Lisäravinteet?

[cunccu]

Tutkimukset ovat paljon kontrolloidumpia, placebo-efekti jää pois

Kyllähän normi pakkislainen(, jolla on varaa ostaa isoja määriä eri lisäravinteita) hyötyy placebo-efektistäki. Jos mietitään noitten kaikkien mainittemies roska-aineitten yhteenlaskettuja lumevaikutuksia, niin kyllähän niillä kovastikki saadaan aikaan

 

[Thomppa]

Ei. Yksikään tutkimus ei tue käyttöä, jos proteiinin saanti olisi muutenkin runsasta. Glutamiini ja arginiini eivät tee oikein mitään. Leusiini tekee, mutta siitä ei ole todisteita, että optimaalisen määrän saavuttamiseen tulisi käyttää lisäravinteita.

Aletaa sitte vääntämää iha tosissaa kun ei tässä muukaan auta...


Arginiini

More than fifty research studies reportedly support the value of arginine supplementation for athletes. Arginine is considered to be key to efficient muscle metabolism because of its role in the transport, storage, and elimination of nitrogen. Creatine is derived from arginine, as are guanidophosphate and phosphoarginine, all of which have roles in muscle metabolism.

Colgan, Ph.D., Michael, Optimum Sports Nutrition: Your Competitive Edge (Ronkonkoma NY: 1993, Advanced Research Press), pages 268, 330, 333-334. ISBN 0-964840-5-9

Arginine facilitates a reduction in body fat, while increasing lean muscle mass. Arginine inhibits the absorption of dietary fat.

Balch, M.D., James F., and Balch, C.N.C, Phyllis A., Prescription for Nutritional Healing, Second Edition (Garden City Park, NY: 1997, Avery Publishing Group), pages 35-36. ISBN 0-89529-727-2

Arginine aids in liver detoxification by neutralizing ammonia, and may benefit in the treatment of liver disorders such as liver injury, hepatic cirrhosis, and fatty liver degeneration.

1. Braverman, M.D., E.R, The Healing Nutrients Within (New Canaan, CT: Keats Publishing, Inc., 1997), pages 18, 21-23, 212, 214, 219-221, 223, 228-229. ISBN 0-87983-706-3
2. Balch, M.D., James F., and Balch, C.N.C, Phyllis A., Prescription for Nutritional Healing, Second Edition (Garden City Park, NY: 1997, Avery Publishing Group), pages 35-36. ISBN 0-89529-727-2
3. Hendler, M.D., Ph.D., Sheldon Saul, The Doctor's Vitamin and Mineral Encyclopedia (New York: 1990, Fireside), pages 209-215. ISBN 0-671-66784-X

L-glutamiini

L-glutamine is the most prevalent amino acid in the bloodstream and because human cells readily synthesize it, is usually considered a non-essential amino acid. It is found in high concentration in skeletal muscle, lung, liver, brain, and stomach tissue. Skeletal muscle contains the greatest intracellular concentration of glutamine, comprising up to 60 percent of total body glutamine stores, and is considered the primary storage depot and exporter of glutamine to other tissues. Under certain pathological circumstances the body's tissues need more glutamine than the amount supplied by diet and biosynthesis. During catabolic stress intracellular glutamine levels can drop more than 50 percent, and it is under these circumstances that supplemental glutamine becomes necessary.

1. Souba WW. Glutamine Physiology, Biochemistry, and Nutrition in Critical Illness. Austin, TX: R.G. Landes Co.; 1992.

Näitä on NIIIIIIIIIIIIIIIIIIIIIIIIIIIIIIIN paljon, etten jaksa edes enempää laittaa. Ja sä väität, ettei ole yhtään puolesta?

 

[ysikymppinen]

Arginiinista.

Dig Dis Sci. 2007 Aug;52(8):1826-32. Epub 2007 Apr 4.
Lack of effect of acute enteral arginine infusion on whole-body and intestinal protein metabolism in humans.

Claeyssens S, Lecleire S, Leblond J, Marion R, Hecketsweiler B, Lavoinne A, Ducrotté P, Déchelotte P, Coëffier M.

Appareil Digestif, Environnement et Nutrition (ADEN EA 3234), Institut Fédératif de Recherche Multidisciplinaire sur les Peptides, and CIC-INSERM-CHU, Rouen, France.

Arginine is a conditionally essential amino acid and exerts anabolic effects. We studied the effects of enteral arginine on whole-body and duodenal protein metabolism. Eight healthy fasted volunteers received randomly a 5-hr enteral infusion of either arginine (Arg; 20 g) or an isonitrogenous amino acid mixture (AA) and an IV infusion of [13C]leucine. Duodenal biopsies were performed. Whole-body protein turnover and duodenal protein synthesis (FSR) were calculated from GC/MS-assessed enrichment. The mRNA levels for major components of proteolytic pathways, ubiquitin, cathepsin D, and m-calpain, were evaluated by RT-PCR. Results were compared using paired Wilcoxon test. Endogenous, oxidative, and nonoxidative leucine fluxes were not different after Arg and AA infusions, respectively. Duodenal mucosal protein FSR (71% +/- 26% vs 81% +/- 30%/day) and mRNA levels of ubiquitin, cathepsin D, and m-calpain were also similar after Arg and AA infusions. We conclude that in healthy subjects, arginine infusion exerts no effect on whole-body and duodenal protein metabolism. Whether arginine might specifically affect these parameters in catabolic or inflammatory situations remains to be determined.

Med Sci Sports Exerc. 2009 Apr;41(4):773-9.
Hemodynamic and vascular response to resistance exercise with L-arginine.

Fahs CA, Heffernan KS, Fernhall B.

Department of Kinesiology and Community Health, Exercise and Cardiovascular Research Laboratory, University of Illinois at Urbana-Champaign, Champaign, IL 61820, USA.

PURPOSE: L-arginine, the precursor to nitric oxide (NO), has been shown to improve endothelial function in patients with endothelial dysfunction. Resistance exercise has been shown to increase arterial stiffness acutely with no definitive cause. It is possible that a reduction in NO bioavailability is responsible for this. The purpose of this study was to examine the effect of acute L-arginine supplementation and resistance exercise on arterial function. METHODS: Eighteen (N = 18) young men (24.2 +/- 0.7 yr) volunteered for this study. In a crossover design, subjects underwent body composition testing, 1-repetition maximum testing for the bench press and the biceps curls and performed two acute bouts of resistance exercise in which they consumed either placebo or 7 g L-arginine before each resistance exercise bout. Anthropometric measures, augmentation index (AIx), arterial stiffness, and forearm blood flow (FBF) were assessed before and after each treatment condition. RESULTS: There were significant (P < 0.05) time effects after the resistance exercise; there was a reduction in brachial stiffness (P = 0.0001), an increase in central aortic stiffness (P = 0.004), an increase in AIx (P = 0.023), an increase in FBF (P = 0.000), and an increase in arm circumference (P = 0.0001) after exercise. CONCLUSIONS: The increase in central arterial stiffness and wave reflection was not attenuated by acute supplementation with L-arginine; furthermore, blood flow was not augmented with supplementation. On the basis of these data, l-arginine does not appear to change the hemodynamic and vascular responses to resistance exercise.

