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How Amino Acids Improve Endurance

January 03, 2018 8 min read

How Amino Acids Improve Endurance

It is well known that amino acids are the building blocks of muscle.   They play very specific key roles in health and performance in human physiology and help athletes retain muscle and burn fat.   Proteins are made up of both essential and non-essential amino acids that can be used by the body for a plethora of benefits.   Some of these key benefits beyond muscle building include improved glycogen resynthesis, improved mineral absorption and improved focus during exercise.   The body must break the protein down into these free form amino acids in order for them to function.   Consuming amino acids in their free form is beneficial since these amino acids can address their function almost immediately.

Glutamine

Glutamine is the most abundant amino acid in the body, accounting for greater than 60% of the total intramuscular free amino acid pool. Virtually every cell in the body uses this non-essential amino acid.

BCAAs-Metabolism

image credit: the balancedbeautyblog.

Glutamine is synthesized in both skeletal muscle and in adipose tissue in addition to the lungs, liver and brain. Because the body has the ability to produce glutamine it has long been considered a non-essential amino acid, which simply means the body has a mechanism to produce this powerful amino acid. However, clinical evidence shows that, during times of stress, the body cannot produce enough glutamine to keep up with demand which in turn can reduce performance, immune function and mood. As a result, glutamine has recently been classified as a conditional non-essential amino acid. Glutamine offers a significant benefit to exercising individuals and those looking to increase lean muscle mass and decrease body fat. Supplemental glutamine can help promote cell volumization, the mechanism of drawing of water INSIDE muscle cells which can help increase muscle hydration, increase protein synthesis (the making of proteins), and decrease proteolysis (the breakdown of protein).

Glutamine and overtraining

Intense physical exercise drains glutamine stores faster than the body can replenish them. Glutamine levels in the serum are dramatically reduced following exhaustive exercise.When this occurs, the body breaks down muscles and becomes catabolic.  With reduced glutamine levels, performance and recovery are compromised. There is evidence that supports glutamine supplementation for recovery, glycogen storage, synthesis of other amino acids and reduction of the catabolic effects of over-training.   Glutamine has also been shown to aid in recovery and recuperation in addition to boosting immune function. It accomplishes this as one of the building blocks for the body’s most powerful anti-oxidant, glutathione, and may possibly cause extra growth hormone release with just a 4 gram oral dosage.

A strict and strenuous training program, which does not allow for enough recovery time, may cause an athlete to experience over-training syndrome (OTS). Researchers have effectively correlated OTS to amino acid imbalances. Decreased performance, worsened mood, and increased incidence of infections  characterize these amino acid imbalances caused by OTS.  Athletes who exercise extensively and are suffering from OTS may become immuno-suppressed.  This can lead to increased infection and upper respiratory illness. In addition, recent clinical trials have shown that over-trained endurance athletes suffer from chronic low plasma glutamine levels. Maintaining normal levels of intramuscular glutamine is critical in preventing the breakdown of skeletal muscle and catabolism (the breakdown of muscle). There is also strong evidence that glutamine acts as an immuno-stimulant, which reduces the incidence of infection during training and racing. The best time to take a glutamine or glutamine peptide supplement is right after a hard exercise session since glutamine stores in muscle can be depleted up to 40% after exhaustive exercise.

Branched Chain Amino Acids (BCAAs)

Low levels of branched chain amino acids (BCAAs) may contribute to fatigue or the perception of fatigue through a process called ‘central fatigue’.  BCAA’s include the essential amino acids leucine, isoleucine, and valine. They are very popular among strength athletes yet there is strong evidence validating their use for endurance training and racing.   Numerous research studies have shown these three key amino acids are extremely important to consume, especially during dieting and exercising (and according to one study, BCAAs are even more important when exercising in the heat). During exercise, the body uses a mix of glucose, fats, and even protein as a fuel source. When diet and carbohydrate intake is lower than normal, the percentage of protein the body uses for fuel (specifically Leucine, Isoleucine, and Valine) dramatically increases. The body will pull those needed amino acids from the continuously circulating pool of amino acids in the bloodstream.

