Why glutamine is a waste

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I know some of you may have seen these studies and such on another board, but due to popular request, I will post some studies showing why glutamine is a waste of money

Let the games begin!

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Glutamine and Protein Synthesis — The other side of the coin

We've seen the theory that glutamine levels in the blood and muscle may decrease during or following exercise, and that this decrease correlates with reduced levels of protein synthesis. Several studies have addressed whether this relationship between glutamine and protein synthesis was a coincidental or a causal (meaning that one caused the other) relationship.

The first study compared the abilities of glutamine and the amino acid alanine to stimulate protein synthesis in rats with artificially reduced blood and muscle glutamine levels.(23) As expected, glutamine infusion increased intramuscular glutamine levels, while alanine didn't. Surprisingly, even depleting muscle glutamine levels by 60% had no effect on protein synthesis. What may also surprise you is that restoring blood and muscle glutamine levels to normal had no effect on protein synthesis compared to rats receiving no glutamine treatment! Additionally, even though whole body protein turnover didn't change, alanine stimulated protein synthesis!

In support of this contention, researchers studied the effect of glutamine supplementation on septic rats. Sepsis is a severely catabolic condition, during which glutamine levels (and protein synthesis) fall. Again, this study showed that despite increasing muscle glutamine levels to even higher than normal, it had no effect on protein synthesis or the catabolic state of the rats.(11)

Cumulatively, these studies show that decreased or increased levels of glutamine in the muscle has no effect on protein synthesis.

Another study, performed on people, examined the effect of adding glutamine to an amino acid mixture on muscle protein synthesis .(30) Ultimately, infusion of the original amino acid mixture increased protein synthesis by nearly 50%, but adding glutamine to this mix had no additional effect. This study is particularly relevant because most consumers of glutamine do so following a workout, along with other amino acids (or a whole protein).

Finally, Wusteman et al., used a drug to reduce muscle protein synthesis, along with muscle glutamine levels, in rats.(29) Much like the Olde Damink et al. study, restoring muscle glutamine levels to normal had no effect on protein synthesis. This study further supports the concept that blood and muscle glutamine levels have no bearing on protein synthesis and protein turnover.

Another One Bites the Dust

You may recall that the theory of exercise induced immunosuppression is often cited, based on the fact that glutamine levels decrease after exercise, as does our immunity.(10)

What we must now address is whether the relationship between the body’s glutamine stores and the effects of exercise on the immune system exhibit a causal or coincidental relationship (just as we did for protein synthesis). A recent review article in "The Journal of Applied Physiology" examined this connection between plasma glutamine and exercise-induced immunosuppression.(15)

The study admitted that there are conflicting reports about plasma glutamine levels following long duration exercise, repeated high intensity bouts, as well as short single high intensity bouts. This indicates that plasma glutamine concentrations may be affected differently depending on the intensity and duration of exercise.

Even data on blood glutamine concentrations following eccentric exercise is mixed, which can relate directly to bodybuilders and their use of heavy loads. Based on the relatively small reductions in plasma glutamine that might occur following exercise, supplementation with glutamine wouldn’t likely affect the immune cells.

More importantly, there are several studies showing that glutamine supplementation doesn't alter exercise-induced suppression of the immune system! The bottom line is that blood glutamine levels, whether they drop or not following exercise, don’t seem to affect immunity to any great extent, which precludes the use of glutamine for this reason.

Another recent review looked at over 75 research papers pertaining to the effect of glutamine on immunity and muscle growth, and came to the following conclusion: "Overall, although glutamine obviously plays important metabolic roles within the body, supplementation does not appear to provide consistent beneficial or therapeutic effects, except during certain catabolic situations. Glutamine availability, therefore, does not seem to be a limitation in many challenge situations."(19)

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What about the glycogen?

Yep, we have one final theory to validate spending God-awful amounts of money on glutamine; that of enhanced glycogen resynthesis following our workouts. In addition to the aforementioned studies showing better glycogen storage, there is also a study showing no effect of oral glutamine on glycogen regeneration following high intensity interval training.(26)

This issue was actually addressed by the authors of the Candow study, who found no strength or mass changes in trained individuals using glutamine (versus a placebo).(7) They suggested that the studies done showing enhanced glycogen recovery used exercise bouts which depleted intramuscular glycogen by 90%(!), while resistance exercise only depletes muscular glycogen by ~36%.

The bottom line is that the jury is still out on glutamine enhancing glycogen resynthesis following resistance exercise, but it seems unlikely that it would have any effect. Toss in the huge amounts of high glycemic carbs that most of us use following our workouts, and it’s almost a sure bet that glutamine won’t do anything for additional glycogen storage under normal dietary situations.

Things That Mom Never Told You About Glutamine Supplementation

It’s important to examine the method used for getting glutamine into the body in the human studies presented. Unfortunately, getting glutamine into our blood and to our muscles is a lot harder than one may expect. It was mentioned earlier that many cells of the body use glutamine for fuel. Well one area of cells that just loves glutamine is the gastrointestinal tract. In fact, it can account for up to 40% of glutamine utilization in the body! Now figure out the first area to come into contact with our "wonder supplement," and you can see that you have to take a whole crap-load of the stuff all at once, just so our gut doesn’t use it all!

Now, dumping 20g of one amino acid into our bodies at once may sound fun to some, but then again we can safely call these people masochists. For the rest of us, this huge glutamine dump may lead to some GI distress, which we all know is NOT fun.

Fortunately, the two studies performed with bodybuilders using relatively high dosages of glutamine (0.3g/kg/d and 0.9g/kg lean mass/d) reported no side effects of any kind.(2, 7) What is unfortunate is that the authors of these studies also showed no positive effect of any kind!

Glutamine and Resistance Trained Athletes: The Studies

One recent study examined the effect of acute glutamine ingestion on weightlifting performance.(2) This study examined the potential buffering effect of glutamine on lactic acid production during resistance exercise (to the point of momentary muscular failure).

One hour following glutamine ingestion (0.3g/kg), glycine ingestion (0.3g/kg), or placebo drink ingestion, the trained subjects performed 2 sets each of leg press (@ 200% body weight) and bench press (@ 100% body weight). This would equate to an average of ~23g of either amino acid ingested all at once, but there were no reports of GI discomfort.

Each subject consumed one of the three supplements before three separate testing sessions separated by a week. There was no effect of glutamine on number of reps performed compared to glycine or placebo ingestion. These results indicate that a high dose of glutamine ingested before exercise has no positive or negative effects on weightlifting performance in trained subjects.

If you’re interested in glutamine for its effect on muscle mass and strength, you’re in luck because a study was done on that, too! This next study is undoubtedly one of the best kept secrets in bodybuilding! In this study, the trained subjects consumed either 0.9g/kg lean body mass/day (average of 45g/day!), or a placebo, in 2 divided doses.(7)

It's noteworthy that using this amount of glutamine would run over 1200$USD per year for a 200lb guy!

By the end of the 6-week period, there were no differences in terms of 1Rep Max on squat or bench between the groups. There were also no differences between groups when it came to the gains in lean body mass (i.e. the amount of muscle they put on) during the trial period. This study was well designed and used the highest amount of glutamine ever studied for these purposes.

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Glutamine Ain't All That Bad

After kicking the crap out of glutamine for most bodybuilding purposes, it is important to realize that there are certain situations where glutamine can be useful.

A recent study from the journal "Metabolism" shows that glutamine injections following glucocorticoid (ie catabolic steroid -such as cortisol) treatment can increase protein synthesis in the gastrointestinal system of dogs.(16) Unfortunately, nonoxidative leucine disposal, a measure of whole-body protein synthesis, remained unchanged in the glutamine treated group.

There are a dozen ways you could interpret these findings, but at least we can say that glutamine supplementation may improve protein synthesis in some tissues following gluccocorticoid treatment. In fact, glucocorticoid treatment is one area where glutamine supplementation may really help!

Another study with rats supports this contention, again using corticosteroid administration.(14) Although glutamine infusion had no effect on muscle protein synthesis in the rats not receiving cortisol, there was a beneficial effect in the glucocorticoid treated rats. In fact, glutamine infusion actually attenuated more than 70% of the muscle wasting caused by the cortisol injections!

Along these lines, certain catabolic conditions (such as sepsis) may be another useful situation in which glutamine could help out. One literature review clearly concluded that "The increased intake of glutamine has resulted in lower septic morbidity in certain critically ill patient populations."(3) This means that people with certain catabolic medical conditions may live longer when taking glutamine. Keeping this in mind, we also know that AIDS can be associated with muscle wasting. Recent evidence has arisen to demonstrate that glutamine supplementation may attenuate AIDS-induced muscle wasting.(25)

Overall, these studies show that glutamine could be very helpful for muscle mass during corticosteroid treatment and certain wasting conditions. For those of you who think that your everyday training may be intense enough to simulate a catabolic condition, keep in mind that these people are dying because of their catabolism, so you're really no where near that level.

The only time a bodybuilder even remotely approaches these kind of catabolic conditions is when improperly coming off a cycle of anabolic steroids. In this situation the user has minimal anabolic stimulus from Testosterone and a large amount of cortisol just waiting to eat that muscle (again, this is only when done improperly). In this situation, glutamine supplementation might help, but it's not a situation you should be in anyway.

The other time that glutamine supplementation may be beneficial to bodybuilders is when on a low carbohydrate diet. Glutamine can not only be converted to glucose, but may also have an anapleurotic effect.(5) In other words, it may replenish metabolic intermediates, in this case, ATP (especially important when you're lacking carbs). This is another article unto itself, so I'll leave it at that for now.