Arginiinin käyttäminen NO:n (Nitric Oxide) aktivointiin ei oikein ole perusteltua, koska normaalilla ihmisellä arginiinitasot ovat jo tarpeeksi korkealla.

Insulin and the arginine paradox.
S Kurz and D G Harrison
J Clin Invest. 1997 February 1; 99(3): 369–370

An implicit, and often stated, conclusions from these studies is that a deficiency of arginine exists, such that this amino acid is rate limiting in terms of NO synthase activity. The perplexing aspect of that is that the intracellular concentration of arginine far exceeds the Km of NO synthases. Therefore it seems unlikely that L-arginine colud ever be rate limiting in vivo.

1: J Nutr Biochem. 2008 Aug 15. [Epub ahead of print]Click here to read Links
No effect of short-term arginine supplementation on nitric oxide production, metabolism and performance in intermittent exercise in athletes.
Liu TH, Wu CL, Chiang CW, Lo YW, Tseng HF, Chang CK.

Department of Physical Education, Taiwan Sport University, 404 Taichung, Taiwan.

Arginine supplementation has been shown to alleviate endothelial dysfunction and improve exercise performance through increasing nitric oxide production in patients with cardiopulmonary diseases. In addition, arginine supplementation could decrease accumulations of lactate and ammonia, metabolites involved in development of muscular fatigue. The aim of this study was to investigate the effect of short-term arginine supplementation on performance in intermittent anaerobic exercise and the underlying mechanism in well-trained male athletes. Ten elite male college judo athletes participated with a randomized crossover, placebo-controlled design. The subjects consumed 6 g/day arginine (ARG trial) or placebo (CON trial) for 3 days then performed an intermittent anaerobic exercise test on a cycle ergometer. Blood samples were collected before supplementation, before and during exercise and 0, 3, 6, 10, 30 and 60 min after exercise. ARG trial had significantly higher arginine concentrations than CON trial at the same time point before, during and after exercise. In both trials, nitrate and nitrite concentration was significantly higher during and 6 min after exercise comparing to the basal concentration. The increase in nitrate and nitrite concentration during exercise in both trials was parallel to the increase in plasma citrulline concentrations. There was no significant difference between the 2 trials in plasma nitrate and nitrite, lactate and ammonia concentrations and peak and average power in the exercise. The results of this study suggested that short-term arginine supplementation had no effect on nitric oxide production, lactate and ammonia metabolism and performance in intermittent anaerobic exercise in well-trained male athletes

Int J Sports Med. 2005 Jun;26(5):344-9.
Influence of chronic supplementation of arginine aspartate in endurance athletes on performance and substrate metabolism - a randomized, double-blind, placebo-controlled study.

Abel T, Knechtle B, Perret C, Eser P, von Arx P, Knecht H.

Institute of Sports Medicine, Swiss Paraplegic Centre, Nottwil.

The intake of arginine aspartate has been shown to increase anabolic hormones like human growth hormone (hGH) and glucagon. The aim of our study was to investigate whether daily intake of two different dosages of arginine asparate during four weeks affects selected parameters of overtraining syndrome like performance, metabolic and endocrine parameters. Thirty male endurance-trained athletes were included in a randomized, double-blind, placebo-controlled study and divided into three groups. During four weeks, they ingested either arginine aspartate with a high concentration (H) of 5.7 g arginine and 8.7 g aspartate, with a low concentration (L) of 2.8 g arginine and 2.2 g aspartate or placebo (P).VO(2)peak and time to exhaustion were determined on a cycling ergometer in an incremental exercise test before and after supplementation. Before and after each incremental exercise test, concentrations of hGH, glucagon, testosterone, cortisol, ferritine, lactate, and urea were measured. Compared to placebo, no significant differences on endurance performance (VO(2)peak, time to exhaustion), endocrine (concentration of hGH, glucagon, cortisol, and testosterone) and metabolic parameters (concentration of lactate, ferritine, and urea) were found after chronic arginine aspartate supplementation. The chronic intake of arginine asparate during four weeks by male endurance athletes showed independent of dosage no influence on performance, selected metabolic or endocrine parameters. Consequently, there seems to be no apparent reason why the supplementation of arginine aspartate should be an effective ergogenic aid. The practice of using arginine aspartate as potential ergogenics should be critically reevaluated. Further investigations with higher dosage and extended supplementation periods should be performed.

Plasma arginine, citrulline, and ornithine kinetics in adults, with observations on nitric oxide synthesis

L. Castillo, M. Sanchez, J. Vogt, T. E. Chapman, T. C. DeRojas-Walker, S. R. Tannenbaum, A. M. Ajami and V. R. Young
Laboratory of Human Nutrition, School of Science, Massachusetts Institute of Technology, Cambridge 02139.

The plasma fluxes of ornithine (Orn), arginine (Arg), and citrulline (Cit) and rate of conversion of labeled ornithine-to-citrulline (QOrn-->Cit) were estimated in six healthy adult men receiving an arginine-rich or arginine-free L-amino acid-based diet, each for 6 days. On day 7 an 8-h (3-h fast, 5-h fed) primed continuous intravenous infusion of L-[guanido-15N,15N] arginine, L-[ureido-13C]citrulline, L-[5,5,2H2]ornithine, and L-[5,5,5-2H3]leucine was conducted. Mean citrulline fluxes (mumol.kg-1.h-1) were 10.4-13.6 for the various conditions and/or diets and remained unchanged (P > 0.05). Arginine flux was lowered (P < 0.01) by 38% for fed state during arginine-free period. Ornithine fluxes for arginine-rich were (P < 0.01) reduced with the arginine-free diet. Rates of QOrn-->Cit declined by 30% (P < .05) during the fed arginine-free period. Short-term restriction in the dietary supply of arginine did not alter the rate of whole body nitric oxide synthesis. One subject showed a very high output of nitrate on arginine-free diet (6 times average for remaining subjects)

Arq Bras Endocrinol Metabol. 2007 Jun;51(4):587-92. Links
[Effect of L-arginine supplementation on secretion of human growth hormone and insulin-like growth factor in adults]

[Article in Portuguese]


