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TweetHow Cortisol Breaks Down Muscle
Understanding cortisol's catabolic activity in muscle provides some insight into the way certain food supplements may help spare muscle by inhibiting it. Cortisol is known to reduce body protein stores in all tissues except for the liver. It does that through several mechanisms, including a reduction in the synthesis of cellular RNA, which is essential for protein synthesis. Since anabolic steroids promote muscle protein synthesis by increasing RNA, cortisol has exactly the opposite effect.
Cortisol mobilizes amino acids from muscle for transport to the liver, where they undergo a process called gluconeogenesis that results in increased glucose production. While this is vital for a rapid source of energy during severe stress, it also results in muscle breakdown. Insulin opposes cortisol in the action, but high stress activity promotes cortisol domination over insulin.
Recent studies show that consuming carbohydrates and protein immediately following a workout both increases insulin release and potently blunts cortisol. The dosage of carbs required for this effect is one gram per kilogram (2.2 pounds) of bodyweight taken immediately after training and again one hour later. In addition, including at least 50 grams of protein helps maximize insulin release.
Cortisol appears to promote the synthesis of a protein-degrading substance called ubiquitin that rapidly breaks down muscle. Interestingly, a drug called clenbuterol that's favored by some bodybuilders may work by inhibiting ubiquitin synthesis in muscle, thereby exerting an anticatabolic effect. Other hormones, such as growth hormone and insulinlike growth factor 1 (IGF-1), appear to inhibit the ubiquitin system as well.
Cortisol also works by stimulating the exit of the amino acid glutamine from muscle. When that occurs, rapid muscle catabolism follows. Several studies show that taking supplemental glutamine may block much of the catabolic effects of cortisol in muscle.
A study conducted about two years ago showed that as little as two grams of oral glutamine significantly increased growth hormone release. That alone would give you an anticatabolic effect, since growth hormone opposes the actions of cortisol in muscle. In fact, studies indicate that decreasing cortisol release in the body results in an upgraded growth hormone response.
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TweetI thought glutamine was proven to be useless?
Tweetgreat thread....
TweetIMO cortisol is a bb's enemy.
Bro I'm no guru, know it all but I'll vouch for creatine/glutamine/slin combo.I thought glutamine was proven to be useless?
TweetWhere at? It's the only effective supplement I've ever used. Creatine is useless IMO, I mean at least it doesn't work for me.Originally posted by whitetail
I thought glutamine was proven to be useless?
TweetGlutamine is WorthlessOriginally posted by Raoul3
Where at? It's the only effective supplement I've ever used. Creatine is useless IMO, I mean at least it doesn't work for me.
Effect of glutamine supplementation combined with resistance training in young adults.
Candow DG, Chilibeck PD, Burke DG, Davison KS, Smith-Palmer T.
College of Kinesiology, University of Saskatchewan, Saskatoon, Canada.
The purpose of this study was to assess the effect of oral glutamine supplementation combined with resistance training in young adults. A group of 31 subjects, aged 18-24 years, were randomly allocated to groups (double blind) to receive either glutamine (0.9 g x kg lean tissue mass(-1) x day(-1); n = 17) or a placebo (0.9 g maltodextrin x kg lean tissue mass(-1) x day(-1); n = 14 during 6 weeks of total body resistance training. Exercises were performed for four to five sets of 6-12 repetitions at intensities ranging from 60% to 90% 1 repetition maximum (1 RM). Before and after training, measurements were taken of 1 RM squat and bench press strength, peak knee extension torque (using an isokinetic dynamometer), lean tissue mass (dual energy X-ray absorptiometry) and muscle protein degradation (urinary 3-methylhistidine by high performance liquid chromatography). Repeated measures ANOVA showed that strength, torque, lean tissue mass and 3-methylhistidine increased with training (P < 0.05), with no significant difference between groups. Both groups increased their 1 RM squat by approximately 30% and 1 RM bench press by approximately 14%. The glutamine group showed increases of 6% for knee extension torque, 2% for lean tissue mass and 41% for urinary levels of 3-methylhistidine. The placebo group increased knee extension torque by 5%, lean tissue mass by 1.7% and 3-methylhistidine by 56%. We conclude that glutamine supplementation during resistance training has no significant effect on muscle performance, body composition or muscle protein degradation in young healthy adults.
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J Strength Cond Res 2002 Feb;16(1):157-60
The effects of high-dose glutamine ingestion on weightlifting performance
Antonio J, Sanders MS, Kalman D, Woodgate D, Street C.
Sports Science Laboratory, University of Delaware, Newark, Delaware 19716, USA.
The purpose of this study was to determine if high-dose glutamine ingestion affected weightlifting performance. In a double-blind, placebo-controlled, crossover study, 6 resistance-trained men (mean +/- SE: age, 21.5 +/- 0.3 years; weight, 76.5 +/- 2.8 kg(-1)) performed weightlifting exercises after the ingestion of glutamine or glycine (0.3 g x kg(-1)) mixed with calorie-free fruit juice or placebo (calorie-free fruit juice only). Each subject underwent each of the 3 treatments in a randomized order. One hour after ingestion, subjects performed 4 total sets of exercise to momentary muscular failure (2 sets of leg presses at 200% of body weight, 2 sets of bench presses at 100% of body weight). There were no differences in the average number of maximal repetitions performed in the leg press or bench press exercises among the 3 groups. These data indicate that the short-term ingestion of glutamine does not enhance weightlifting performance in resistance-trained men.