You may be asking why you’ve never heard of most of these studies, and why everything you’ve heard about glutamine was always so amazing. I can indirectly answer that by reminding you of one simple fact: no one makes money by showing that supplements don’t work. I’ll leave the rest of the thinking on this matter to you.

Despite this, you may still be skeptical regarding the points mentioned, based on the original dogmatic theories associated with glutamine use (and how long you’ve been hit over the head with them). But then again, that’s why they’re just theories. To paraphrase Homer Simpson: "Sure it may work in theory, but then again even communism works...in theory."

It's the mark of a great person who can devise a theory, drawing from many different ideas, and stick to it. Without this, science would be meaningless. But it's the mark of an even greater person when they can admit, without shame, that their idea is wrong.

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Sometimes theories pan out and sometimes they don’t, but we have to be able to let go of them once they're shown to be incorrect. This doesn’t mean that we shouldn’t believe new theories when they first come out; it just means that we have to be conscious about the fact that they aren’t dogma and may be wrong.

Case in point: The theory behind glutamine was so great that I refused to believe the authors of the Candow et al. (2001) study when they told me the results in person. I was an educated bodybuilder and I wasn’t going to let some egghead scientist (who was actually more muscular than I was, and therefore far from being just an "egghead") tell me that I was wrong. Of course, I wanted to believe that glutamine was useful (even though I got nothing from it) and when someone wants to believe something you can’t convince them otherwise.

Since then I’ve had a while to let the results sink in. I know that most believers in glutamine will also have a hard time accepting the reality of the situation, which is why I didn’t just try to convincingly show that glutamine wasn’t as great as everyone thought; I tried to overwhelmingly demonstrate it.

Bottom Line

Glutamine is good for hospital patients and rich people with money to waste. If you’re involved in resistance training and already have proper post workout nutrition, along with a moderate carb intake, then glutamine probably won’t do anything for you. In fact, none of the proposed theories dealing with glutamine supplementation have worked out in the athletic world. It’s also one of the most expensive supplements around (simply based on dosage recommendations), so it’s way too costly to use for personal experimentation — especially when the updated scientific literature doesn’t support the theories.

References:

1. Antonio J, Street C.

Glutamine: a potentially useful supplement for athletes. Can J Appl Physiol 1999 Feb;24(1):1-14

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

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

3. Boelens PG, Nijveldt RJ, Houdijk AP, Meijer S, van Leeuwen PA.

Glutamine alimentation in catabolic state. J Nutr 2001 Sep;131(9 Suppl):2569S-77S; discussion 2590S

4. Bowtell JL, Gelly K, Jackman ML, Patel A, Simeoni M, Rennie MJ.

Effect of oral glutamine on whole body carbohydrate storage during recovery from exhaustive exercise. J Appl Physiol 1999 Jun;86(6):1770-7

5. Bruce M, Constantin-Teodosiu D, Greenhaff PL, Boobis LH, Williams C, Bowtell JL.

Glutamine supplementation promotes anaplerosis but not oxidative energy delivery in human skeletal muscle. Am J Physiol Endocrinol Metab 2001 Apr;280(4):E669-75

6. Bush JA, Dohi K, Mastro AM, Volek J, Lynch JM, Triplett-McBride, Putukian M, Sebastianelli WJ, Newton RU, Hakkinen K, Kraemer WJ. Exercise and recovery responses of lymphokines to heavy resistance exercise J Str Cond Res 2000 14(3) 344-349

7. Candow DG, Chilibeck PD, Burke DG, Davison KS, Smith-Palmer T.

Effect of glutamine supplementation combined with resistance training in young adults. Eur J Appl Physiol 2001 Dec;86(2):142-9

8. Castell LM, Poortmans JR, Newsholme EA.

Does glutamine have a role in reducing infections in athletes? Eur J Appl Physiol Occup Physiol 1996;73(5):488-90

9. Castell LM, Newsholme EA.

The effects of oral glutamine supplementation on athletes after prolonged, exhaustive exercise. Nutrition 1997 Jul-Aug;13(7-8):738-42

10. Castell LM.

Can glutamine modify the apparent immunodepression observed after prolonged, exhaustive exercise? Nutrition 2002 May;18(5):371-5

11. Fang CH, James JH, Fischer JE, Hasselgren PO.

Is muscle protein turnover regulated by intracellular glutamine during sepsis? JPEN J Parenter Enteral Nutr 1995 Jul-Aug;19(4):279-85

12. Hammarqvist F, Wernerman J, von der Decken A, Vinnars E.

Alanyl-glutamine counteracts the depletion of free glutamine and the postoperative decline in protein synthesis in skeletal muscle. Ann Surg 1990 Nov;212(5):637-44

13. Hankard RG, Haymond MW, Darmaun D.

Effect of glutamine on leucine metabolism in humans. Am J Physiol 1996 Oct;271(4 Pt 1):E748-54

14. Hickson RC, Czerwinski SM, Wegrzyn LE.

Glutamine prevents downregulation of myosin heavy chain synthesis and muscle atrophy from glucocorticoids. Am J Physiol 1995 Apr;268(4 Pt 1):E730-4

15. Hiscock N, Pedersen BK.

Exercise-induced immunodepression- plasma glutamine is not the link. J Appl Physiol 2002 Sep;93(3):813-22

16. Humbert B, Nguyen P, Dumon H, Deschamps JY, Darmaun D.

Does enteral glutamine modulate whole-body leucine kinetics in hypercatabolic dogs in a fed state? Metabolism 2002 May;51(5):628-35

17. Jepson MM, Bates PC, Broadbent P, Pell JM, Millward DJ.

Relationship between glutamine concentration and protein synthesis in rat skeletal muscle. Am J Physiol 1988 Aug;255(2 Pt 1):E166-72

18. Lacey JM, Wilmore DW.

Is glutamine a conditionally essential amino acid? Nutr Rev 1990 Aug;48(8):297-309

19. Lobley GE, Hoskin SO, McNeil CJ.

Glutamine in animal science and production. J Nutr 2001 Sep;131(9 Suppl):2525S-31S; discussion 2532S-4S

20. Low SY, Taylor PM, Rennie MJ.

Responses of glutamine transport in cultured rat skeletal muscle to osmotically induced changes in cell volume. J Physiol 1996 May 1;492 ( Pt 3):877-85

21. 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 May 4;215(1):187-91

22. MacLennan PA, Smith K, Weryk B, Watt PW, Rennie MJ.

Inhibition of protein breakdown by glutamine in perfused rat skeletal muscle. FEBS Lett 1988 Sep 12;237(1-2):133-6

23. Olde Damink SW, de Blaauw I, Deutz NE, Soeters PB.

Effects in vivo of decreased plasma and intracellular muscle glutamine concentration on whole-body and hindquarter protein kinetics in rats. Clin Sci (Lond) 1999 Jun;96(6):639-46

24. Petersson B, von der Decken A, Vinnars E, Wernerman J.

Long-term effects of postoperative total parenteral nutrition supplemented with glycylglutamine on subjective fatigue and muscle protein synthesis. Br J Surg 1994 Oct;81(10):1520-3

25. Shabert JK, Winslow C, Lacey JM, Wilmore DW.

Glutamine-antioxidant supplementation increases body cell mass in AIDS patients with weight loss: a randomized, double-blind controlled trial. Nutrition 1999 Nov-Dec;15(11-12):860-4

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

The effect of free glutamine and peptide ingestion on the rate of muscle glycogen resynthesis in man. Int J Sports Med 2000 Jan;21(1):25-30

27. Varnier M, Leese GP, Thompson J, Rennie MJ.

Stimulatory effect of glutamine on glycogen accumulation in human skeletal muscle. Am J Physiol 1995 Aug;269(2 Pt 1):E309-15

28. Vom Dahl S, Haussinger D.

Nutritional state and the swelling-induced inhibition of proteolysis in perfused rat liver. J Nutr 1996 Feb;126(2):395-402

29. Wusteman M, Tate H, Elia M.

The use of a constant infusion of [3H]phenylalanine to measure the effects of glutamine infusions on muscle protein synthesis in rats given turpentine. Nutrition 1995 Jan-Feb;11(1):27-31

30. Zachwieja JJ, Witt TL, Yarasheski KE.

Intravenous glutamine does not stimulate mixed muscle protein synthesis in healthy young men and women. Metabolism 2000 Dec;49(12):1555-60

31. Zorzano A, Fandos C, Palacin M.

Role of plasma membrane transporters in muscle metabolism. Biochem J 2000 Aug 1;349 Pt 3:667-88

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From Patrick Arnold, a leading industry expert, Who has a B.S. in Chemistry from the University of New Haven, Owner of Ergopharm, and vice-president of Proviant Technologies Inc.

"fooling around with glutamine is a waste of time, unless you are sick or very weakened"


"compare the differences in physiological response to exercise with essential amino acids, or even just branch chain amino acids, to glutamine. we are talking very impressive responses compared to nothing

yet people reach for the bottle of glutamine first

dumbassess

seriously, its time someone cleaned house"

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From Lok7y, a representative of Avant Labs

"Glutamine is a waste of money--really unnecessary IMHO"

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More studies...


Muscle glutamine depletion in the intensive care unit

Gianni Biolo, , Francesca Zorat, Raffaella Antonione and Beniamino Ciocchi

Department of Clinical, Morphological and Technological Sciences, University of Trieste, Trieste, Italy

Received 28 October 2004; revised 3 May 2005; accepted 4 May 2005. Available online 31 May 2005.