Fayh AP, Friedman R, Sapata KB, de Oliveira AR.
Laboratório de Pesquisa do Exercício, Escola de Educação Física, Universidade Federal do Rio Grande do Sul, Rua Felizardo 750, 90690-200 Porto Alegre, RS. apfayh@yahoo.com.br
Based on presumptions that the infusion of amino acids can augment the release of human growth hormone (hGH) and that this metabolism is related with secretion of insulin-like growth factor I (IGF-I), the purpose of this study was to verify the effect of L-arginine supplementation on GH and IGF-I in adults. Seventeen male individuals participated on the study and were randomized to receive L-arginine (n= 10) or placebo (n= 7), seven grams per day for seven days. Before and after the supplementation period, the volunteers realized blood collection in fasting to verify both GH and IGF-I levels, as well as urine collection to verify urea excretion. At the end of the experimental period, it was verified that the group that received L-arginine augmented the urea in urine excretion (to 2684.1 +/- 475.2 mg/dl from 2967.2 +/- 409.7 mg/dl, p= 0.002), therefore it did not alter significantly the release of hormones evaluated. The group which received placebo did not alter significantly any evaluated parameters. The L-arginine supplementation during seven days was ineffective to augment both GH and IGF-I release in individual male adults[/QUOTE]

Oral arginine attenuates the growth hormone response to resistance exercise
S. R. Collier, E. Collins, and J. A. Kanaley

Department of Exercise Science, Syracuse University, Syracuse, New York

Submitted 7 March 2006 ; accepted in final form 23 May 2006

This study investigated the combined effect of resistance exercise and arginine ingestion on spontaneous growth hormone (GH) release. Eight healthy male subjects were studied randomly on four separate occasions [placebo, arginine (Arg), placebo + exercise (Ex), arginine + exercise (Arg+Ex)]. Subjects had blood sampled every 10 min for 3.5 h. After baseline sampling (30 min), subjects ingested a 7-g dose of arginine or placebo (blinded, randomly assigned). On the exercise days, the subject performed 3 sets of 9 exercises, 10 repetitions at 80% one repetition maximum. Resting GH concentrations were similar on each study day. Integrated GH area under the curve was significantly higher on the Ex day (508.7 ? 169.6 min?ng/ml; P < 0.05) than on any of the other study days. Arg+Ex (260.5 ? 76.8 min?ng/ml) resulted in a greater response than the placebo day but not significantly greater than the Arg day. The GH half-life and half duration were not influenced by the stimulus administered. The GH secretory burst mass was larger, but not significantly, on the Arg, Ex, and Arg+Ex day than the placebo day. Endogenous GH production rate (Ex > Arg+Ex > Arg > placebo) was greater on the Ex and Arg+Ex day than on the placebo day (P < 0.05) but there were no differences between the Ex and Arg+Ex day. Oral arginine alone (7 g) stimulated GH release, but a greater GH response was seen with exercise alone. The combined effect of arginine before exercise attenuates the GH response. Autonegative feedback possibly causes a refractory period such that when the two stimuli are presented there will be suppression of the somatotrope.

J Cardiovasc Pharmacol. 1996 Jul;28(1):158-66.
Effects of in vivo and in vitro L-arginine supplementation on healthy human vessels.

Chin-Dusting JP, Alexander CT, Arnold PJ, Hodgson WC, Lux AS, Jennings GL.

Alfred and Baker Medical Unit, Baker Medical Research Institute, Prahran, Victoria, Australia.

We studied the influence of dietary L-arginine (L-ARG) supplementation on forearm resistance arteries in vivo and the effect of exogenous addition of L-ARG to subcutaneous arteries isolated from gluteal biopsies. Twenty-six healthy males were recruited, and 16 were randomly allocated in a double-blind protocol to receive either oral L-ARG 20 g/day or placebo for 28 days. We examined responses to acetylcholine (ACh), sodium nitroprusside (SNP) and NG-monomethyl-L-arginine (L-NMMA) on forearm resistance arteries using venous occlusion plethysmography performed before and after supplementation of L-ARG (or placebo). L-ARG 20 g/day had no effect on plasma L-ARG levels (% mol based on total amino acid pool; before vs. after L-ARG 3.43 +/- 0.31 vs. 3.76 +/- 0.05), weekly blood pressure (BP) measurements, or plasma biochemical analysis of liver function enzymes, urea, or electrolyte levels. On the other hand, analysis of the major amino acids in plasma showed a significant difference in profile after L-ARG, but not placebo supplementation (Mann Whitney U test, p < 0.05), indicating a domino effect of chronic oral L-ARG supplementation on other amino acids. This may result from a change in appetite and thus protein intake after L-ARG supplementation. At the dose given, neither L-ARG nor placebo had any effect on forearm blood flow (FBF) responses to ACh (area under the dose-response curve, before vs. after L-ARG 1,763 +/- 260.1 vs. 1,862.8 +/- 163.6 U, Student's paired t test; p > 0.05), SNP, or L-NMMA. Gluteal skin biopsies were performed on 10 different untreated subjects. Subcutaneous arteries were isolated and mounted as ring preparations in isometric small vessel myographs. Full concentration-response curves to norepinephrine (NE), ACh, substance P, and a single response to SNP (10 microM) were obtained with and without addition of either L- or D-ARG 10 microM. Both L-ARG [-log EC50 (M) before vs. after arginine 7.12 +/- 0.15 vs. 6.66 +/- 0.16, Student's paired t test, p < 0.005] and D-ARG [-log EC50 (M) before vs. after arginine 7.36 +/- 0.17 vs. 6.85 +/- 0.18; Student's paired t test, p < 0.05] significantly antagonized responses to NE in subcutaneous arteries isolated from healthy humans. With the exception of a subset of vessels in which some endothelial dysfunction was observed, neither of the isomers of arginine had any effect on the responses to ACh, substance P, or SNP. In the subset vessels already described (n = 5), in which responses to ACh were < 90% maximal dilatation, L- but not D-ARG significantly increased the potency to ACh [-log EC50 (M) before vs. after L-ARG 7.42 +/- 0.20 vs. 8.27 +/- 0.28. Student's paired t test, p < 0.05]. We conclude that oral supplementation with L-ARG 20 g/day for 28 days does not affect endothelial function in normal healthy adults, possibly because the dose given in the current study was inadequate or because chronic oral administration leads to dissipation of arginine to other pathways, as evidenced by the change in total amino acid profile but not L-ARG plasma concentration, or because L-ARG cannot improve normal endothelium-mediated vasodilatation. These concepts are supported by our findings that responses to ACh and substance P were not altered by L-ARG in subcutaneous arteries isolated from healthy subjects.

Regul Toxicol Pharmacol. 2008 Apr;50(3):376-99. Epub 2008 Jan 26.
Risk assessment for the amino acids taurine, L-glutamine and L-arginine.

Shao A, Hathcock JN.

