and my conclusion from reading all those abstract I could find is that if you have the (money) to afford it then get it as insurance , if not then don't buy it , you get glutamine from supplements and food.
    Exactly what Im trying to prove. Food alone + a protein powder, you're getting more than enough.

  29. Yep , we agree on this matter now

  30. Originally posted by YellowJacket

    Yes and marathon runner and a bodybuilder are very comparable

    The second one is related to treatment of trauma victims. This was posted several times on various boards and soon deleted once everyone realizes a intense training weight lifter's immune system can not be compared to an AIDS patient or surgery victim, come on, you should know better than that.
    I am glad you noticed this as the only one of your articles that even mentions bodybuilders is # 2, and they state nothing conclusive, but that the data indicate that the short-term ingestion of glutamine does not enhance weightlifting performance in resistance-trained men. So what? No one takes it to increase performance OR increase carbohydrate metabolism or to boost the auto-immune system, but to prevent soft tissue injury. Since none of your studies has any relevance as pertains to the main use of glutamine in the bodybuilding community, that is, muscle tissue recovery, and only one even mentions weight lifters at all, the burden of proof is still on your shoulders. I find glutamine to be an important supp for muscle recovery, far more than mere placebo effect (nice try though)

    Most of the vets here see a real world difference in just protein vs protein+ glutamine.

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