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Martinogdenbsx said:who has had decent results with it then?
PreMier said:Glutamine IS worthless. Even David Tolson thinks so.
gopro said:Oh, well if HE says so, I'm changing my mind on the whole subject!
PreMier said:Do you know as much about supplementation as David?
PreMier said:Good reply.
I will choose to listen to David, and the studies posted by him on this one though. Along with the ones on pubmed. IMO glutamine will give me nothing but a lighter wallet
PreMier said:IMO glutamine will give me nothing but a lighter wallet
Robert DiMaggio said:maybe it will, maybe it will not, is it not worth trying for 6 months to at least find out for yourself?
are you really going to read articles and base everything you do and don't do on them?
[font=verdana, arial, helvetica]http://www.hypertrophy-specific.com...ct=ST;f=13;t=25
Here are the reasons to take glutamine.
1) Immune support. Supplemental use of glutamine, either in oral, enteral, or parenteral form, increases intestinal villous height, stimulates gut mucosal cellular proliferation, and maintains mucosal integrity. It also prevents intestinal hyperpermeability and bacterial translocation, which may be involved in sepsis and the development of multiple organ failure. One study reported that athletes reported fewer incedences of upper respiratory tract infections while supplementing with glutamine (2 grams) after they ran.
2) Gastrointestinal support. 70-80% of orally administered glutamine is absorbed into the cells of your GI tract. It remains there and is metabolised by those cells without ever reaching the blood stream (image). In sicknesses such as sepsis it has been shown to help improve survival because of improved GI tract function.
Thats pretty much it.
There is no real benefit for someone looking to build bigger muscles. That 10% of dietary glutamine that gets past the GI tract is taken up by the liver where it is converted into sugar (gluconeogenesis) and stored as glycogen in the liver.
Don't let in-vitro research fool you into thinking oral glutamine will have an effect on a healthy individuals muscle mass. Yes, glutamine does regulate protein synthesis to a certain extent under some situations. However, you can't make it happen by taking it orally. Don't let ads with some pro-bodybuilder holding a bottle of glutamine fool you. Even if that pro-bodybuilder is taking it...it isn't doing anything for him either.
Here are a couple good "in-vivo" research studies to start with:
1. 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.
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.
Keep in mind that if you are eating protein powders, especially any thing with whey in it, you are getting plenty of glutamine. The question of glutamines worth in the newsletter centered on its effect on building mass and/or strength, not anything to do with the gastrointestinal track.
In short, only 47-50% of orally administered glutamine can be expected to make it past the liver and other organs, into the blood stream. And only about 10% can be expected to reach extracellular spaces.[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. Journal of Applied Physiology. 1999 Jun;86(6):1770-7] Now, this is the main argument against glutamine. 90% of the glutamine you take orally never even makes it to your muscles. This isn't to say it is wasted. Your GI tract loves glutamine from reasons explained earlier. If you are having intestinal problems nothing is better. If you are trying to increase protein synthesis by loading glutamine, it isn't going to work[/font]
PreMier said:How would you feel if I also told you that BCAA's were a waste?
David Tolson said:Well we've managed to establish that glutamine is useless, I would like to take the next step. I just finished a lot of research on BCAA's, and an article. Here is about 1/4th of the article.
Are BCAA supplements necessary?
Given the information above, there is significant evidence indicating various benefits of BCAA ingestion for athletes. However, the pertitent issue then becomes whether or not BCAA supplements have any advantage over ingestion of protein and/or carbohydrates, which are both significantly less expensive.
The first issue is whether or not BCAA's are superior to protein in stimulating protein synthesis. One study indicates that there is a decline in plasma leucine over five weeks of training in speed and strength athletes consuming 1.26 g protein per kg bodyweight daily, and that leucine supplementation prevents this decrease [4]. However, this study is only confirming a well known fact, which is that strength athletes need high amounts of dietary protein. Studies indicate that in bodybuilders and strength trainers, the amount of dietary protein needed to maximally stimulate protein synthesis is in the realm of 1.4-1.8 g/kg bodyweight (about .6-.7 g/lb), and also that most of these athletes consume well above this amount [31]. For example, a study in stength athletes compared daily dietary protein intakes of .86 g/kg, 1.40 g/kg, and 2.40 g/kg, and found that whole body protein synthesis was increased in the 1.40 g/kg group compared to the lower group, but not further increased in the 2.40 g/kg group. However, rates of leucine oxidation were much higher in the high protein group [32]. This means that if protein intake is adequate, it is doubtful that BCAA supplementation could further stimulate protein synthesis, as the extra amino acids will just be readily catabolized.