Council for Responsible Nutrition, 1828 L Street, NW, Suite 900, Washington, DC 20036-5114, USA. ashao@crnusa.org

Taurine, glutamine and arginine are examples of amino acids which have become increasingly popular as ingredients in dietary supplements and functional foods and beverages. Animal and human clinical research suggests that oral supplementation of these amino acids provides additional health and/or performance benefits beyond those observed from normal intake of dietary protein. The increased consumer awareness and use of these amino acids as ingredients in dietary supplements and functional foods warrant a comprehensive review of their safety through quantitative risk assessment, and identification of a potential safe upper level of intake. The absence of a systematic pattern of adverse effects in humans in response to orally administered taurine (Tau), l-glutamine (Gln) and l-arginine (Arg) precluded the selection of a no observed adverse effect level (NOAEL) or lowest observed adverse effect level (LOAEL). Therefore, by definition, the usual approach to risk assessment for identification of a tolerable upper level of intake (UL) could not be used. Instead, the newer method described as the Observed Safe Level (OSL) or Highest Observed Intake (HOI) was utilized. The OSL risk assessments indicate that based on the available published human clinical trial data, the evidence for the absence of adverse effects is strong for Tau at supplemental intakes up to 3 g/d, Gln at intakes up to 14 g/d and Arg at intakes up to 20 g/d, and these levels are identified as the respective OSLs for normal healthy adults. Although much higher levels of each of these amino acids have been tested without adverse effects and may be safe, the data for intakes above these levels are not sufficient for a confident conclusion of long-term safety, and therefore these values are not selected as the OSLs.

Int J Sports Med. 1999 Jul;20(5):315-21.
The effect of arginine or glycine supplementation on gastrointestinal function, muscle injury, serum amino acid concentrations and performance during a marathon run.

Buchman AL, O'Brien W, Ou CN, Rognerud C, Alvarez M, Dennis K, Ahn C.

Division of Gastroenterology, Hepatology and Nutrition, University of Texas Houston Health Science Center, USA. abuchman@heart-med.uth.tmc.edu

Gastrointestinal bleeding and increased intestinal permeability have been observed in marathon runners. We sought to determine if L-arginine would be useful for prevention of these complications. Twenty-three runners were randomized to receive L-arginine (A) or glycine (placebo) (G), 10 grams 3 times daily for 14 days prior to the 1997 Houston-Methodist Marathon. Serum, stool hemoccults and lactulose:mannitol permeabilities were obtained at baseline, immediately after completion of the marathon and approximately 48 hours later. Runners rated their symptoms of nausea and vomiting, belching and indigestion, abdominal pain and bloating, diarrhea, and extremity pain on a 1-5 scale of increasing severity. The L:M was unchanged in either group during the three collections. Occult bleeding occurred in 8%/20% in A and G groups, respectively, p = NS) immediately post-marathon. No runners had occult bleeding 48 hours post-race. Gastrointestinal symptom scores were minimal to nonexistent. Extremity pain scores were similar for groups A and G (2.1+/-1.4 and 2.8+/-1.6, respectively, (p = NS). Fluid intake was similar between both groups (1875+/-1547 vs. 1506+/-970 ml, p = NS). Serum amylase was normal at baseline and remained virtually unchanged. Serum lipase was normal at baseline and immediately post-race in both groups, but increased at 48 hours post-race (82.2+/-34.3 to 121.5+/-53.3 mg/dl [A], p = 0.02 and 114.3+/-55.7 to 181.9+/-162.2 mg/dl [G], p = 0.09). CPK increased significantly and similarly in both groups immediately post-race, and even more dramatically 48 hours post-race (130.3+/-130.8 to 738.8+/-902.9, p = 0.007 to 1966.5+/-3.166.0 mg/dl [A] and 140.9+/-77.9 to 863.0+/-772.3, p = 0.003 to 5619+/-10636.8mg/dl [G]). Modest post-race decreases were seen in most serum amino acids in both groups. Finish times were longer than predicted (23+/-21 and 9+/-7 min for A and G groups, respectively, p = 0.049). Our study failed to show a clear benefit of arginine supplementation for the prevention of intestinal ischemia/reperfusion injury associated with endurance running, but either a detrimental affect on performance with arginine, or enhanced performance with glycine. Skeletal muscle injury was unaffected by arginine or glycine supplementation. The delayed increase in serum lipase suggests mild pancreatic injury, affected by either arginine or glycine supplementation.

1: J Appl Physiol. 1988 Aug;65(2):579-84. Links
Body composition response to exogenous GH during training in highly conditioned adults.
Crist DM, Peake GT, Egan PA, Waters DL.

Department of Medicine, University of New Mexico School of Medicine, Albuquerque 87131.

The effects of biosynthetic methionyl-human growth hormone (met-hGH) on body composition and endogenous secretion of growth hormone (GH) and insulin-like growth factor I (IGF-I) were studied in eight well-trained exercising adults between 22 and 33 yr of age. By the use of double-blind procedures, met-hGH (2.67 mg/0.5 ml diluent, 3 days/wk) and bacteriostatic water (placebo, 0.5 ml, 3 days/wk) were administered in a repeated-measures design that counterbalanced treatment order. Duration of each treatment was 6 wk. Subjects trained with progressive resistance exercise throughout and were maintained on a high-protein diet monitored by extensive compositional analyses of daily dietary intake records. Hydrodensitometry revealed that met-hGH significantly decreased percent body fat (%fat) and increased fat-free weight (FFW) and FFW/fat weight (FW), whereas the placebo treatment did not change any of these measures. Changes in FFW/FW correlated with the relative dose of met-hGH but did not correlate with either the peak GH response to L-dopa/arginine stimulation or IGF-I levels obtained after treatment with placebo. There were no differences between treatments in the dietary intakes of total kilocalories, protein, carbohydrates, and fat. Mean IGF-I levels were elevated after treatment with met-hGH compared with postplacebo levels. After treatment with met-hGH, five of seven subjects had a suppressed GH response to stimulation from either L-dopa/arginine or submaximal exercise. We conclude that supraphysiological doses of met-hGH will alter body composition in exercising adults in a relative dose-dependent manner and that such treatment may suppress endogenous release of GH in some individuals.

American Journal of Clinical Nutrition, Vol. 72, No. 1, 96-105, July 2000

Plasma insulin responses after ingestion of different amino acid or protein mixtures with carbohydrate1,2,3
Luc JC van Loon, Wim HM Saris, Hans Verhagen and Anton JM Wagenmakers

The data in this study show clearly that oral ingestion of large amounts of free arginine (0.4 g arginine•kg body wt-1•h-1, as ingested in trial 2) is not an effective means of increasing plasma insulin concentrations (Figure 4AGo) and plasma arginine concentrations (Table 3Go). Ingestion of drink 2 caused severe diarrhea and the urge to defecate in all subjects for several hours during and after the trial. These gastrointestinal problems appeared to prevent intestinal absorption of the arginine because lower concentrations of arginine were seen in plasma after ingestion of drink 2 than after ingestion of drinks 3, 4, and 10 (ingestion rates of 0.13, 0.10, and 0.07 g arginine•kg body wt-1•h-1, respectively). These problems also indicate that in sports practice, ingestion of large amounts of arginine to stimulate growth hormone release and muscle anabolism is not recommended. On the other hand, low doses of arginine (<2 g), as present in commercial sports supplements, do not increase plasma insulin and growth hormone concentrations (23–25).