Abstract
Glutamine is primarily synthesized in skeletal muscle and enables transfer of nitrogen to splanchnic tissues, kidneys and immune system. Discrepancy between increasing rates of glutamine utilization at whole body level and relative impairment of de novo synthesis in skeletal muscle leads to systemic glutamine deficiency and characterizes critical illness. Glutamine depletion at whole body level may contribute to gut, liver and immune system disfunctions, whereas its intramuscular deficiency may directly contribute to lean body mass loss. Severe intramuscular glutamine depletion also develops because of outward transport system upregulation, which is not counteracted by increased de novo synthesis. The negative impact of systemic glutamine depletion on critically ill patients is suggested both by the association between a lower plasma glutamine concentration and poor outcome and by a clear clinical benefit after glutamine supplementation. Enteral glutamine administration preferentially increases glutamine disposal in splanchnic tissues, whereas parenteral supplementation provides glutamine to the whole organism. Nonetheless, systemic administration was ineffective in preventing muscle depletion, due to a relative inability of skeletal muscle to seize glutamine from the bloodstream. Intramuscular glutamine depletion could be potentially counteracted by promoting de novo glutamine synthesis with pharmacological or nutritional interventions.

Keywords: Glutamine; Kinetics; Skeletal muscle; Critical illness


Article Outline
1. Introduction
2. Inter-organ glutamine kinetics
2.1. Glutamine appearance
2.2. Storage in skeletal muscle
2.3. Transmembrane glutamine transport
2.4. Splanchnic metabolism of dietary glutamine
2.5. Whole body glutamine utilization
3. Regulation of muscle glutamine synthesis
4. Systemic and muscle glutamine depletion in critical illness
5. Clinical consequences of glutamine depletion
6. Glutamine supplementation
References


1. Introduction
Following tissue injury or severe infections, critically ill patients experience metabolic alterations leading to muscle proteolysis activation, enhanced liver gluconeogenesis and tissue insulin resistance (Griffiths, 2003). In addition, these patients exhibit marked reductions in plasma and tissue concentrations of glutamine, the most abundant free amino acid in body compartments (Melis, ter Wengel, Boelens, & van Leeuwen, 2004). Glutamine is primarily synthesized in skeletal muscle and enables transfer of nitrogen to splanchnic tissues, kidneys and immune system. Furthermore, glutamine plays a regulatory role in several specific cell processes. In critically ill patients, glutamine depletion is proportional to severity of illness (Oudemans-van Straaten, Bosman, Treskes, van der Spoel, & Zandstra, 2001) and is not readily reversible by nutrition or other therapeutical approaches (Tjader et al., 2004). Evidence indicates that supplementation with exogenous glutamine in order to enhance its inter-organ flux is often associated with improved outcome of patients (Novak, Heyland, Avenell, Drover, & Su, 2002). In this paper, we will review recent data on glutamine metabolism both in health and disease states, aiming at defining kinetic mechanisms that lead to glutamine depletion.

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2. Inter-organ glutamine kinetics
2.1. Glutamine appearance
Tracer kinetic studies in normal volunteers indicate that approximately 90 g of glutamine appear every day in the bloodstream, 80 g from body tissues and 10 g from nutrient intake (Biolo, Fleming, Maggi, & Wolfe, 1995) (Fig. 1). Thus, approximately one-third of all nitrogen derived from protein metabolism is transported in the form of glutamine. The bulk of glutamine entering plasma is derived from skeletal muscle (Biolo et al., 1995). All together, lung, liver and adipose tissue do not therefore account for more than 50% of whole body glutamine appearance. Lung glutamine release has been directly assessed in humans by determining the pulmonary artero-systemic arterial concentration difference with the Fick principle (Herskowitz et al., 1991). Relatively healthy subjects were studied before elective surgery to determine lung glutamine exchange (Herskowitz et al., 1991). In these conditions, lung glutamine release appeared to be lower than that observed in skeletal muscle in a different study (Biolo et al., 1995). When turnover of free glutamine was assessed in muscle (Fig. 1), the rate of appearance in cell cytoplasm was three times greater than its release into the bloodstream (Biolo et al., 1995). Glutamine de novo synthesis accounted for 85% of intramuscular appearance, whereas only 15% of the intracellular amino acid was derived from proteolysis (Biolo et al., 1995).


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Fig. 1. Body glutamine kinetics assessed by stable isotopes in physiological conditions, numerical data are calculated from Biolo et al. (1995). CNS, central nervous system; GABA, gamma-aminobutyric acid.



2.2. Storage in skeletal muscle
In skeletal muscle, after de novo synthesis, free glutamine is largely stored in the cytoplasm. In muscle, glutamine is the most abundant free amino acid: its concentration is infact 50–200 times greater than that of the all essential amino acids (Biolo et al., 1995). In physiological conditions, intramuscular free glutamine concentrations range from 10 to 20 mmol/l of tissue water. Thus, this amino acid significantly contributes to total cell osmolarity and hydration (Haussinger, Roth, Lang, & Gerok, 1993). Osmo-sensing structures located inside cells, allow transduction of information depending on the extent of cell hydration, and therefore, allow enzyme activity and gene expression modifications. Indeed, through this mechanism, changes in glutamine muscle cell concentrations may directly regulate protein synthesis and degradation (Table 1), since cell swelling and shrinking are major anabolic and catabolic signals, respectively (Haussinger, Graf, & Weiergraber, 2001). The difference between intracellular and interstitial concentrations of glutamine is determinant of muscle cell hydration. Such transmembrane concentration gradient is largely dependent on cell membrane transport system activity.

Table 1.

Organ-specific regulative potential of glutamine Immune cells
Nucleotide synthesis precursor
Fuel for proliferating immune cells
Modulation of cytokine secretion
Enhances T-lymphocyte response
Synthesis of immunoglobulins A
Modulation of heat shock proteins
Attenuation of NO formation
Supports neutrophil and macrophage functions
Gastrointestinal tract
Nucleotide synthesis precursor
Fuel for proliferating enterocytes
Maintenance of gut-associated lymphoid tissue
Maintenance of gut barrier
Modulation of heat shock proteins
Attenuation of NO formation
Liver
Substrate for ureagenesis
Gluconeogenetic precursor
Glutathione synthesis (antioxidant)
Osmotic signaling mechanism in regulation of protein synthesis and degradation
Precursor of taurine
Modulation of heat shock proteins
Attenuation of NO formation
Precursor of taurine
Kidney
Substrate for renal gluconeogenesis
Acid/base regulation
Ammoniogenesis
Skeletal muscle
Ammonia scavenger
Nitrogen transport (one third of circulating nitrogen)
Osmotic signaling in regulation of protein synthesis and degradation
Lung
Fuel for proliferating endothelial cells
Nitrogen transport
Modulation of heat shock proteins
Central nervous system
Shuttle for glutamate
GABA synthesis


NO, nitric oxide; GABA, gamma-aminobutyric acid.




2.3. Transmembrane glutamine transport
In physiological conditions, transport systems maintain a large transmembrane gradient because intracellular glutamine concentration is 25–30 times greater than extracellular values. Several glutamine transporters have been described in human skeletal muscle (Bode, 2001). Na+-dependent glutamine transporters include ASC, B0,+, y1L, A and N systems, while Na+-independent transporters include L, b0,+ and n systems. Every glutamine transporter exhibits overlapping affinity for the transport of several other amino acids. Transmembrane Na+ electrochemical gradient, maintained by the Na+/K+-ATPase, drives the uptake of amino acids against their concentration gradient through Na+-dependent transporters. This accounts for the maintenance of glutamine cytoplasmatic levels above their transmembrane equilibrium distribution (Bode, 2001).

By utilizing a new technique based on amino acid isotopic tracers in combination with the leg artero-venous technique and muscle biopsies, we were able to determine the bi-directional kinetics of membrane amino acid transport in humans (Biolo et al., 1995). We found that the relative inward transmembrane transport contribution to the intracellular turnover rate of each individual free amino acid was extremely variable. Transport from blood accounted for only 25% of the intramuscular glutamine pool turnover. In contrast, the intracellular pools of most essential amino acids, such as phenylalanine or leucine, derived largely from the extracellular space. Thus, exogenous administration of amino acids that are readily taken up by membrane transport systems will rapidly lead to increases in their intracellular concentration, while free glutamine intracellular concentration will only change slowly after exogenous supplementation (Hammarqvist, Wernerman, Ali, von der Decken, & Vinnars, 1989; Petersson, Waller, Vinnars, & Wernerman, 1994; Tjader et al., 2004).

Transmembrane amino acid transport systems have been mostly investigated focusing on their inward direction activity. Nonetheless, evidence indicates that skeletal muscle is, in all circumstances, a net exporter of glutamine (Ahmed, Peter, Taylor, Harper, & Rennie, 1995). We may predict, therefore, that outward transport systems may play an important role in the inter-organ glutamine exchange regulation. In the last years, attention was focused on the role of system N in the regulation of glutamine efflux from skeletal muscle to the bloodstream (Bode, 2001). In a previous study, we investigated the outward transport kinetics of different amino acids (Biolo et al., 1995). Outward transport rates were normalized per unit of intracellular concentration of free amino acids in order to express the ability of outward transporters to release amino acids at any given concentration. Glutamine outward transport activity of was 30–40 times lower than leucine and phenylalanine and almost eight times lower than lysine. Such relative inability of skeletal muscle to release free glutamine explains its large transmembrane gradient.