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TweetI remember along time ago when one of these guys I knew thought he was taking Test Suspension and it was cortisol. I had 2bottles myself but I never took it , just through it out. He broke out really bad I mean some nasty shit. Not really sure how it effected his workouts and body weight , dont really remember.
TweetInt J Sports Med 2000 Jan;21(1):25-30 Related Articles, Links
The effect of free glutamine and peptide ingestion on the rate of muscle glycogen resynthesis in man.
van Hall G, Saris WH, van de Schoor PA, Wagenmakers AJ.
Department of Human Biology, Maastricht University, The Netherlands. 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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TweetMetabolism 2000 Dec;49(12):1555-60 Related Articles, Links
Intravenous glutamine does not stimulate mixed muscle protein synthesis in healthy young men and women.
Zachwieja JJ, Witt TL, Yarasheski KE.
Exercise and Nutrition Program, Pennington Biomedical Research Center, Baton Rouge, LA, USA.
We investigated the effects of a glutamine-supplemented amino acid mixture on vastus lateralis muscle protein synthesis rate in healthy young men and women. Three men and 3 women (27.8 +/- 2.0 yr, 22.2 +/- 1.0 body mass index [BMI], 56.1 +/- 4.5 kg lean body mass [LBM]) received a 14-hour primed, constant intravenous infusion of L[1-13C]leucine to evaluate the fractional rate of mixed muscle protein synthesis. In addition to tracer administration, a clinically relevant amino acid mixture supplemented with either glutamine or glycine in amounts isonitrogenous to glutamine, was infused. Amino acid mixtures were infused on separate occasions in random order at a rate of 0.04 g/kg/h (glutamine at approximately 0.01 g/kg/h) with at least 2 weeks between treatment. For 2 days before and on the day of an infusion, dietary intake was controlled so that each subject received 1.5 g protein/kg/d. Compared with our previous report in the postabsorptive state, amino acid infusion increased the fractional rate of mixed muscle protein synthesis by 48% (P < .05); however, the addition of glutamine to the amino acid mixture did not further elevate muscle protein synthesis rate (ie, 0.071% +/- 0.008%/h for amino acids + glutamine v 0.060% +/- 0.008%/h for amino acids + glycine; P = .316). Plasma glutamine concentrations were higher (P < .05) during the glutamine-supplemented infusion, but free intramuscular glutamine levels were not increased (P = .363). Both plasma and free intramuscular glycine levels were increased when extra glycine was included in the infused amino acid mixture (both P < .0001). We conclude that intravenous infusion of amino acids increases the fractional rate of mixed muscle protein synthesis, but addition of glutamine to the amino acid mixture does not further stimulate muscle protein synthesis rate in healthy young men and women.
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TweetJ Appl Physiol 2002 Sep;93(3):813-22 Related Articles, Links
Exercise-induced immunodepression- plasma glutamine is not the link.
Hiscock N, Pedersen BK.
Copenhagen Muscle Research Centre and Department of Infectious Diseases, Rigshospitalet, University of Copenhagen, DK-2100 Copenhagen, Denmark.
The amino acid glutamine is known to be important for the function of some immune cells in vitro. It has been proposed that the decrease in plasma glutamine concentration in relation to catabolic conditions, including prolonged, exhaustive exercise, results in a lack of glutamine for these cells and may be responsible for the transient immunodepression commonly observed after acute, exhaustive exercise. It has been unclear, however, whether the magnitude of the observed decrease in plasma glutamine concentration would be great enough to compromise the function of immune cells. In fact, intracellular glutamine concentration may not be compromised when plasma levels are decreased postexercise. In addition, a number of recent intervention studies with glutamine feeding demonstrate that, although the plasma concentration of glutamine is kept constant during and after acute, strenuous exercise, glutamine supplementation does not abolish the postexercise decrease in in vitro cellular immunity, including low lymphocyte number, impaired lymphocyte proliferation, impaired natural killer and lymphokine-activated killer cell activity, as well as low production rate and concentration of salivary IgA. It is concluded that, although the glutamine hypothesis may explain immunodepression related to other stressful conditions such as trauma and burn, plasma glutamine concentration is not likely to play a mechanistic role in exercise-induced immunodepression.
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TweetEffect of glutamine and protein supplementation on exercise-induced decreases in salivary IgA.
Krzywkowski K, Petersen EW, Ostrowski K, Link-Amster H, Boza J, Halkjaer-Kristensen J, Pedersen BK.
The Copenhagen Muscle Research Centre, Rigshospitalet, 2200 Copenhagen, Denmark.
Postexercise immune impairment has been linked to exercise-induced decrease in plasma glutamine concentration. This study examined the possibility of abolishing the exercise-induced decrease in salivary IgA through glutamine supplementation during and after intense exercise. Eleven athletes performed cycle ergometer exercise for 2 h at 75% of maximal oxygen uptake on 3 separate days. Glutamine (a total of 17.5 g), protein (a total of 68.5 g/6.2 g protein-bound glutamine), and placebo supplements were given during and up to 2 h after exercise. Unstimulated, timed saliva samples were obtained before exercise and 20 min, 140 min, 4 h, and 22 h postexercise. The exercise protocol induced a decrease in salivary IgA (IgA concentration, IgA output, and IgA relative to total protein). The plasma concentration of glutamine was decreased by 15% 2 h postexercise in the placebo group, whereas this decline was abolished by both glutamine and protein supplements.None of the supplements, however, was able to abolish the decline in salivary IgA. This study does not support that postexercise decrease in salivary IgA is related to plasma glutamine concentrations.
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