 

[Mike]

Onko sun mielestä kehoaan raskaasti rasittava normaali ihminen ja keho sekä ruoansulatus normaalissa tilassa?

 

[ysikymppinen]

More than fifty research studies reportedly support the value of arginine supplementation for athletes. Arginine is considered to be key to efficient muscle metabolism because of its role in the transport, storage, and elimination of nitrogen. Creatine is derived from arginine, as are guanidophosphate and phosphoarginine, all of which have roles in muscle metabolism.
Colgan, Ph.D., Michael, Optimum Sports Nutrition: Your Competitive Edge (Ronkonkoma NY: 1993, Advanced Research Press), pages 268, 330, 333-334. ISBN 0-964840-5-9

Vuodelta 1993. Tuon jälkeen on menty paljon eteenpäin. Lue edellinen postaukseni.

Arginine facilitates a reduction in body fat, while increasing lean muscle mass. Arginine inhibits the absorption of dietary fat.
Balch, M.D., James F., and Balch, C.N.C, Phyllis A., Prescription for Nutritional Healing, Second Edition (Garden City Park, NY: 1997, Avery Publishing Group), pages 35-36. ISBN 0-89529-727-2

Perusteet/lähteet, että tähän tarvitaan arginiinia lisäravinteena.

Arginine aids in liver detoxification by neutralizing ammonia, and may benefit in the treatment of liver disorders such as liver injury, hepatic cirrhosis, and fatty liver degeneration.
1. Braverman, M.D., E.R, The Healing Nutrients Within (New Canaan, CT: Keats Publishing, Inc., 1997), pages 18, 21-23, 212, 214, 219-221, 223, 228-229. ISBN 0-87983-706-3
2. Balch, M.D., James F., and Balch, C.N.C, Phyllis A., Prescription for Nutritional Healing, Second Edition (Garden City Park, NY: 1997, Avery Publishing Group), pages 35-36. ISBN 0-89529-727-2
3. Hendler, M.D., Ph.D., Sheldon Saul, The Doctor's Vitamin and Mineral Encyclopedia (New York: 1990, Fireside), pages 209-215. ISBN 0-671-66784-X

Ja nämä jutut auttavat normipakkislaista miten?

L-glutamiini

L-glutamine is the most prevalent amino acid in the bloodstream and because human cells readily synthesize it, is usually considered a non-essential amino acid. It is found in high concentration in skeletal muscle, lung, liver, brain, and stomach tissue. Skeletal muscle contains the greatest intracellular concentration of glutamine, comprising up to 60 percent of total body glutamine stores, and is considered the primary storage depot and exporter of glutamine to other tissues. Under certain pathological circumstances the body's tissues need more glutamine than the amount supplied by diet and biosynthesis. During catabolic stress intracellular glutamine levels can drop more than 50 percent, and it is under these circumstances that supplemental glutamine becomes necessary.
1. Souba WW. Glutamine Physiology, Biochemistry, and Nutrition in Critical Illness. Austin, TX: R.G. Landes Co.; 1992.

Mikään tässä ei viittaa, että glutamiinia pitäisi käyttää lisäravinteena. Odotapa puolisen tuntia niin teen samankaltaisen läpkatsauksen glutamiinin kuin tein edellisessä postauksessani arginiinin.

Näitä on NIIIIIIIIIIIIIIIIIIIIIIIIIIIIIIIN paljon, etten jaksa edes enempää laittaa. Ja sä väität, ettei ole yhtään puolesta?

Et kuitenkaan laittanut yhtään viitteitä siihen, että arginiinia ja glutamiinia tarvitsisi lisäravinteena.

 

[ysikymppinen]

Onko sun mielestä kehoaan raskaasti rasittava normaali ihminen ja keho sekä ruoansulatus normaalissa tilassa?

Normaalitilassa tarkoitin, että ihmisellä ei ole jotain kroonista tai akuuttia sairautta, jolloin (tietyissä sairauksissa) glutamiinista ja arginiinista voi olla apua. Mutta tämä ei päde normipakkislaiseen.

 

[Thomppa]

Joo hyvä saatiin tähänkin ketjuun pari kymmentä sivua lainauksia tutkimustiedoista. Entä sitten? Tilanne ei muuttunut yhtikäs mihinkää. Se missä olit väärässä, noita tutkimuksia on myös puoltavia, ei vain ja ainoastaan vastaisia. Se on taas jokaisen oma asia mitä pitää oikeana ja mihin uskoo. Itse en käytä prodejauhojen,krean, kalaöljyn ja d-vitamiinin lisäksi mitään muita, koska en näe niitä tarpeelliseksi itselleni, enkä normitreenajalle. Plus tekee aika ison loven lompakkoon pitkällä aikavälillä. Eli en voi itse sanoa käytännön tasolla mitään esim. arginiin toimivuudesta, kun ei ole tullut kokeiltua. Mutta kyllä on sulla hienoja tutkimuksia. Käytännön kokemukset vain puhuvat taas puolestaan ja uskon mieluusti enemmän niitä (mm. lukuisat ammattilais kehonrakentajat). Vaikken edelleenkään näe näillä 'hifi' lisäravinteille normitreenaajalle käyttöä.

e.

Normaalitilassa tarkoitin, että ihmisellä ei ole jotain kroonista tai akuuttia sairautta, jolloin (tietyissä sairauksissa) glutamiinista ja arginiinista voi olla apua. Mutta tämä ei päde normipakkislaiseen.

Miten niistä voi olla apua, jos ne kerta EIVÄT TOIMI? Miten ****tussa se on mahdollista. Eihän lääkeaineistakaan normaalitilassa ole suurta hyöytä...

 

[Mike]

Ja luulet, että esim jonkun jalkatreenin jälkeen keho on ihan normaalissa tilassa ja voit popsia huoletta kananrintaa? Vai olisko tässä aikapaljon muuttujia, jotka puoltavat määrättyjen ravinteiden käyttöä?

 

[Thomppa]

Et kuitenkaan laittanut yhtään viitteitä siihen, että arginiinia ja glutamiinia tarvitsisi lisäravinteena.

Kyllä olen kirjoittanut varsin vahvoja perusteita, miksi tulisi käyttää lisäravinteena. Lues ajatuksella tai sitten oot väärällä foorumilla.

 

[-Alfa-]

Ja luulet, että esim jonkun jalkatreenin jälkeen keho on ihan normaalissa tilassa ja voit popsia huoletta kananrintaa?

Totta. Ei ole niin pienintäkään pelkoa että kunnon jalkatreenin jälkeen pystyis syömään mitään kiinteää.

Ei onnistu, pakki menee välittömästi nurin.

 

[ysikymppinen]

edit. sori kone temppuili...