It is now evident that several factors may regulate system N activity. Cytokines, cortisol and other hormones activate this transport system in vitro (Watkins, Dudrick, Copeland, & Souba, 1994). In addition, system N-mediated glutamine transport is highly dependent on membrane electrical potential: its progressive depolarization within physiologic ranges results in a switch from glutamine uptake to glutamine release (Fei et al., 2000). Experimental evidence indicates that there is an early transmembrane potential decrease in skeletal muscle during sepsis and after trauma, possibly due to the action of a high molecular weight circulating plasma protein complex (Button et al., 2001). Critically ill patients are characterized by reduced ability to generate action potentials in muscle fibers, and this often leads to a well defined clinical myopathy (Rich & Pinter, 2003). Thus, upregulation of outward transport systems by humoral factors or electrical transmembrane potential changes may play a key role in the rapid mobilization of muscle free glutamine large reservoirs, leading to the release of the amino acid into the bloodstream when its requirements increase in tissues other than skeletal muscle.

2.4. Splanchnic metabolism of dietary glutamine
Glutamine accounts for about 8–12% of total amino acid content of dietary proteins. The total oral intake and absorption of the free amino acid is, therefore, about 10 g per day, but this represents only 12% of the whole body glutamine appearance (Fig. 1). In addition, systemic availability of enteral glutamine is further reduced by first pass splanchnic metabolism. Studies involving oral ingestion of stable isotope-labelled glutamine indicate that 50–70% of enterally administered glutamine is taken up during first pass by splanchnic organs (gut and liver) (Matthews, Marano, & Campbell, 1993) where it is largely oxidized (Haisch, Fukagawa, & Matthews, 2000). Thus, kinetic data indicate that whole body glutamine availability largely depends on the rate of endogenous synthesis in skeletal muscle.

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2.5. Whole body glutamine utilization
In physiological conditions, approximately 90 g of glutamine appear daily in the bloodstream. Eighty grams are derived from endogenous sources, mainly skeletal muscle and lung, whereas 10 g are deriving from oral intake. Thereafter, circulating glutamine is preferentially taken up by liver, kidneys, gut mucosa, central nervous system and immune cells (Fig. 1). Evidence indicates that these tissues utilize glutamine at high rates and that glutamine utilization is essential for their function (Table 1) (Newsholme, Procopio, Lima, Pithon-Curi, & Curi, 2003). Glutamine tracer kinetic studies (Perriello et al., 1997) indicate that 40–60% of plasma glutamine disappearance is due to oxidation, 10–20% to gluconeogenesis and most of the remainder to protein synthesis and incorporation into macromolecules. The immediate product of glutamine metabolism is glutamate, generated by the glutaminase enzyme (Fig. 2). Glutamine and glutamate are precursors of many compounds, including hepatic and renal glucose, urinary ammonia, intracellular glutathione, nitric oxide and nucleic acids (Fig. 2; Table 1). Furthermore, glutamine is a major fuel for rapidly dividing cells of intestinal mucosa and immune system (Table 1) (Newsholme et al., 2003). We may predict, therefore, that in pathological conditions characterized by activation of immune system, gut dysfunction, increased oxidative stress or metabolic acidosis, glutamine requirements and disposal may be increased (Newsholme, 2001). Kinetic studies in critically ill patients have shown that whole body glutamine disposal is increased both in absolute terms (Gore & Jahoor, 1994) and as metabolic amino acid clearance rate (i.e., rate of disposal divided by the prevailing glutamine concentration in plasma) (Jackson et al., 1999).


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Fig. 2. Overview of glutamine and glutamate metabolism. Glutamate is produced from glutamine through glutaminase activity. Glutamate can be converted into glutamine through glutamine synthetase activity. TCA, tricarboxylic acid; GABA, gamma-aminobutyric acid.



3. Regulation of muscle glutamine synthesis
The described kinetic studies indicate that skeletal muscle is the main site of glutamine production and release because of its large free glutamine pool and its capacity for de novo synthesis. Immediate precursors of glutamine synthesis are glutamate and free ammonia (Fig. 2); the process is catalyzed by glutamine synthetase. Glutamate is synthesized by transamination of the branched chain amino acids leucine, isoleucine and valine, which are extensively decarboxylated in skeletal muscle. In this reaction, the branched chain amino acids react with α-ketoglutarate to produce α-ketoacids and glutamate in presence of the branched chain amino acid aminotransaminase enzyme. We may, therefore, predict that muscle glutamine synthesis does not only require intramuscular availability of branched chain amino acids for transamination but also an adequate flux of energy substrates through the pyruvate dehydrogenase and the tricarboxylic acid cycle as well as an adequate source of carbon skeletons. Several lines of evidence support the key role of these regulatory mechanisms for glutamine synthesis in vivo. First, studies using infusion of leucine, labelled with nitrogen stable isotopes, demonstrated direct tracer incorporation into glutamine (Darmaun & Dechelotte, 1991). Second, in contrast to most amino acids, glutamine release from skeletal muscle is not decreased in the postprandial state: enteral and parenteral nutrient administration infact lead to significant stimulation of glutamine de novo synthesis (Darmaun et al., 1994). Third, when dicholoracetate, a potent activator of the pyruvate dehydrogenase complex through inhibition of the pyruvate dehydrogenase kinase, was infused in burnt patients, muscle glutamine concentrations increased significantly (Ferrando et al., 1998). Fourth, hyperinsulinemia, in combination with glucose infusion to maintain euglycemia, increased muscle glucose uptake with subsequent conversion to glutamine and accelerated release of the amino acid (Meyer, Woerle, & Gerich, 2004). Finally, supplementation with α-ketoglutarate was able to increase muscle free glutamine (Hammarqvist, Wernerman, von der Decken, & Vinnars, 1991). Glutamine synthesis is also regulated by glutamine synthetase activity. Hormones and substrates may directly modulate enzyme activity through transcriptional and post-transcriptional mechanisms. Glucocorticoids can up-regulate glutamine synthetase mRNA levels in muscle cells through a glucocorticoid receptor-dependent process (Max et al., 1987). In vivo, glutamine synthetase mRNA levels can increase roughly 10-fold in response to glucocorticoid administration (Max et al., 1988). In healthy humans, physiological elevations of plasma cortisol levels lead to significant stimulation of glutamine production, primarily because of an increase in glutamine de novo synthesis (Darmaun, Matthews, & Bier, 1988). Growth hormone may also potentially increase the glutamine synthetase gene expression (Nolan, Masters, & Dunn, 1990). Nonetheless, we recently found that the rate of glutamine release from leg muscle decreased after administration of growth hormone to trauma patients despite the increased enzyme gene expression (Biolo, Iscra et al., 2000). Also catecholamines are indeed important regulators of glutamine production. Effects on glutamine metabolism were studied in isolated skeletal muscle. Physiological levels of epinephrine reduced glutamine formation and release from skeletal muscle, via a beta-adrenergic receptor pathway and the adenylate cyclase system (Nie, Wallberg-Henriksson, Johansson, & Henriksson, 1989). In addition to these hormone-dependent effects, glutamine synthetase expression is directly induced in rat skeletal muscle cells by treatment with inflammatory cytokines, such as tumor necrosis factor alpha and interleukin-1 beta (Huang & O’Banion, 1998). Glutamine synthetase activity is also directly regulated by glutamine concentrations through a post-transcriptional mechanism that increases enzyme activity when tissue glutamine levels are low (Feng, Shiber, & Max, 1990).

Levels of physical activity may also directly regulate muscle glutamine production. During exercise, substrate flux through the TCA and branched chain amino acid oxidation greatly increases (Gibala, MacLean, Graham, & Saltin, 1998). Glutamine synthesis and release are, therefore, significantly stimulated (Van Hall, Saltin, & Wagenmakers, 1999) leading to increased plasma glutamine concentrations, as observed following short-term moderate exercise or during endurance training (Hood & Terjung, 1994). Glutamine concentrations increase despite the fact that exercise in rats decreases the activity of glutamine synthetase and prevents glucocorticoid-mediated enzyme induction (Falduto, Young, & Hickson, 1992). These results suggest that after exercise, as after growth hormone administration, glutamine synthesis regulation by precursor availability may overcome the effects of changes in glutamine synthetase expression or activity. Glutamine concentration is decreased after prolonged, exhaustive training, in contrast to moderate exercise, possibly due to increased glutamine demand as a consequence of immune system activation (Rowbottom, Keast, & Morton, 1996). Athletes with overtraining syndrome also have low plasma glutamine. Glutamine levels remain low even after several weeks of rest (Hiscock & Mackinnon, 1998). It has been hypothesized that there could be a link between exercise-mediated changes in glutamine metabolism and the epidemiological data showing that athletes are at increased risk for upper respiratory tract infections during periods of heavy training and following race events (Nieman, 1997). In contrast to physical exercise, the effects of immobility on glutamine metabolism have been poorly investigated. In animal models of muscle unloading or denervation, glutamine synthesis rates and intracellular levels are decreased, despite a greater activity of glutamine synthetase (Feng, Konagaya et al., 1990; Jaspers, Jacob, & Tischler, 1986). In addition, rats exposed to 7 days of weightlessness during the Spacelab-3 shuttle flight exhibited decreased muscle levels of free glutamine (Steffen & Musacchia, 1986). In agreement with these animal studies, in a recent short-term bed rest study in normal volunteers (Biolo et al., 2004), we observed that de novo glutamine synthesis rate at the whole body level significantly decreased by about 10% following 15 days of muscle unloading (Biolo et al., unpublished). Previous evidence indicates that during muscle unloading, activities of the tricarboxylic acid cycle enzymes are reduced in both animals and humans (Berg, Dudley, Hather, & Tesch, 1993). This alteration may lead to decreased glutamate and glutamine synthesis.