If these amino acids not replenished from an outside source, the body will breakdown other areas of the body in order to supply this pool. Studies have shown that subjects who consume an effective dose of BCAAs while endurance training have greater levels of lean muscle mass retention than control subjects who ingest a placebo (and typically lose muscle during the same dieting period). Additionally, BCAAs form antibodies that combat invading bacteria and viruses. The body cannot manufacture its own BCAAs, so they must be supplied through diet and supplementation. BCAAs have also been studied for their ability to improve exercise capacity in heat.  Studies showed that supplementing with BCAAs significantly improved moderate exercise performance in the heat.

BCAAs and Central Fatigue

Branched Chain Amino Acids are also associated with a syndrome termed central fatigue. Following exhaustive exercise, BCAAs are depleted from the working muscle and from the circulating pool of amino acids. This depleted state causes an imbalance of the BCAA to Tryptophan (another amino acid) ratio..

When BCAAs are low, tryptophan (a precursor to serotonin) is more readily available and can cause increases in serotonin. This increase in serotonin causes a feeling of sleepiness and lethargy.  This imbalance causes an athlete to become lethargic and almost sleepy even during exercise.

Using free form BCAAs during exercise will help stop the tryptophan/serotonin mechanism which helps athletes stay focused and have a sense of mental strength and energy.

 

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EFS Contains 2g Glutamine & BCAA’s

 

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EFSPRO Contains 2g Glutamine & BCAA’s

 

 

ultragen_new_flavors-600Ultragen contains 4.5g Glutamine & BCAA’s

  

Glutamine References

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Hiscock N, et. al. Glutamine supplementation further enhances exercise-induced plasma IL-6. J Appl Physiol. 2003 Jul;95(1): 145-8. Epub 2003 Feb 28.

Bassit RA, et. al, Branched-chain amino acid supplementation and the immune response of long-distance athletes. Nutrition. 2002 May;18(5):376-9

Blomstrand E, Saltin B. BCAA intake affects protein metabolism in muscle after but not during exercise in humans. Am J Physiol Endocrinol Metab. 2001 Aug;281(2):E365-74

Halson SL, et al. Immunoligical responses to overreaching in cyclists. Med Sci Sports Exerc. 2003 May;35(5):854-861

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Castell, L.M., et al. The role of glutamine in the immune system and in intestinal function in catabolic states. Amino Acids 7 (1994): 231-243

Castell, L.M., J.R. Poortmans, and E.A. Newsholme. Does glutamine have a role in reducing infection in athletes? European Journal of Applied Physiology 73 (1996): 488-490.

Van Hall, G., Saris, W.H.M., Van De Schoor, P.A., and Watenmakers, A.J.M., 2000. “The effects of free glutamine and peptide ingestion on the rate of muscle glycogen re-synthesis in man.” International Journal of Sports Medicine, 21:25-30.

BCAAs References

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Blomstrand E, Hassmen P, Ek S, Ekblom B, Newsholme EA. Influence of ingesting a solution of branchedchain amino acids on perceived exertion during exercise. Acta Physiol Scand. 1997 Jan;159(1):41-9.

Blomstrand E, Hassmen P, Ekblom B, Newsholme EA. Administration of branched-chain amino acids during sustained exercise–effects on performance and on plasma concentration of some amino acids. Eur J Appl Physiol Occup Physiol. 1991;63(2):83-8.

Castell LM, Yamamoto T, Phoenix J, Newsholme EA. The role of tryptophan in fatigue in different conditions of stress. Adv Exp Med Biol. 1999;467:697-704.

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Davis JM, Bailey SP, Woods JA, Galiano FJ, Hamilton MT, Bartoli WP. Effects of carbohydrate feedings on plasma free tryptophan and branched-chain amino acids during prolonged cycling. Eur J Appl Physiol Occup Physiol. 1992;65(6):513-9.