 

[ysikymppinen]

Tässä jotain.

Review

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.

Int J Sports Med. 2000 Jan;21(1):25-30.
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.

Metabolism. 2000 Dec;49(12):1555-60.
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.

Med Sci Sports Exerc. 1998 Jun;30(6):856-62.
Effect of glutamine supplementation on changes in the immune system induced by repeated exercise.

Rohde T, MacLean DA, Pedersen BK.

Copenhagen Muscle Research Centre, Department of Infectious Diseases M, Rigshospitalet, University Hospital, Denmark. trohde@rh.dk

The ability of lymphocytes to proliferate and generate lymphokine activated killer (LAK) cell activity in vitro is dependent on glutamine. In relation to intense exercise the lymphocyte concentration, the proliferative response, the natural killer and LAK cell activity, and the plasma glutamine concentration decline. It has been hypothesized that in relation to physical activity a lack of glutamine may temporarily affect the function of the immune system. PURPOSE: The purpose of this study was to examine the influence of glutamine supplementation on exercise-induced immune changes. METHODS: In a randomized cross-over placebo-controlled study, eight healthy male subjects performed three bouts of ergometer bicycle exercise lasting 60, 45, and 30 min at 75% of their VO2max separated by 2 h of rest. RESULTS: The arterial plasma glutamine concentration declined from 508 +/- 35 (pre-exercise) to 402 +/- 38 microM (2 h after the last exercise bout) in the placebo trial and was maintained above pre-exercise levels in the glutamine supplementation trial. The numbers of circulating lymphocytes and the phytohemagglutinin-stimulated lymphocyte proliferative response declined 2 h after, respectively, during each bout of exercise, whereas the LAK cell activity declined 2 h after the third bout. Glutamine supplementation in vivo, given in the described doses at the specific times, did not influence these changes. CONCLUSION: The present study does not appear to support the hypothesis that those aspects of postexercise immune changes studied are caused by decreased plasma glutamine concentrations.

Am J Physiol Cell Physiol. 2001 Oct;281(4):C1259-65.
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.

Br J Sports Med 1998;32:25-32 doi:10.1136/bjsm.32.1.25
Contrasting plasma free amino acid patterns in elite athletes: association with fatigue and infection.

1. K J Kingsbury,
2. L Kay,
3. M Hjelm

+ Author Affiliations

1.
MDL Laboratory, London, United Kingdom.

Abstract

AIM: There is little information on the plasma free amino acid patterns of elite athletes against which fatigue and nutrition can be considered. Therefore the aim was to include analysis of this pattern in the medical screening of elite athletes during both especially intense and light training periods. METHODS: Plasma amino acid analysis was undertaken in three situations. (1) A medical screening service was offered to elite athletes during an intense training period before the 1992 Olympics. Screening included a blood haematological/biochemical profile and a microbial screen in athletes who presented with infection. The athletes were divided into three groups who differed in training fatigue and were considered separately. Group A (21 track and field athletes) had no lasting fatigue; group B (12 judo competitors) reported heavy fatigue at night but recovered overnight to continue training; group C (18 track and field athletes, one rower) had chronic fatigue and had been unable to train normally for at least several weeks. (2) Athletes from each group were further screened during a post-Olympic light training period. (3) Athletes who still had low amino acid levels during the light training period were reanalysed after three weeks of additional protein intake. RESULTS: (1) The pre-Olympics amino acid patterns were as follows. Group A had a normal amino acid pattern (glutamine 554 (25.2) micromol/l, histidine 79 (6.1) micromol/l, total amino acids 2839 (92.1) micromol/l); all results are means (SEM). By comparison, both groups B and C had decreased plasma glutamine (average 33%; p<0.001) with, especially in group B, decreased histidine, glucogenic, ketogenic, and branched chain amino acids (p<0.05 to p<0.001). None in group A, one in group B, but ten athletes in group C presented with infection: all 11 athletes had plasma glutamine levels of less than 450 micromol/l. No intergroup differences in haematological or other blood biochemical parameters, apart from a lower plasma creatine kinase activity in group C than in group B (p<0.05) and a low neutrophil to lymphocyte ratio in the athletes with viral infections (1.2 (0.17)), were found. (2) During post-Olympic light training, group A showed no significant amino acid changes. In contrast, group B recovered normal amino acid levels (glutamine 528 (41.4) micromol/l, histidine 76 (5.3) micromol/l, and total amino acids 2772 (165) micromol/l) (p<0.05 to p<0.001) to give a pattern comparable with that of group A, whereas, in group C, valine and threonine had increased (p<0.05), but glutamine (441 (24.5) micromol/l) and histidine (58 (5.3) micromol/l) remained low. Thus none in group A, two in group B, but ten (53%) in group C still had plasma glutamine levels below 450 micromol/l, including eight of the 11 athletes who had presented with infection. (3) With the additional protein intake, virtually all persisting low glutamine levels increased to above 500 micromol/l. Plasma glutamine rose to 592 (35.1) micromol/l and histidine to 86 (6.0) micromol/l. Total amino acids increased to 2761 (128) micromol/l (p<0.05 to p<0.001) and the amino acid pattern normalised. Six of the ten athletes on this protein intake returned to increased training within the three weeks. CONCLUSION: Analysis of these results provided contrasting plasma amino acid patterns: (a) a normal pattern in those without lasting fatigue; (b) marked but temporary changes in those with acute fatigue; (c) a persistent decrease in plasma amino acids, mainly glutamine, in those with chronic fatigue and infection, for which an inadequate protein intake appeared to be a factor.

The Effects Of Glutamine On Muscle Strength And Body Composition: 241 Board #148 11:00 AM - 12:30 PM
Thistlethwaite, John R.; Swanson, Scott C.; Scheuermann, Barry W.

Medicine & Science in Sports & Exercise:
May 2005 - Volume 37 - Issue 5 - p S45


METHODS

This study included 12 subjects (21 ± 2 yrs) who were randomly assigned to: glutamine (GL; n=6) or control (Con; n=6) groups. All subjects underwent 7 wks of resistive training (2 sessions/wk) involving bench press, shoulder (military) press, and leg squat exercise. Workload was determined from pre-training measurements of one repetition maximum (RM). The training program consisted of 1 set of 8 repetitions at 60% RM, 1 set of 6 repetitions at 75% RM, and 1 set at 90% RM to fatigue performed each training session. During training, subjects consumed 4 servings of either a placebo (Con; 10g glucose) or glutamine (10g) twice daily on training days (2 immediately after workout and 2 before bed). Body composition (as % body fat) was measured before and after supplementation by bioelectrical impedance. Changes in muscular strength and body composition were compared between the groups by repeated measures ANOVA. Significance was set at p ± 0.05.
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RESULTS

RM for all 3 lifts were added together (pre and post training) and averaged in each group. Average total weight lifted significantly increased (P ≤ 0.05) in each group (GL: pre-323.3 kg vs. post-388.0 kg; Con: pre-258.2 kg vs. post-306.9 kg). No significant difference was observed between the GL and Con groups in percent increase of average total weight lifted (16.7% and 15.9% respectively). Body composition also did not differ between the groups (GL: pre-10.7% vs. post-10.1%; Con: pre-11.3% vs. post-10.9%).
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CONCLUSION

Glutamine supplementation does not increase muscle strength or significantly change body composition following resistive training.