[Trans_Isomer]

4. Systemic and muscle glutamine depletion in critical illness
Critical illness is characterized by increased production of cytokines and stress hormones, such as glucocorticoids and catecholamines. These mediators interact with bed rest and, possibly, with hyponutrition to produce a cluster of metabolic abnormalities such as muscle wasting, insulin resistance and glutamine kinetic alterations. Systemic glutamine depletion results from discrepancies between rates of skeletal muscle release and uptake in other tissues. In addition, severe intramuscular glutamine depletion develops because transport systems upregulation, accelerating outflux from muscle, is not adequately matched by an increase in de novo synthesis. Muscle and plasma glutamine concentrations decrease proportionally to severity of diseases. In addition, the ratio between muscle cells and plasma glutamine concentrations decreases progressively from physiological values of 20–30 to values of 10–15 in more severe conditions (Biolo, Fleming et al., 2000; Flaring, Rooyackers, Wernerman, & Hammarqvist, 2003; Wernerman, 2003), clearly showing an upregulation of outward transport systems. Regarding muscle glutamine production, critical illness may be associated with either increased or decreased de novo synthesis. While tumor necrosis factor-alpha directly induces glutamine synthetase, the two major stress hormones, cortisol and epinephrine, have opposite effects on its synthesis. In addition, bed rest and hyponutrition may further decrease glutamine synthesis. In a recent study, we have determined, in skeletal muscle and during the post-absorptive state, glutamine synthesis de novo rate both in normal controls and in patients with severe burns during the “flow” phase after injury. We found that in burn patients, muscle glutamine synthesis was 50% lower than in healthy controls (Biolo, Fleming et al., 2000). Nonetheless, glutamine appearance rate was found either decreased (Jackson et al., 1999) or accelerated (Gore & Jahoor, 1994) when determined by stable isotopes at the whole body level. We may, therefore, speculate that, while glutamine synthesis is suppressed in muscle, it may be accelerated in other tissues. Evidence indicates infact that in lungs, glutamine synthesis is greatly accelerated after surgical stress (Herskowitz et al., 1991).

5. Clinical consequences of glutamine depletion
Glutamine depletion at whole body level may impair physiological functions of gut, liver and immune system (Newsholme et al., 2003), whereas intramuscular glutamine depletion may directly contribute to lean body mass wasting (Jepson, Bates, Broadbent, Pell, & Millward, 1988) (Table 1) and delayed recovery from illness.

6. Glutamine supplementation
Critical illness is characterized by increased glutamine utilization leading to depletion of the amino acid. Nonetheless, standard nutrition support solutions contain none (standard parenteral formulas) or very little glutamine (polymeric casein-derived enteral formulas). A lower plasma glutamine concentration (i.e., <0.420 mmol/l) is associated with a higher ICU mortality (60% versus 29%), supporting the hypothesis of a negative impact of glutamine depletion on clinical outcome of critically ill patients (Oudemans-van Straaten et al., 2001). In addition, there is evidence for a clear clinical benefit of glutamine supplementation in critically ill patients. A recent meta-analysis evaluated six randomized studies on glutamine supplementation in serious illness (Novak et al., 2002). The authors conclude that glutamine supplementation is associated with a strong trend toward a reduction in mortality, a lower infectious complication rate and a shorter hospitalization. More recently, four other randomized trials have been published. The results of the ten studies are summarized in Table 2 (Brantley & Pierce, 2000; Conejero et al., 2002, Garrel et al., 2003 and Goeters et al., 2002; Griffiths, Jones, & Palmer, 1997; Hall et al., 2003 and Houdijk et al., 1998; Jones, Palmer, & Griffiths, 1999; Powell-Tuck et al., 1999 and Wischmeyer et al., 2001). These studies show that survival is improved by glutamine supplementation only in high mortality rate settings. The effective daily supplementation dose ranged from 20 to 40 g. These glutamine administration rates approximately match the extent of the decrease in muscle glutamine de novo synthesis observed in burn patients (Biolo, Fleming et al., 2000). There is clear evidence that both enteral or parenteral supplementation can be effective in counteracting the systemic depletion glutamine. Enteral glutamine administration preferentially increases glutamine disposal in splanchnic tissues, whereas parenteral supplementation provides glutamine to the whole organism.
Glutamine supplementation was mostly ineffective in preventing muscle glutamine depletion in critically ill patients, because of the relative inability of this tissue in the uptake of the circulating amino acid. Intramuscular glutamine depletion should, therefore, be preferentially counteracted by promoting de novo glutamine synthesis. Clinical studies have shown that stimulation of pyruvate oxidation by dichloroacetate administration in burnt patients (Ferrando et al., 1998) and supplementation of ketoglutarate in post-surgical patients (Hammarqvist et al., 1991) may improve glutamine synthesis in skeletal muscle. In addition, branched chain amino acid administration may affect de novo muscle glutamine production rate by increasing nitrogen availability for ketoglutarate transamination (Darmaun & Dechelotte, 1991).

[Trans_Isomer]

How many studies like this have to come out before you people stop wasting your money?

The purpose was to determine if glutamine supplementation would prevent a loss of lean mass in athletes during a 12-day weight reduction program. It was hypothesized that supplementation would spare lean body mass. Subjects (n=18) exercised and dieted to create a 4186kJ·day-1 energy deficit and a 8372 kJ·day-1 energy deficit on days 1-5, days 6-12, respectively. The glutamine (GLN) group (n=9) ingested 0.35 g·kg-1 body mass of glutamine while a placebo was administered to the remaining subjects. Body mass (BM), lean body mass (LBM) and fat mass (FM), were measured at days 0, 6, and 12. GLN and placebo groups both lost significant amounts of BM, LBM and FM. There were no significant differences between groups. The findings indicate little benefit for retention of lean mass with supplementation of glutamine during a short-term weight reduction program.

Glutamine supplementation did not benefit athletes during short-term
weight reduction

Kevin, J. Finn, Robin Lund and Mona Rosene-Treadwell
http://www20.uludag.edu.tr/%7Ehakan/...4/7/v2n4-7.htm

[Trans_Isomer]

From the "Beast" Darek Charlebois'


"Just some anecdotal findings...

I used to be big on Glutmine 30-40 grams a day (Pre & Post Workout and before bed). For the past month, I have not used any glutamine. This week, I hit my new PRs with 400 X 4 on Squat and 500 X 2 on Deadlift. I have not noticed any decline in recovery or performance since I stopped taking Glutamine..."

[Trans_Isomer]

Borrowed from "Big'r"

Glutamine production in muscle protein is 50% lower than assumed

-Results of tracer studies indicate that skeletal muscle contributes to approximately 70% of overall glutamine production in healthy adults; the contribution of de novo synthesis being estimated at approximately 60%. Direct and specific measurements of glutamine in intact muscle protein are 50% lower than assumed previously (G1).

Most amino acids are precursors for alanine and glutamine synthesis in skeletal muscle

-Cysteine, leucine, valine, methionine, isoleucine, tyrosine, lysine, and phenylalanine increase the rate of glutamine synthesis. The progressive decline in alanine and glutamine synthesis noted on prolonged incubation is prevented by the addition of amino acids to the incubation medium (G2)

90% of the glutamine you take orally never even makes it to your muscles. Glutamine supplementation decreases it's own synthesis and mostly turns itself into glucose.

-Systemic glutamine administration is ineffective in preventing muscle depletion, due to a relative inability of skeletal muscle to seize glutamine from the bloodstream. Transport from blood accounts for only 25% of the intramuscular glutamine pool turnover. In contrast, the intracellular pools of most essential amino acids, such as phenylalanine or leucine, derived largely from the extracellular space. Studies involving oral ingestion of stable isotope-labelled glutamine indicate that 50-70% of enterally administered glutamine is taken up during first pass by splanchnic organs (gut and liver). (G14).
-Glutamine orally is successful in elevating plasma glutamine at the peak concentration by 46%, which suggests that a substantial proportion of the oral load escaped utilization by the gut mucosal cells and uptake by the liver and kidneys. If the entire glutamine dose had been distributed within the blood (8% body wt) and extracellular fluid (20% lean body mass) compartments, then a 3-mM rise in blood glutamine concentration might have been expected, whereas plasma glutamine concentration was only observed to rise by 0.3 mM. This might suggest that only 10% of the oral dose reached the extracellular fluid compartments (G15).
-Infusion of glutamine increases plasma glutamine concentration and turnover only threefold, formation of glucose from glutamine increased sevenfold. Furthermore, glutamine infusion decreased its own de novo synthesis (4.55 +/- 0.22 vs. 2.81 +/- 0.62 micromol x kg(-1) x min(-1);P < 0.02) (G16).

Glutamine does not prevent exercise-induced immune impairment. Carbs do. And glutamine does not influence hormonal levels

-Consuming 30-60 g carbohydrate x h(-1) during sustained intensive exercise attenuates rises in stress hormones such as cortisol and appears to limit the degree of exercise-induced immune depression. Convincing evidence that so-called 'immune-boosting' supplements, including high doses of antioxidant vitamins, glutamine, zinc, probiotics and Echinacea, prevent exercise-induced immune impairment is currently lacking (G31).
-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 (G32).
-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 (G33).
-Nutritional supplementation with glutamine abolishes the exercise-induced decline in plasma glutamine, but does not influence post-exercise immune impairment. However, carbohydrate loading diminishes most exercise effects of cytokines, lymphocyte and neutrophils (G34).

Glutamine does not increase protein synthesis

-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 (G6).
-Short intravenous infusion of glutamine does not acutely stimulate duodenal protein synthesis in well-nourished, growing dogs (G8).

