L-Glutamine and Ketosis.

Discussion in 'Dieting / Supplement Discussion' started by Pug Ugly, Jan 13, 2009.

  1. Pug Ugly White Belt

    Pug Ugly
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    I may be barking up the wrong tree here completely (and I apologize if this is in a sticky; I couldn't find it) but when entering ketosis, should I stop supplementing with L-Glutamine as (and I may be wrong) it helps the liver replenish glycogen?.. In ketosis, your liver's stores of glycogen is used up, right?.. I'm all searched out, please just give me a hand here. :eek:
    Reason being I'm switching to a paleo type diet and I'd like to know if the Glu. is going to halt weight loss.. If so, I'll stop taking it.
     
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  2. ronin0352 Lift, Eat, Sleep, Repeat

    ronin0352
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    Um, you should stop supplementing with glutamine regardless of what kind of diet you're on.
     
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  3. Pug Ugly White Belt

    Pug Ugly
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    Care to post a link or something if you're not going to tell me why?

    edit: I'm not trying to be a shit. I'm just curious as I haven't come across anything that made me think it's bad, in fact everything I've read and heard has drawn me to it as a very good thing to take.
     
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  4. Steakeater** Banned

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  5. Pug Ugly White Belt

    Pug Ugly
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    Thank you!
     
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  6. Pug Ugly White Belt

    Pug Ugly
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    So.. if you're attempting a low carb diet and your protein intake is too high, you can make your liver produce too much glycogen and thereby slow down your weight loss.

    High protein = Body creates carbohydrate.

    Which means the addition of glutamine supplementation is not only unnecessary but actually detrimental to a LC way of eating by creating more carbohydrate..

    Yeesh. Thanks again guys.
     
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  7. ronin0352 Lift, Eat, Sleep, Repeat

    ronin0352
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    YW, sorry I wasn't more detailed with my original response. I just got home from the gym & need to log my training :D
     
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  8. MikeMartial Black Belt

    MikeMartial
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    While glutamine is fairly pointless, you've got some major concepts wrong. High protein does NOT mean your body is "creating" carbohydrates. Yes, glucose is a carbohydrate, and glycogen (stored form of glucose) is also considered a carbohydrate by definition, and excess protein CAN and WILL be converted into glycogen via gluconeogenesis, it does so without the release of insulin. This IS going to happen in ketosis---in fact, it's essential. Fuck, I bet that's as clear as mud. Hopefully, a bit clearer. :icon_neut

    Your liver is going to replenish glycogen stores regardless of what you put into your body. It has to, because it and the brain require SOME glucose, and skeletal muscles require glycogen. The whole point of a ketogenic diet is to reduce insulin secretion and increase glucagon secretion to cause the body to start using triglycerides as fuel---but your body will still make glucose, but just from different sources.

    Also, for clarification, there is a VAST difference between a low carb diet and a ketogenic diet. To quote Lyle McDonald "A true ketogenic diet contains, by definition, less than 100 g carbs/day. But while all ketogenic diets are low-carbohydrate, not all low-carbohydrate diets are ketogenic"

    From an athletic standpoint, a ketogenic diet isn't favorable; the 3 weeks to adapt to ketosis and increased time to restore muscle glycogen makes it undesirable. Plus, unless one is severely disciplined, slipping "out" of ketosis back into utilizing carbs for fuel would theoretically trash this adaptation. A better option for an athlete is either constant low carb, or cyclic low carb, IMO.

    In regards to glutamine and actual ketosis, yes, it would probably be bad, because glutamine is an insulin secretagogue. How strong of one, I have no idea. But considering all the complete protein one would be eating while on a ketogenic diet, I see no point in consuming more through supplementation.
     
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  9. fat_wilhelm Black Belt

    fat_wilhelm
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    All hail the food mod!
     
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  10. fat_wilhelm Black Belt

    fat_wilhelm
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    Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers.

    Boza JJ, Dangin M, Moennoz D, Montigon F, Vuichoud J, Jarret A, Pouteau E, Gremaud G, Oguey-Araymon S, Courtois D, Woupeyi A, Finot PA, Ballevre O.

    Nestle Research Center, Vers-Chez-Les-Blanc, 1000 Lausanne 26, Switzerland.

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


    Oxidation of glutamine by the splanchnic bed in humans.

    Haisch M, Fukagawa NK, Matthews DE.

    Departments of Medicine and Chemistry, University of Vermont, Burlington, Vermont 05405, USA.

    [1,2-(13)C(2)]glutamine and [ring-(2)H(5)]phenylalanine were infused for 7 h into five postabsorptive healthy subjects on two occasions. On one occasion, the tracers were infused intravenously for 3.5 h and then by a nasogastric tube for 3.5 h. The order of infusion was reversed on the other occasion. From the plasma tracer enrichment measurements at plateau during the intravenous and nasogastric infusion periods, we determined that 27 +/- 2% of the enterally delivered phenylalanine and 64 +/- 2% of the glutamine were removed on the first pass by the splanchnic bed. Glutamine flux was 303 +/- 8 micromol. kg(-1). h(-1). Of the enterally delivered [(13)C]glutamine tracer, 73 +/- 2% was recovered as exhaled CO(2) compared with 58 +/- 1% of the intravenously infused tracer. The fraction of the enterally delivered tracer that was oxidized specifically on the first pass by the splanchnic bed was 53 +/- 2%, comprising 83% of the total tracer extracted. From the appearance of (13)C in plasma glucose, we estimated that 7 and 10% of the intravenously and nasogastrically infused glutamine tracers, respectively, were converted to glucose. The results for glutamine flux and first-pass extraction were similar to our previously reported values when a [2-(15)N]glutamine tracer [Matthews DE, Morano MA, and Campbell RG, Am J Physiol Endocrinol ****b 264: E848-E854, 1993] was used. The results of [(13)C]glutamine tracer disposal demonstrate that the major fate of enteral glutamine extraction is for oxidation and that only a minor portion is used for gluconeogenesis.