©2005The American College of Sports Medicine

GLUTAMINE SUPPLEMENTATION DID NOT BENEFIT ATHLETES DURING SHORT-TERM WEIGHT REDUCTION

Kevin J., Finn and Robin Lund, and Mona, Rosene-Treadwell (2003) GLUTAMINE SUPPLEMENTATION DID NOT BENEFIT ATHLETES DURING SHORT-TERM WEIGHT REDUCTION. Journal of Sports Science and Medicine , 2 .

Abstract

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 4186kJآ·day-1 energy deficit and a 8372 kJآ·day-1 energy deficit on days 1-5, days 6-12, respectively. The glutamine (GLN) group (n=9) ingested 0.35 gآ·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.

J Appl Physiol. 2002 Sep;93(3):813-22.
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.

Sports Med. 2003;33(5):323-45.
Glutamine supplementation in vitro and in vivo, in exercise and in immunodepression.

Castell L.

Nuffield Department of Anaesthetics, University of Oxford, England. lindy.castell@nda.ox.ac.uk

In situations of stress, such as clinical trauma, starvation or prolonged, strenuous exercise, the concentration of glutamine in the blood is decreased, often substantially. In endurance athletes this decrease occurs concomitantly with relatively transient immunodepression. Glutamine is used as a fuel by some cells of the immune system. Provision of glutamine or a glutamine precursor, such as branched chain amino acids, has been seen to have a beneficial effect on gut function, on morbidity and mortality, and on some aspects of immune cell function in clinical studies. It has also been seen to decrease the self-reported incidence of illness in endurance athletes. So far, there is no firm evidence as to precisely which aspect of the immune system is affected by glutamine feeding during the transient immunodepression that occurs after prolonged, strenuous exercise. However, there is increasing evidence that neutrophils may be implicated. Other aspects of glutamine and glutamine supplementation are also addressed.

J Nutr. 2008 Oct;138(10):2045S-2049S.
Dosing and efficacy of glutamine supplementation in human exercise and sport training.

Gleeson M.

School of Sport and Exercise Sciences, Loughborough University, Loughborough LE11 3TU England. m.gleeson@lboro.ac.uk

Some athletes can have high intakes of l-glutamine because of their high energy and protein intakes and also because they consume protein supplements, protein hydrolysates, and free amino acids. Prolonged exercise and periods of heavy training are associated with a decrease in the plasma glutamine concentration and this has been suggested to be a potential cause of the exercise-induced immune impairment and increased susceptibility to infection in athletes. However, several recent glutamine feeding intervention studies indicate that although the plasma glutamine concentration can be kept constant during and after prolonged strenuous exercise, the glutamine supplementation does not prevent the postexercise changes in several aspects of immune function. Although glutamine is essential for lymphocyte proliferation, the plasma glutamine concentration does not fall sufficiently low after exercise to compromise the rate of proliferation. Acute intakes of glutamine of approximately 20-30 g seem to be without ill effect in healthy adult humans and no harm was reported in 1 study in which athletes consumed 28 g glutamine every day for 14 d. Doses of up to 0.65 g/kg body mass of glutamine (in solution or as a suspension) have been reported to be tolerated by patients and did not result in abnormal plasma ammonia levels. However, the suggested reasons for taking glutamine supplements (support for immune system, increased glycogen synthesis, anticatabolic effect) have received little support from well-controlled scientific studies in healthy, well-nourished humans.

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 Metabolism 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.

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.

Facts and fallacies of purported ergogenic amino acid supplements.

Williams MH.

Department of Exercise Science, Physical Education, and Recreation, Old Dominion University, Norfolk, Virginia, USA. mwilliam@odu.edu

Although current research suggests that individuals involved in either high-intensity resistance or endurance exercise may have an increased need for dietary protein, the available research is either equivocal or negative relative to the ergogenic effects of supplementation with individual amino acids. Although some research suggests that the induction of hyperaminoacidemia via intravenous infusion of a balanced amino acid mixture may induce an increased muscle protein synthesis after exercise, no data support the finding that oral supplementation with amino acids, in contrast to dietary protein, as the source of amino acids is more effective. Some well-controlled studies suggest that aspartate salt supplementation may enhance endurance performance, but other studies do not, meriting additional research. Current data, including results for several well-controlled studies, indicated that supplementation with arginine, ornithine, or lysine, either separately or in combination, does not enhance the effect of exercise stimulation on either hGH or various measures of muscular strength or power in experienced weightlifters. Plasma levels of BCAA and tryptophan may play important roles in the cause of central fatigue during exercise, but the effects of BCAA or tryptophan supplementation do not seem to be effective ergogenics for endurance exercise performance, particularly when compared with carbohydrate supplementation, a more natural choice. Although glutamine supplementation may increase plasma glutamine levels, its effect on enhancement of the immune system and prevention of adverse effects of the overtraining syndrome are equivocal. Glycine, a precursor for creatine, does not seem to possess the ergogenic potential of creatine supplementation. Research with metabolic by-products of amino acid metabolism is in its infancy, and current research findings are equivocal relative to ergogenic applications. In general, physically active individuals are advised to obtain necessary amino acids through consumption of natural, high-quality protein foods.

Curr Sports Med Rep. 2007 Jul;6(4):265-8.
Glutamine: the nonessential amino acid for performance enhancement.

Phillips GC.

University of Iowa Children's Hospital, Iowa City, IA 52242, USA. george-phillips@uiowa.edu

Glutamine is a popular dietary supplement consumed for purported ergogenic benefits of increased strength, quicker recovery, decreased frequency of respiratory infections, and prevention of overtraining. From a biochemical standpoint, glutamine does play a physiologic role in each of these areas, but it remains only one of a host of factors involved. This review examines the effects of glutamine on exercise and demonstrates a lack of evidence for definitive positive ergogenic benefits as a result of glutamine supplementation.

J Sports Med Phys Fitness. 1998 Sep;38(3):240-4.
Acute L-glutamine ingestion does not improve maximal effort exercise.

Haub MD, Potteiger JA, Nau KL, Webster MJ, Zebas CJ.

Exercise Physiology Laboratory, University of Kansas, Lawrence 66045, USA.