Glutamine prevents protein degradation but not more effectively than carbs

-0,9 g/kg glutamine during resistance training has no significant effect on muscle performance, body composition or muscle protein degradation compared to 0,9 g/kg maltodextrin (G9).
-Glutamine preserves protein synthesis in Caco-2 cells submitted to "luminal fasting", but higher glutamine doses did not enhance protein synthesis beyond control fed values. And glucose supplementation restored FSR as effi-ciently as glutamine (G10).

Carbhohydrate or BCAA supplementation prevents decrease in glutamine levels during exercise

-Carbohydrate supplementation affects positively the immune response of cyclists by avoiding or minimizing changes in plasma glutamine concentration (G11).
-Following an exercise bout, a decrease in plasma glutamine concentration can be observed, which is completely abolished by BCAA supplementation (G12).
-BCAA supplementation during a triathlon completely prevents the decrease in plasma glutamine (G13).
-7 distance runners reduced muscle gycogen. A high carb meal (80% carbs) before 60 min. exercise increases plasma glutamine. A 14 h fast before exercise does not change plasma glutamine. Plasma BCAA did not change under either dietary condition (G17).

Fasting decreases glutamine transport. And supplementation during fasting does not prevent muscle loss

-During fasting, skeletal muscle exports increased amounts of glutamine (Gln) while increasing the production of this amino acid by glutamine synthetase (GS) in order to maintain the intramuscular Gln pool (G41).
-Background: One of the major activities of the enterocyte is amino acid transport, which is important not only for the organism but also for the integrity of the mucosa. Bowel rest during the postoperative period is marked by decreased calorie and protein intake with atrophy of the brush border mucosa.
Fasting for 72 hours decreases glutamine and arginine transport. Alanine MeAIB, and leucine transport were maintained (G42).
-0.35 g/kg glutamine/day does not prevent loss of lean muscle in athletes during a 12-day weight reduction program (G43).

Glutamine does not enhance performance

-6 resistance-trained men performed weightlifting exercises after ingesting 0.3 g/kg glutamine. This did not enhance performance (G22).



REFERENCES

(G1) http://www.ncbi.nlm.nih.gov/entrez/q...016&query_hl=1
(G2) http://www.ncbi.nlm.nih.gov/entrez/q...059&query_hl=1
(G6) http://www.ncbi.nlm.nih.gov/entrez/q...116&query_hl=1
(G7) http://www.ncbi.nlm.nih.gov/entrez/q...808&query_hl=1
(G8) http://www.ncbi.nlm.nih.gov/entrez/q...312&query_hl=1
(G9) http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
(G10) http://ajpgi.physiology.org/cgi/content/full/285/1/G128
(G11) http://www.ncbi.nlm.nih.gov/entrez/q...341&query_hl=1
(G12) http://www.ncbi.nlm.nih.gov/entrez/q...939&query_hl=1
(G13) http://www.ncbi.nlm.nih.gov/entrez/q...884&query_hl=1
(G14)http://www.ncbi.nlm.nih.gov/entrez/q...750&query_hl=5
Complete studie: http://forum.*****************/showth...16#post7234016
(G15)http://jap.physiology.org/cgi/content/full/86/6/1770
(G16)http://ajpendo.physiology.org/cgi/co...act/272/3/E437
(G17)http://www.ncbi.nlm.nih.gov/entrez/q...952&query_hl=1
(G22)http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
(G31)http://www.ncbi.nlm.nih.gov/entrez/q...437&query_hl=1
(G32)http://www.ncbi.nlm.nih.gov/entrez/q...472&query_hl=1
(G33)http://www.ncbi.nlm.nih.gov/entrez/q...663&query_hl=1
(G34)http://www.ncbi.nlm.nih.gov/entrez/q...210&query_hl=1
(G41)http://www.ncbi.nlm.nih.gov/entrez/q...760&query_hl=1
(G42)http://www.ncbi.nlm.nih.gov/entrez/q...166&query_hl=1
(G43)http://www.jssm.org/vol2/n4/7/v2n4-7pdf.pdf

[Trans_Isomer]

From Will Brink

"I think the best we can say about glutamine is it (may) be useful for gut health in some gut related pathologies, it (may) be useful post op, and (may) be useful for preventing/treating OTS in athletes as some data found low glutamine levels correlated to OTS, but true cause and effect data of glutamine to OTS is lacking. Glutamine is just not an anabolic or even anti catabolic supp in healthy athletes."

[Trans_Isomer]

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.

[Trans_Isomer]

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.

[Trans_Isomer]

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.

[garb]

wow...that sure is a lot there trans. is that a term paper your handind in or what....lol

seriously tho great posts, i learned a lot of info from them...i just wish you would have posted this like 3 weeks ago when i bought a whole thing of glutamine. o well, you live and learn

good posts again.....

[Trans_Isomer]

From Bobo

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)...

[Trans_Isomer]

wow...that sure is a lot there trans. is that a term paper your handind in or what....lol

seriously tho great posts, i learned a lot of info from them...i just wish you would have posted this like 3 weeks ago when i bought a whole thing of glutamine. o well, you live and learn

good posts again.....

No, not a term paper, just some info I found on the internet
BTW, can you return the glutamine? :)

[snakemw]

great post trans. thanks for posting it up for everybody.

[Trans_Isomer]

great post trans. thanks for posting it up for everybody.

No problem, just let me know if you need more studies, lol

[snakemw]

i think i am good to go on the studies for awhile. ill probably have to read them over again cuz my eyes started going crossed about half way through them. lol

[ghostwheel]

So i guess I won't be buying anymore Glutamine when my supply runs out..

[SNS8778]

Good posts Trans.

I see two sides to this debate:

One - there are alot of studies that show what you posted that glutamine is not very effective.

Two - there are still not studies to confirm the effectiveness of some steroids that we all know work. Just something to think about.

My take on it:
There are many products in this industry that hold no value whatsoever. However, Glutamine has been a tried and true seller in this industry for a long time and there is virtually no marketing behind it anymore for that to be marketing related, so obviously some people feel that it helps them.

My personal experience:
For myself, low dose glutamine intake does not provide benefits to me. However, on higher doses (25 grams per day and above), I notice a definate improvement in recovery time and soreness. When cutting, I notice a definate effect on recovery time, soreness, and maintaining muscle.

Something to Always Remember with Supplements:
Everything works different for different people.

A Hint:
There are many things on the horizon to improve upon the downfalls of glutamine (i.e. absorption, need for high doses, etc.)

[dinoiii]

Trans

my God, you are really giving me a run for money in how much one person can post. you have certainly taken the title I think. I am not sure still how glutamine can be written off as a complete waste (your title) as you kind of offered the opposition a time to shine.

I found that Steve's post offered great insght into what the two sides could be. I respect Loki and PA and their opinions still stick out in my mind.

It is a forum, however, and it is important to understand the basic idea behind inhibiting the catabolic effects of cortisol and where the hell this idea originated in the first place and why it is subject for debate - focusing on the healthy weight trained individual for practical purposes to benefit people on this board.

I think the major focus on glutamine as a supplement came from the Hickson group in 1996 where they did animal studies infusing BOTH glutamine AND cortisol which ultimately indicated that glutamine could counteract the muscle wasting effects of cortisol. As you so thoroughly pointed out - this may not apply to healthy humans. The key points to remember though are:

(1) Lowering cortisol doesn't alter metabolism in any way or increase exercise performance!

-and-

(2) If you are lifting weights, then cortisol doesn't have a strong effect on muscle breakdown anyway!

-and-

(3) More experienced lifters release LESS cortisol when exposed to the same type of training as beginners - A HUGE FAULT OF SOME OF THE STUDIES YOU POSTED which offered NO CONTROL FOR THIS.



So - what the hell am I saying:
Well, in a way I agree with you - while glutamine may counteract cortisol in clinical situations, it doesn't appear to do so in healthy people, nor does it appear necessary, especially when the subjects have normal cortisol or even low cortisol (for some weight trained individuals)!

However, I agree with Steve in that it shouldn't be ruled out. Certain situations do warrant its use. First, it DOES increase the size of muscle cells and clearly plays an important role in cell volume regulation. The only problem is that this was in a petri dish and I am unaware of replication in animal or human subjects.

So what is your support?
Hehe - I will use my evil cardio to prove that this is not so open and shut. When are cortisol levels increased the most: aerobic training!!! I encourage you to read the full study (not abstract) by Castell and Newsholme (1997) with solely 5-8 grams of ingestion post aerobic training bout showing positive effects on immune functioning secondary to decreased cortisol proposal.

Another Hankard and co. (1996) showed a constant infusion into the digestive tract of oral glutamine of HEALTHY PEOPLE which showed increased PROTEIN SYNTHESIS. However, perhaps Steve is on to something with current oral absorption rates as it tends to directly contribute to cells of the GI first.

And lets not forget the true unfortunate. You get a greater insulin response when ingesting glutamine with carbs (not that I am a fan of carbs you will soon learn better). Check out Bowtell's group from 1999 and Mittendorfer and co. from 2001.





Now, in summary - I agree with EVERYONE's comments - really I do but as with ALL supplements, it is of MORE IMPORTANCE how you use it rather than if you just use it at all. This is what is the problem now. You MUST be supplement savvy to a degree.

There are times I would consider people NEEDING the amino and others well...

There's a lot of anti-arginine research too, but this has not hurt people's beliefs here, has it? Appropriate timing and the like are all things to consider in this debate - too many people don't step away and look at it like Steve did. Granted, I think he likely will have a bit more vested interest based on his last comment. ;-)

But this time, I have to agree again - even without the ominous stay tuned vibe.