    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.


    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.


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

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

    Department of Human Biology, Maastricht University, The Netherlands. RH01769@RH.DK

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

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

    Zachwieja JJ, Witt TL, Yarasheski KE.

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

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


    Exercise-induced immunodepression- plasma glutamine is not the link.

    Hiscock N, Pedersen BK.

    Copenhagen Muscle Research Centre and Department of Infectious Diseases, Rigshospitalet, University of Copenhagen, DK-2100 Copenhagen, Denmark.

    The amino acid glutamine is known to be important for the function of some immune cells in vitro. It has been proposed that the decrease in plasma glutamine concentration in relation to catabolic conditions, including prolonged, exhaustive exercise, results in a lack of glutamine for these cells and may be responsible for the transient immunodepression commonly observed after acute, exhaustive exercise. It has been unclear, however, whether the magnitude of the observed decrease in plasma glutamine concentration would be great enough to compromise the function of immune cells. In fact, intracellular glutamine concentration may not be compromised when plasma levels are decreased postexercise. In addition, a number of recent intervention studies with glutamine feeding demonstrate that, although the plasma concentration of glutamine is kept constant during and after acute, strenuous exercise, glutamine supplementation does not abolish the postexercise decrease in in vitro cellular immunity, including low lymphocyte number, impaired lymphocyte proliferation, impaired natural killer and lymphokine-activated killer cell activity, as well as low production rate and concentration of salivary IgA. It is concluded that, although the glutamine hypothesis may explain immunodepression related to other stressful conditions such as trauma and burn, plasma glutamine concentration is not likely to play a mechanistic role in exercise-induced immunodepression.


    Addition of glutamine to essential amino acids and carbohydrate does not enhance anabolism in young human males following exercise.

    Wilkinson SB, Kim PL, Armstrong D, Phillips SM.

    Exercise ****bolism Research Group, Department of Kinesiology, McMaster University, 1280 Main St. West, Hamilton, ON L8S 4K1, Canada.

    We examined the effect of a post-exercise oral carbohydrate (CHO, 1 g.kg(-1).h(-1)) and essential amino acid (EAA, 9.25 g) solution containing glutamine (0.3 g/kg BW; GLN trial) versus an isoenergetic CHO-EAA solution without glutamine (control, CON trial) on muscle glycogen resynthesis and whole-body protein turnover following 90 min of cycling at 65% VO2 peak. Over the course of 3 h of recovery, muscle biopsies were taken to measure glycogen resynthesis and mixed muscle protein synthesis (MPS), by incorporation of [ring-2H5] phenylalanine. Infusion of [1-13C] leucine was used to measure whole-body protein turnover. Exercise resulted in a significant decrease in muscle glycogen (p < 0.05) with similar declines in each trial. Glycogen resynthesis following 3 h of recovery indicated no difference in total accumulation or rate of repletion. Leucine oxidation increased 2.5 fold (p < 0.05) during exercise, returned to resting levels immediately post-exercise,and was again elevated at 3 h post-exercise (p < 0.05). Leucine flux, an index of whole-body protein breakdown rate, was reduced during exercise, but increased to resting levels immediately post-exercise, and was further increased at 3 h post-exercise (p < 0.05), but only during the CON trial. Exercise resulted in a marked suppression of whole-body protein synthesis (50% of rest; p < 0.05), which was restored post-exercise; however, the addition of glutamine did not affect whole-body protein synthesis post-exercise. The rate of MPS was not different between trials. The addition of glutamine to a CHO + EAA beverage had no effect on post-exercise muscle glycogen resynthesis or muscle protein synthesis, but may suppress a rise in whole-body proteolysis during the later stages of recovery.
     
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  12. MikeMartial Black Belt

    MikeMartial
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    All hail the food mod? Pfft. Y'all better damn well listen up when Fat Wilhelm posts in D&S. It's a rare occasion, but when he does, you better READ MOTHERFUCKER.
     
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  13. Pug Ugly White Belt

    Pug Ugly
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    MikeMartial - As always, a great explanation to a pretty jumbled and undereducated post.. This is exactly the answer I was looking for.

    fatWilhelm - Awesome reference and conclusions.. Just read it all.

    Thanks for taking all the time.. I guess there's lots of info out there, I just have to learn how to look harder.
     
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  14. otnemeM Blue Belt

    otnemeM
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    Studies are all fine, I already knew most of them and as such was a hardcore naysayer.

    Then I tried it, 8g dose, once or twice a day on an empty stomach. Now I can say I notice the difference in holding LBM while cutting.

    As the poet said, do not quote me books for what I saw with my own eyes. Or something.
     
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