Davis JM, Welsh RS, De Volve KL, Alderson NA. Effects of branched-chain amino acids and carbohydrate on fatigue during intermittent, high-intensity running. Int J Sports Med. 1999 Jul;20(5):309-14.

Davis JM. Carbohydrates, branched-chain amino acids, and endurance: the central fatigue hypothesis. Int J Sport Nutr. 1995 Jun;5 Suppl:S29-38.

Davis JM. Central and peripheral factors in fatigue. J Sports Sci. 1995 Summer;13 Spec No:S49-53.

Gastmann UA, Lehmann MJ. Overtraining and the BCAA hypothesis. Med Sci Sports Exerc. 1998 Jul;30(7):1173-8.

Hassmen P, Blomstrand E, Ekblom B, Newsholme EA. Branched-chain amino acid supplementation during 30-km competitive run: mood and cognitive performance. Nutrition. 1994 Sep-Oct;10(5):405-10.

Lehmann M, Huonker M, Dimeo F, Heinz N, Gastmann U, Treis N, Steinacker JM, Keul J, Kajewski R, Haussinger D. Serum amino acid concentrations in nine athletes before and after the 1993 Colmar ultra triathlon. Int J Sports Med. 1995 Apr;16(3):155-9.

Lehmann M, Mann H, Gastmann U, Keul J, Vetter D, Steinacker JM, Haussinger D. Unaccustomed highmileage vs intensity training-related changes in performance and serum amino acid levels. Int J Sports Med. 1996 Apr;17(3):187-92.

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Mittleman KD, Ricci MR, Bailey SP. Branched-chain amino acids prolong exercise during heat stress in men and women. Med Sci Sports Exerc. 1998 Jan;30(1):83-91.

Newsholme EA, Blomstrand E. Tryptophan, 5-hydroxytryptamine and a possible explanation for central fatigue. Adv Exp Med Biol. 1995;384:315-20.

Raguso, C.A., Pereira, P., Young, V.R., 1999. “A tracer investigation of obligatory oxidative amino acid losses in healthy young adults.” American Journal of Clinical Nutrition, October, 70(4):474-483.

Schena, F., Guerrini, F., Tregnaghi, P., and Kayser, B., 1992. “Branched-chain amino acid supplementation during trekking at high altitude.” European Journal of Applied Physiology, 65:394-398.

Struder HK, Hollmann W, Platen P, Donike M, Gotzmann A, Weber K. Influence of paroxetine, branchedchain amino acids and tyrosine on neuroendocrine system responses and fatigue in humans. Horm Metab Res. 1998 Apr;30(4):188-94.

Schena, F., Guerrini, F., Tregnaghi, P., and Kayser, B., 1992. “Branched-chain amino acid supplementation during trekking at high altitude.” European Journal of Applied Physiology, 65:394-398.

Tanaka H, West KA, Duncan GE, Bassett DR Jr. Changes in plasma tryptophan/branched chain amino acid ratio in responses to training volume variation. Int J Sports Med. 1997 May;18(4):270-5.

Verger P, Aymard P, Cynobert L, Anton G, Luigi R. Effects of administration of branched-chain amino acids vs. glucose during acute exercise in the rat. Physiol Behav. 1994 Mar;55(3):523-6.

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Yamamoto T, Castell LM, Botella J, Powell H, Hall GM, Young A, Newsholme EA. Changes in the albumin binding of tryptophan during postoperative recovery: a possible link with central fatigue? Brain Res Bull. 1997;43(1):43-6.

Yamamoto T, Newsholme EA. Diminished central fatigue by inhibition of the L-system transporter for the uptake of tryptophan. Brain Res Bull. 2000 May 1;52(1):35-8.

Raguso, C.A., Pereira, P., Young, V.R., 1999. “A tracer investigation of obligatory oxidative amino acid losses in healthy young adults.” American Journal of Clinical Nutrition, October, 70(4):474-483.

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Raguso, C.A., Pereira, P., Young, V.R., 1999. “A tracer investigation of obligatory oxidative amino acid losses in healthy young adults.” American Journal of Clinical Nutrition, October, 70(4):474-483.



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