[SNS8778]

Good post Dinoii.

As far as vested interest, we are looking into another form of glutamine. That said though, I would have had more vested interest in thrashing regular glutamine to promote the idea I'm looking at.

Also, many that have known me all along know I do use glutamine (when I work out lol) and that I am a fan of it at high doses at the appropriate times. Its not a huge difference maker, but for my personal results, its been worth the money to me or obviously I wouldnt use it.

[dinoiii]

I know a lot of people that use it religiously actually. I think that is anecdotal enough but yeah there are what I would feel appropriate times to use it.

Hey check out my article later in the article section. One of your products is mentioned and if you would like to add to it, I would love to hear input.

[Trans_Isomer]

Hmmm... where do I start? :)

First, thanks for the "longest post" award dinoii, lol

First, the argument that glutamine is still a hot seller. Well, so is creatine serum, and we all know that it actually contains no creatine at all, but STILL SELLS! Muscletech products are probaly the most popular out there, are they good because lots of people buy them? Hell no! Its usually the overlooked supplements that hold the most promise. People beleive glutamine works for them because:

1) They have no idea about nutrition/supplements/drugs and have other people inform them about them

2) Some People have more steroids than water in their veins

3)People who are commonly taking tens of drugs and supps at the same time, so how can they particularly say its the glutamine working?

I dont know of anyone who just takes glutamine. The people I knew of taking it that said it "helped" them also took M1T, lots of whey protein, vitamins, and creatine. With all this coursing throughout their system, im sure they "knew" it was the glutamine.

Ive even used glutamine! It was recommended by some of my buds when I was in high school. So I bought some, and took 30, 40, (and I even think 50) grams of that crap for about 3 weeks. And guess what? No increase in strength, recovery, hydration or anything. But what I did experience was some bad "gastrointestinal distress" (I dont think going to the bathroom for number two 5-6 times a day is normal).



Take a look at this study:
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.


Some say glutamine didnt work for some people because they didnt dose it high enough. Look at this study, 0.9 g x kg lean tissue mass, that sure looks like quite a bit of glutamine to me. And the conclusion, glutamine supplementation during resistance training has no significant effect on muscle performance, body composition or muscle protein degradation in young healthy adults.

Heres a quote taken from another article:

"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)..."


Ok, I realize a lot of whats out there dont have clinical trials or anything behind them, but with the amount of overwhelming evidence suggesting glutamine might be a bad idea to use, why would anyone buy it?

If you take in 1.5-2g of protein per pound of bodyweight, you are getting PLENTY of the different amino acids. You know what the recommended intake of protein actually is? .8g x kg bodyweight. You can see that bodybuilders intake of the different amino acids is already quite high.

Lets take a popular brand, say Dymatize. A 1000g of glutamine is about $40. With the NUMEROUS studies showing glutamine's uselessness for bodybuilders, do you want to spend $40 on something that only works according to your bud in the gym? Im sure if you spent that $40 bucks on some ON 100% whey protein youd get some better gains. Oh, and since 5lbs of ON's protein only cost $30 bucks, the additional $10 can be used for some creatine mono. That combo will beat glutamine any day (not sure if "beat" is the best word as it denotes a type of competition, and with glutamine im not sure there is any).

I dont know if adding a delivery system will make glutamine "work". I guess thats something to be left to anyone who wants to try it out.

I still find it funny people beleive in glutamine with all the studies showing that it sucks! I leave this post with a quote from my earlier article posting...

Glutamine is good for hospital patients and rich people with money to waste. If you’re involved in resistance training and already have proper post workout nutrition, along with a moderate carb intake, then glutamine probably won’t do anything for you. In fact, none of the proposed theories dealing with glutamine supplementation have worked out in the athletic world. It’s also one of the most expensive supplements around (simply based on dosage recommendations), so it’s way too costly to use for personal experimentation — especially when the updated scientific literature doesn’t support the theories.

[dinoiii]

Ok,

nice post again...

understand though I did not disagree and you will be happy to know I do NOT use it....with the addendum (RIGHT NOW). Do I believe it has its place...unfortunately, I still do.

They blanketed it in the aforementioned study. While I see that they used healthy subjects, they still did not take into consideration DIFFERENT training volumes, durations, etc... but the same ones. I am particular about using supplements at the right time, NOT the using of supplements alone.



And agian, I agree on your earlier points about creatine serum and Muscletech supps. One thing that differs between these two supps and glutamine supp buyers I think is that those using M-Tech are the newer people in the lifting game or the weekend warrior whereas the repeat buyers of glutamine remain the hard core.

The serum - well, that's just a felony!

[Trans_Isomer]

OK heres a funny story that popped into my head reading your last post dinoii, lol. I think this is how it goes

Anyone seen the old star wars? I think it was Return of the Jedi. When on the planet with the little bear creatures, Luke turns himself in to try and change his father (Darth Vader) to be good. While walking with his father he tried to persuade him to turn away from the dark side. Luke says "Father I know there is still good in you" and darth vader replies "You dont know the power of the dark side" so this is how this skit goes...

Trans_Isomer turns himself in to the dark side in order to save his father from the brotology of glutamine

(T_I): Father, I know there is still reason and cost-effectiveness left in you
(Dinoii): You dont know the power of GLUTAMINE!

Now, while on the Dark Star...

(While looking out the window of the dark star seeing a GNC with customers being attacked by the Pro-Salesman GNC staff)

(Darth Sidious): Soon you will join us
(T_I): I will never abandon reason and cost-effectiveness
(Darth Sidious): You and your studies are fighting a losing battle, soon all your rebel scum will be shopping at GNC
(Dinoii): You will join us or die
(T_I): I will never join you!

(T_I looking down at Darth Sidious' lap seeing all the studies in a folder)

(Darth Sidious): You want your precious's studies dont you?
(T_I looking angrily at Darth Sidious)
(Darth Sidious): Post these studies, and complete your journey to the dark side of supplementation!

(T_I uses the force to snatch the studies from DS, tries to post them, and is countered with rebute from dinoii (Darth Vader))

(After a debate, Darth Sidious (DS) begins to use the dark side of the force.. Brotology)

(DS): You will pay for your lack of vision
(T_I): You mean the hundreds to studies that prove you wrong?
(DS): Behold the power of BROTOLOGY!!

(T_I becomes confused and dazed by the brotological effects of Darth Sidious' post)

(Dinoii struggles with the reason and cost-effectiveness within, looking back and forth at T_I and DS's post. Dinoii then clicks on reply, and submits a powerful message)

(Dinoii): understand though I did not disagree and you will be happy to know I do NOT use it
(DS): Noooooooooooooooooooooooo!!!

(T_I replies with a post to the wary dinoii)

(T_I): Father, I knew there was still good in you, let me help you...
(Dinoii): No, you must go, I am already saved...

(T_I then drives fast away from the GNC as it explodes and all customers were able to get out alive. People then celebrate on online forums knowing they are saving money, and that brotology has been defeated....)

THE END!!

[garb]

lol.....thats a good one trans

[snakemw]

thats pretty good trans. thats the best verison of Star Wars i have heard of.

[ckozlgod]

Glutamine definately works for me...but is it worth the money?

No. I don't get THAT sore anymore, it's bearable and I am able to "rough" it just fine without it. When I did use Glutamine, it definately helped a lot in recovery. That was back when I first started working out. So it was beneficial for me then because obviously when you first start out...you get sore like no other. I think it also depends on your dosage like SNS8778 said.

Save your nickels and buy something that you know works best for you.

[dinoiii]

Omigod T_I,

I have obviously underestimated opposition to "Brotology."

I literally was laughing out of my seat that everyone came running to see what the hell the ruckus was about. I leave you with this new "powerful" message: YODA-style

Its rightful place alongside the vanadyl's, chromium's, and myostatin inhibitors, glutamine perhaps has. Yet, the future of this often poorly understood amino - not so clear, it is!




Thanks for the post! ;-)

[Trans_Isomer]

LOL! I had some free time and wanted to have some fun :)

[almostbig]

Sorry if this is a dumb question, but what is Brotology. I searched the net and couldn't find anything but other forums using the word pretty vaguely. I am guessing its bumkiss science but not really sure.

[Trans_Isomer]

Sorry if this is a dumb question, but what is Brotology. I searched the net and couldn't find anything but other forums using the word pretty vaguely. I am guessing its bumkiss science but not really sure.

Basically, its people who dont know what theyre talking about advice. People think because someone might be big or workout a lot that they know about nutrition and/or supplements.

Like for example in my high school, a lot of my friends took glutamine so they said I should. They probaly based this off "I heard from so and so" or "I saw an ad in a workout magazine saying how great it is" when in reality they didnt know what they were talking about. Thats basic brotology

[Trans_Isomer]

To the top

[pu12en12g]

Great thread Trans ;)

[Trans_Isomer]

Great thread Trans ;)

Haha you know it :)

[Trans_Isomer]

Breakin' the law

[mcsteveof2h2h]

great post trans

sadly i have like 1600 grams of L-Glutamine lol

anyone wanna buy some hahaha

[Trans_Isomer]

Thanks, hey atleast you got a good paper weight :)

[mcsteveof2h2h]

lol that i do

[Trans_Isomer]

To the top ^

[Dizzle1]

I should have read this oh about three years ago

[SNS8778]

I should have read this oh about three years ago

I wouldnt necessarily consider it wasted. Me and Trans have agreed to disagree, but I think glutamine does serve a role in bodybuilding under certain conditions. In my OPINION, this is dependent upon what your results are, dosage, and timing.