Perhaps even more enlightening is the work of Tipton et al., who conducted studies on the types and quantities of amino acids that increase protein synthesis in humans during and after exercise [33]. They compared 40 grams of mixed amino acids to 40 grams of essential amino acids (containing a much higher quantity of BCAA's) to compare their effectiveness in stimulating protein synthesis postexercise, and the two supplements provided a equivalent increases in protein synthesis. The authors then concluded that "there is a maximum rate of net synthesis attainable during hyperaminoacidemia after exercise," and that 40 grams of mixed amino acids is enough to maximally stimulate protein synthesis postexercise.
Another issue is that BCAA supplements are in the form of free-form amino acids, as opposed to a whole protein source. Supplement companies often claim that free-form amino acids are absorbed in greater quantity, more effectively, and more quickly, but this is contrary to the scientific evidence. In general, studies indicate that protein hydrolysates are utilized most effectively, followed by whole proteins, followed by free form amino acids. Intestinal transporters exist for both peptides and free amino acids, and peptides are absorbed more rapidly [34]. Peptides that are not absorbed via a transporter can be rapidly broken down enzymatically. Although not the best model for human athletes, studies in food-deprived rats being refed consistently find that whey protein hydrolysate leads to much higher degrees of weight gain and nitrogen retention than free form amino acids, with one study indicating that whole protein is in the middle in terms of effectiveness [35-36]. Comparative studies have also been done in humans. In healthy subjects, whole protein, protein hydrolysate, and free amino acids all resulted in similar nitrogen balance [37]. Another study in healthy humans found that a protein hydrolysate was absorbed equally as rapidly as free form aminos [38]. Ideally, a study more specific to the conditions in question would be available, but this research indicates that fast-digesting proteins could be just as or more effective than free form amino acids for use before or during exercise.
Carbohydrates may also provide many of the benefits of BCAA supplementation at a much lower cost. As mentioned above, two studies found that BCAA's and carbohydrates together did not provide a performance advantage over carbohydrates alone. Carbohydrates will obviously have glycogen sparing and glucose increasing properties as BCAA's do. Also, carbohydrate supplementation prevents the increase in tryptophan levels caused by exercise, although they may not be as effective as BCAA's [20]. Finally, carbohydrates also have glutamine-sparing and positive immune effects in athletes [39].
All in all, it would appear that the positive effects of BCAA's on protein synthesis can be achieved by a high protein diet and use of a fast-acting protein prior to and after exercise, and that most of the other possible benefits on exercise performance could be achieved equally as effectively by ingesting simple carbohydrates prior to exercise. If caloric intake must be limited at all costs, or if protein intake is inadequate, BCAA's may be useful in this respect. Also, a unique benefit of reduced CNS fatigue by decreasing tryptophan buildup cannot yet be discounted. Given the other properties of BCAA's described below, the usefulness of BCAA supplements can further be questioned.
Other effects of BCAA's
In addition to the effects on tryptophan levels, BCAA's may have other effects on the CNS, both direct and indirect. A well established property is that BCAA supplements reduce dopamine levels, an effect that occurs in many sample populations including healthy human volunteers (at doses of 10, 30, and 60 g) [40]. There are two possible reasons for this effect. The primary reason is that BCAA's competitively inhibit transport of phenylalanine and tyrosine to the brain (similar to the inhibition of tryptophan) [41]. Secondly, BCAA's also simultaneously lower the plasma levels of key amino acids required for neurotransmitter synthesis. This occurs because the BCAA's stimulate protein synthesis, but other amino acids are also required for protein synthesis. This issue does not occur with whole protein sources, which also provide the other amino acids required for protein synthesis. BCAA's also consequently lower levels of norepinephrine [42]. In conditions such as mania and hepatic encephalopathy, this effect of BCAA's can be beneficial [41-42]. However, decreased levels of NE and dopamine are generally not desirable in normal individuals. Functional changes induced in healthy humans by BCAA ingestion so far include impaired spatial memory and elevated plasma prolactin [40-41]. There is also a reference in the literature to BCAA ingestion increasing appetite [43].