BACKGROUND: L-glutamine (GLN) may have an ergogenic effect during exercise considering its base generating potential. We attempted to determine whether GLN ingestion influences acid-base balance and improves high intensity exercise performance. METHOD: Ten trained males performed five exercise bouts on a cycle ergometer at 100% of VO2 peak. The first four bouts were 60 sec in duration, while the fifth bout was continued to fatigue. Each bout was separated by 60 sec of recovery. The exercise bouts were initiated 90 min after ingesting 0.03 g.kg body mass-1 of either GLN or placebo (PLC). Venous blood samples were collected pre-ingestion (PRE-IN), pre-exercise (PRE-EX), and following bouts four (B4) and five (B5) and analyzed for pH, bicarbonate concentration (HCO3), and lactate concentration (La-). Time to fatigue for B5 was used as a performance measure. RESULTS: pH, [HCO3], and [La-] were not significantly different (p > 0.05) between conditions for PRE-IN, PRE-EX, B4, and B5. Time to fatigue was not significantly different between conditions and averaged 263.4 +/- 24.5 sec and 263.2 +/- 19.4 sec for the GLN and PLC trials, respectively. CONCLUSIONS: These data indicate that acute ingestion of L-glutamine does not enhance either buffering potential or high intensity exercise performance in trained males.[/B]

Tuossa jotain.

 

[ysikymppinen]

Miten niistä voi olla apua, jos ne kerta EIVÄT TOIMI? Miten ****tussa se on mahdollista. Eihän lääkeaineistakaan normaalitilassa ole suurta hyöytä...

Threadin aloittaja kysyi lihasten kasvatukseen toimivia lisäravinteita - siihen ne eivät toimi lisänä, olettaen riittävä proteiinin saanti.

Tilanne ei muuttunut yhtikäs mihinkää. Se missä olit väärässä, noita tutkimuksia on myös puoltavia, ei vain ja ainoastaan vastaisia

Missä ne sitten ovat? Missä on tutkimus, joka puoltaa glutamiinin ja arginiinin käyttöä, olettaen riittävä proteiinins saanti? Tutkimus joka puoltaa, että muutama gramma arginiinia ja glutamiinia tuo merkittävää ergogeenista apua juuri lisäravinteena?

Ja luulet, että esim jonkun jalkatreenin jälkeen keho on ihan normaalissa tilassa ja voit popsia huoletta kananrintaa?

Tila ei ole kuitenkaan mikään krooninen sairaus jne. jolloin glutamiini ja arginiinitasot laskisivat niin rajusti, että niiden käyttö lisäravinteena olisi ergogeenista.

Vai olisko tässä aikapaljon muuttujia, jotka puoltavat määrättyjen ravinteiden käyttöä?

Mitkä muuttujat?

 

[Mike]

Mitkä muuttujat?

No et kai sä noin tyhmä ole? Ei treenaajan ruokatottumukset tai kehon rasitus ole laisinkaan samalla tasolla mitä peruspertin. Sitä ollaan miinuksella, plussalla, anaboliassa, kataboliassa. Silti kehoa rasitetaan kokoajan kovasti, monta kertaa viikossa. Kyllä siinä alkaa marginaaleilla olemaan merkitystä vuositasolla.

 

[ysikymppinen]

No et kai sä noin tyhmä ole? Ei treenaajan ruokatottumukset tai kehon rasitus ole laisinkaan samalla tasolla mitä peruspertin. Sitä ollaan miinuksella, plussalla, anaboliassa, kataboliassa. Silti kehoa rasitetaan kokoajan kovasti, monta kertaa viikossa. Kyllä siinä alkaa marginaaleilla olemaan merkitystä vuositasolla.

Ja mitä muutama grammaa arginiinia ja glutamiinia auttaa tähän? Siis sen lisäksi, mitä runsas proteiinin saanti ei tekisi.

 

[Thomppa]

Ja mitä muutama grammaa arginiinia ja glutamiinia auttaa tähän? Siis sen lisäksi, mitä runsas proteiinin saanti ei tekisi.

Sulle on tässä sanottu jo niin monta kertaa noi asiat ja aina kysyt perusteluja, mitä sulle on just kerrottu. Lopeta niitten tutkimusten kaivaminen ja käytä omaa järkeäs.

Siis aivan järjetöntä pilkunnussimista. 'Shut up and get it done'

 

[ysikymppinen]

Sulle on tässä sanottu jo niin monta kertaa noi asiat ja aina kysyt perusteluja, mitä sulle on just kerrottu.

Jännää, että tiede ei tue kertomiasi juttuja. Väitätkö, että sinun sanasi menee tieteellisen datan yli?

Ja osaksi varmaan siksi, että et ole vakuuttavasti pystynyt perustelemaan, että jokunen gramma arginiinia tai glutamiinia olisi millään tavalla merkittäväksi avuksi lihasten kasvatuksessa.

 

[Thomppa]

Jännää, että tiede ei tue kertomiasi juttuja. Väitätkö, että sinun sanasi menee tieteellisen datan yli?

Siis nyt oikeesti :D Tossa on edellisellä sivulla kourallinen sitä tiedettä. Taitaa mennä sun kapasiteetin yli lukea tekstiä, joka osoittaa, ettet välttämättä olekkaan 100% oikeassa. Ai ai

 

[ysikymppinen]

Siis nyt oikeesti :D Tossa on edellisellä sivulla kourallinen sitä tiedettä. Taitaa mennä sun kapasiteetin lukea tekstiä, joka osoittaa, ettet välttämättä olekkaan 100% oikeassa. Ai ai

Millä tavalla ne jutut tukevat arginiinin ja glutamiinin käyttämistä lisäravinteena?

Niitä kun saa normaalisti ruoastakin. En ole väittänyt, että arginiini ja glutamiini ovat turhia - olen väittänyt useasti, että lisäravinteena ne ovat. edit. sori jos on unohtunut jostain lauseesta mainita tuo.

Miten ne jutut tukevat hypoteesia, että muutama gramma yksittäisiä aminoja toisi apuja kehonkoostumukseen kun nautitaan vaikka parisataa grammaa proteiinia???

 

[Thomppa]

Millä tavalla ne jutut tukevat arginiinin ja glutamiinin käyttämistä lisäravinteena?

Niitä kun saa normaalisti ruoastakin. En ole väittänyt, että arginiini ja glutamiini ovat turhia - olen väittänyt useasti, että lisäravinteena ne ovat.

Edelleen arginiinia ravinnosta saa kovin vähän. Paras lähde ovat pähkinät n. 3g/100g ja normihera n.2g/100g. Muut tulevat kaukana perässä. Kaikki eivät edes syö pähkinöitä tietyistä syistä yms allergiat. Eikä heraakaan tarvitse kilokaupalla vetää, jolloin mielestäni ravinnosta ei saa tuota 'optimaalisen anabolista' määrää, JOLLOIN ON MIELESTÄNI perusteltua käyttää lisäravinnetta.

e. tosin viisaampaa olisi, jos mahdollista syödä ne normi ruuasta. Taitaa olla ainoa asia mistä ollaan samaa mieltä.