[dinoiii]

And its on here too. The Glutamine Redemption series to soon follow in this very articles section well referenced and exploring quite a bit. I need to have more time in a day though.

[Trans_Isomer]

No need to worry about that article dinoiii, I got the glutamine subject covered :)

[Trans_Isomer]

I wouldnt necessarily consider it wasted. Me and Trans have agreed to disagree, but I think glutamine does serve a role in bodybuilding under certain conditions. In my OPINION, this is dependent upon what your results are, dosage, and timing.

And again, this thread applies to L-Glutamine. There may be ways to improve absorption/bioavailability... ;)

[dinoiii]

No need to worry about that article dinoiii, I got the glutamine subject covered :)


I smile...but you'll soon see we've just scratched the surface. This nutrient will be dissected in such a way, many will NEVER want to go there again!!!


Again, all's I got is "TRUST ME!"

[Trans_Isomer]

I smile...but you'll soon see we've just scratched the surface. This nutrient will be dissected in such a way, many will NEVER want to go there again!!!


Again, all's I got is "TRUST ME!"

I look forward to it! :)

[Trans_Isomer]

*I wanted to post a snippet of Layne Norton's views on glutamine
*Layne Norton is a PhD candidate in the area of nutritional science specializing in amino acid utilization at the University of Illinois. Layne received his BS in Biochemistry from Eckerd College in 2004.

Here is where I explain what happens to orally ingested glutamine
unfortunately, not much glutamine makes it into the bloodstream from oral supplementation. When glutamine enters the small intestine and is absorbed into the mucosal cell, it is then metabolized via brush boarder enzymes to two different products. One product is alanine which is created from the alpha nitrogen on glutamine, the other product is the carbon skelaton left over with the epsilon nitrogen. This carbon skelaton is then oxidized by the gut for fuel while the ammonia group is excreted, or may enter the urea cycle. The alanine from this process is sent to the liver via the portal vein where it is used to form glucose via gluconeogenesis. It is in this way that our body prevents us from overloading ourselves with individual amino acids. The liver and mucosal cells act as a buffer to the peripheral tissues. If this buffer wasn't in place it could have dire health consequences. So to recap, you can't overload yourself with certain amino acids, b/c before ANY nutrient that is orally administered enters the blood stream, it has to pass by the liver, and since the liver regulates amino acid levels, if it "sees" that things may get out of wack it will retain these substrates for gluconeogenesis (making glucose from amino acids) which it will then pass on to the peripheral tissues.


--------------------------------------------------------------------------------------------
this was addressing people who said you need a high dose to get anything from it.

"just real quickly... all of you that are saying... "well they need to use more glutamine"... well that's all well and good... OF COURSE IT WILLHAVE AN ANABOLIC EFFECT WHEN YOU GIVE IT IN A 40G DOSE! It does have nitrogen and though glutamine doesn't stimulate protein synthesis it can donate it's nitrogens and they can be recycled and eventually end up in other amnio acids... as well as glutamine may spare the oxidation of other amino acids... HOWEVER, this is nothing that you wouldn't also get from a corresponding increase in protein intake by 40g.

Many people will say, "well I didn't see results until I upped my glutamine to 30-40g per day" well what most likely happened was one of 2 things

1) they increased their total nitrogen intake to a more beneficial level and saw benefits from it

2) they increased their total calories by 120-160 calories... and gained some weight

We need to look at this and think critically... a corresponding amount of increase in protein intake with an equal amount of nitrogen will do the same thing. "

---------------------------------------------------------------------------------------------

You will not find one well designed study showing that glutamine has an impact on muscle gain/retention in healthy, weight trained individuals. All the studies out there that show benefits to glutamine have the following problems with them.

1) they use glutamine adminstered intraveneously, this bypasses the gut and liver extraction.

2) the studies are done in burned, diseased, or surgical patients. Contrary to what supplement companies would like you to believe, this does NOT relate the physiological state of a trained athlete.

3) the studies are done using glutamine vs. placebo. Of course glutamine will be superior to no calories whatsoever in maintaining muscle mass... that's kind of "duh." Of these studies out there supporting glutamine use in athletes (of which there are few), none of them that I know of have examined glutamine supplementation in people consuming the same amounts of total nitrogen. It's just placebo vs. glutamine, which is terrible experimental design.


Why have you never heard any of this before??? Because glutamine is a cash cow of the industry, you will never see people questioning it's effectiveness in any of the mainstream muscle mags or by any of the pro bodybuilders. Why? Because the supplement companies pay for the advertisements that keep these magazines in business... do you think they would put a glutamine ad in a magazine with a big anti-glutamine article???? Heck no. It wouldn't be good for the magazine either in the long run. So for the most part it is kept hush-hush.

btw, i'm doing my phd in amino acid metabolism

[Jswoll]

I smile...but you'll soon see we've just scratched the surface. This nutrient will be dissected in such a way, many will NEVER want to go there again!!!


Again, all's I got is "TRUST ME!"
I'll be interested to see, I have my own view on the subject...you can tell by my use of glut., but I'm more concerned with the dosing parameters you mentioned to me... I shall see, impatient as always.

[Trans_Isomer]

I'll be interested to see, I have my own view on the subject...you can tell by my use of glut., but I'm more concerned with the dosing parameters you mentioned to me... I shall see, impatient as always.

Why do you beleive it to be of use when hundreds of studies prove otherwise?

[Jswoll]

Why do you beleive it to be of use when hundreds of studies prove otherwise?
In due time, Trans, in due time.

[UNCfan1]

Dang between Dinoii and Trans and all of their studys and science my head is spinning and can a brother get some info in laymans terms lol!! Simplify this stuff for us dumbasses LOL!

[Trans_Isomer]

Dang between Dinoii and Trans and all of their studys and science my head is spinning and can a brother get some info in laymans terms lol!! Simplify this stuff for us dumbasses LOL!


Glutamine is good for hospital patients and rich people with money to waste. If you’re involved in resistance training and already have proper post workout nutrition, along with a moderate carb intake, then glutamine probably won’t do anything for you. In fact, none of the proposed theories dealing with glutamine supplementation have worked out in the athletic world. It’s also one of the most expensive supplements around (simply based on dosage recommendations), so it’s way too costly to use for personal experimentation — especially when the updated scientific literature doesn’t support the theories.

[Trans_Isomer]

And I personally beleive the "results" people propose to see from glutamine is merely because of an increase in calories from the glutamine supplementation, more calores = more mass, recovery, etc.

4cals to 1g of glutamine

Some people take 30-40g a day, = 120-160 more calories added in per glutamine serving

[UNCfan1]

Thanks Trans that made more sense LOL, what is considered proper postwork nutrition, carbs+protein+creatine+BCAA's?

[Trans_Isomer]

Thanks Trans that made more sense LOL, what is considered proper postwork nutrition, carbs+protein+creatine+BCAA's?

Unless your on some super competition no carb diet, then glutamine is a waste. I might see its use during dieting/cutting, but other than that I bet youll see much better results by using another scoop of whey in place for that scoop of glutamine. And I really beleive during even dieting/cutting, you will see minimal, if any results. Glutamine, IMO has been one of the longest on going scams in the supplement industry.

[UNCfan1]

Yeah I have been taking 40g a day, so when mine runs out I won't buy anymore. I thought that glutamine helped with recovery, muscle retention, nitrogen retention, corstiol suppression and so on. Maybe I was wrong.

[Trans_Isomer]

Yeah I have been taking 40g a day, so when mine runs out I won't buy anymore. I thought that glutamine helped with recovery, muscle retention, nitrogen retention, corstiol suppression and so on. Maybe I was wrong.

Calories help with this, positive nitrogen balance helps with this. Glutamine's primary benefit comes from its caloric content.

[UNCfan1]

ok cool thanks trans, ur a bright young man keep up the good work.

[Trans_Isomer]

Grab some BCAA's or EAA's, they are supported from many scientific studies to be very, very beneficial.

One of my favorite quotes from Patrick Arnold of Ergopharm:

"fooling around with glutamine is a waste of time, unless you are sick or very weakened. compare the differences in physiological response to exercise with essential amino acids, or even just branch chain amino acids, to glutamine. we are talking very impressive responses compared to nothing

yet people reach for the bottle of glutamine first

dumbassess

seriously, its time someone cleaned house"

[Trans_Isomer]

ok cool thanks trans, ur a bright young man keep up the good work.

Thanks, im glad I could help. Me and dinoiii have talked about glutamine over the phone as well, and I beleive he will be doing an article showing where glutamine may be helpful. For bodybuilding purposes, I really see none.

[UNCfan1]

Grab some BCAA's or EAA's, they are supported from many scientific studies to be very, very beneficial.i]

Yeah I was thinking about getting All in One or Purple Wrath do u think those would be good enough or should I just go with some regular BCAA powder?

[Trans_Isomer]

Yeah I was thinking about getting All in One or Purple Wrath do u think those would be good enough or should I just go with some regular BCAA powder?

Im a college student so money is always a factor for me. I buy BCAA's in bulk. They taste nasty though. Try to get in 5g right upon awakening in the morning (empty stomach), 5g 5 mins before your workout, 5g during, and 5g post workout, with protein/carb shake 20-30 mins afterwards

[UNCfan1]

ok cool, would it be cool to take 5g with the Trac Extreme preworkout and 5g grams with the SizeOn during the workout?

[UNCfan1]

I have totally gotten of the subject I am sorry.

[Trans_Isomer]

ok cool, would it be cool to take 5g with the Trac Extreme preworkout and 5g grams with the SizeOn during the workout?

I dont see why not