The references
4. Sports Med. 1999 Jun;27(6):347-58. Leucine supplementation and intensive training. Mero A.
20. Amino Acids. 2001;20(1):25-34. Amino acids and central fatigue. Blomstrand E.
31. J Am Coll Nutr. 2000 Oct;19(5 Suppl):513S-521S. Beyond the zone: protein needs of active individuals. Lemon PW.
32. J Appl Physiol. 1992 Nov;73(5):1986-95. Evaluation of protein requirements for trained strength athletes. Tarnopolsky MA, Atkinson SA, MacDougall JD, Chesley A, Phillips S, Schwarcz HP.
33. Am J Physiol. 1999 Apr;276(4 Pt 1):E628-34. Postexercise net protein synthesis in human muscle from orally administered amino acids. Tipton KD, Ferrando AA, Phillips SM, Doyle D Jr, Wolfe RR.
34. Ann Nutr Metab. 1982;26(6):337-52. Characterization and nutritional significance of peptide transport in man. Silk DB, Hegarty JE, Fairclough PD, Clark ML.
35. JPEN J Parenter Enteral Nutr. 1989 Jul-Aug;13(4):382-6. Effect of whey proteins, their oligopeptide hydrolysates and free amino acid mixtures on growth and nitrogen retention in fed and starved rats. Poullain MG, Cezard JP, Roger L, Mendy F.
36. Eur J Nutr. 2000 Dec;39(6):237-43. Protein hydrolysate vs free amino acid-based diets on the nutritional recovery of the starved rat. Boza JJ, Moennoz D, Vuichoud J, Jarret AR, Gaudard-de-Weck D, Ballevre O.
37. Gut. 1985 Jul;26(7):694-9. Relative nutritional value of whole protein, hydrolysed protein and free amino acids in man. Moriarty KJ, Hegarty JE, Fairclough PD, Kelly MJ, Clark ML, Dawson AM.
38. Gut. 1982 Aug;23(8):670-4. Comparison of plasma and intraluminal amino acid profiles in man after meals containing a protein hydrolysate and equivalent amino acid mixture. Hegarty JE, Fairclough PD, Moriarty KJ, Clark ML, Kelly MJ, Dawson AM.
39. Clin Nutr. 2002 Oct;21(5):423-9. Carbohydrate supplementation during intense exercise and the immune response of cyclists. Bacurau RF, Bassit RA, Sawada L, Navarro F, Martins E Jr, Costa Rosa LF.
40. Psychopharmacology (Berl). 2002 Mar;160(2):192-7. Epub 2002 Jan 10. A dose-finding study on the effects of branch chain amino acids on surrogate markers of brain dopamine function. Gijsman HJ, Scarna A, Harmer CJ, McTavish SB, Odontiadis J, Cowen PJ, Goodwin GM.
41. Br J Psychiatry. 2003 Mar;182:210-3. Effects of a branched-chain amino acid drink in mania. Scarna A, Gijsman HJ, McTavish SF, Harmer CJ, Cowen PJ, Goodwin GM.
42. Am J Psychiatry. 2003 Jun;160(6):1117-24. Efficacy of the branched-chain amino acids in the treatment of tardive dyskinesia in men. Richardson MA, Bevans ML, Read LL, Chao HM, Clelland JD, Suckow RF, Maher TJ, Citrome L.
43. Brain Res Bull. 1999 Jul 1;49(4):281-4. Branched-chain amino acid-induced hippocampal norepinephrine release is antagonized by picrotoxin: evidence for a central mode of action. Torigoe K, Potter PE, Katz DP.
Many people swear by BCAA's.
Many people swear by glutamine.
If you give someone a placebo, many people will swear by it.
I will not deny your personal experience. But I will say that I do not think it should constitute a convincing argument for others. I argue that the scientific evidence does not favor BCAA supplementation. If people go on to use them based on feedback that is their prerogative.