Every athlete trains to become bigger, faster, and stronger. Everyone looks within themselves to attain a new level of performance and, at times, supplementation is essential. Today, an athlete can research online and discover a multitude of information on different types of nutritional supplements, but there are still basic supplements that are the most important and revered, such as protein, creatine, and a multi-vitamin. Amino acids, especially Branch chain amino acids (BCAA's) are no different.
Amino Acids In General
- Aspartic Acide
- Glutamic Acid
Muscles can not grow without protein and despite their variety; all proteins are composed of just 20 different amino acids. Proteins are macromolecules constructed from long strings of units called amino acids. Amino acids are the building blocks of proteins. Each amino acid has an amino group (NH3) on one end, a carboxyl acid group on the other, and a C-H group in the middle[10.]. Differences in the charge and structure of the amino acids affect the shape and functions of the proteins constructed from them.
The eight that the body cannot produce, which are isoleuceine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine, are called essential amino acids because they must be ingested in food or supplementation. Two more that the body can make are histidine and arginine, which are sometimes considered essential in children because their rapidly growing bodies cannot synthesize them fast enough[7.]
How often have you walked into your local gym for a workout, only to have your attention seized by the products on sale promising rapid weight and muscle gain through amino acid supplementation? Then again, the sheer cost may have put you off the idea-and besides, being well educated in these matters, you think you know that a moderate carbohydrate and high protein intake is what the scientists say is best. Yet, almost all of us know someone who is more muscular and stronger that swear by amino acid supplementation.
Branched-chain amino acids supplements, commonly referred to as BCAA's, are very popular with athletes these days, who are searching for ways to increase lean mass and performance. The branched chain amino acids are Valine, Leucine, and Iso-leucine. One popular idea is that BCAA's can move through the blood to the brain and decrease the production of serotonin in the brain's interior, thereby lowering mental fatigue by reducing the amount of serotonin, which can create a sense of tiredness. A fair amount of scientific research supports this hypothesis[3.].
When you are training to develop a stronger, more powerful body, it is essential to stimulate and fuel your muscles at the cellular level. Branch chain amino acids (BCAA's), valine, leucine, and isoleucine, make up approximately 1/3 of muscle protein.. BCAA's reduce muscle fatigue, speed recovery, decrease the loss of other amino acids from muscle during exercise and help the body absorb protein[6.]. A deficiency in any one of these aminos will cause muscle loss. Unlike other amino acids, BCAA's are metabolized in the muscle and not the liver.
BCAA's are mutually antagonistic in their absorptive qualities, therefore, must be available at the same time to insure maximum absorption into the muscle system[2.]. BCAA's are also rapidly depleted from the muscle when training. Taking BCAA's before and/or during a work out will increase performance and delay fatigue. Taking BCAA's immediately after or with a post work out meal will lower cortisol (destroys muscle) levels and replace BCAA levels in the muscles faster[8.].
What Are The Functions Of BCAA's?
BCAA's act as nitrogen carriers which assist the muscles in synthesizing other aminos needed for anabolic muscle action. In simpler terms, it is a combining of simpler aminos to form a complex whole muscle tissue[1.]. Therefore, BCAA's stimulate production of insulin, the main function of which is to allow circulating blood sugar to be taken up by the muscle cells and used as a source of energy. This insulin production promotes amino acid uptake by the muscle. BCAA's are both anabolic and anti-catabolic because of their ability to significantly increase protein synthesis, facilitate the release of hormones such as growth hormone (GH), IGF-1, and insulin, and help maintain a favorable testosterone to cortisol ratio.
BCAA's are also excellent anti-catabolic because they can help prevent protein breakdown and muscle loss, which is significantly important to those who are pre-contest diets. During these times of low caloric intake, the use of BCAA is strongly recommended because there is a greater risk of muscle loss due to a decrease in the rate of protein synthesis and an increase of proteolysis, which is the hydrolytic breakdown of proteins into simpler, soluble substances such as peptides and amino acids, as occurs during digestion[4.].
Valine is an aliphatic amino acid that is closely related to leucine and isoleucine, both in structure and function. These amino acids are extremely hydrophobic and are almost always found in the interior of proteins. They are also seldom useful in routine biochemical reactions, but are relegated to the duty of determining the three-dimensional structure of proteins due to their hydrophobic nature[11.]. They are also essential amino acids and must be obtained in the diet. Important sources of valine include soy flour, cottage cheese, fish, meats, and vegetables. Valine is incorporated into proteins and enzymes at the molar rate of 6.9 percent when compared to the other amino acids[8.].
Leucine, like its cousin's isoleucine and valine, is a hydrophobic amino acid that is found as a structural element on the interior of proteins and enzymes. There appears to be no other significant metabolic role for these amino acids, but they are essential and because they are not synthesized by mammalian tissues, must be taken in the diet[8.].
Leucine ties glycine for the position of second most common amino acid found in proteins with a concentration of 7.5 percent on a molar basis compared to the other amino acids[3.]. It provides ingredients for the manufacturing of other essential biochemical components in the body, some of which are utilized for the production of energy, stimulants to the upper brain and helping you to be more alert[10.].
Isoleucine is a member of the aliphatic side-chain amino acid family that is composed of extremely hydrophobic biochemical's that are found principally in the interior of proteins and enzymes. Like several other members of this family (valine and leucine), isoleucine is an essential amino acid that is not synthesized by mammalian tissues[8.]. Another feature of this class of amino acids is that they appear to have no other significant biological role than incorporation into proteins and enzymes, where their main purpose is to help dictate the tertiary structure of the macromolecules.
Isoleucine is incorporated into proteins at a molar rate of 4.6 percent when compared to the other amino acids[11.]. It also provides ingredients for the manufacturing of other essential biochemical components in the body, some of which are utilized for the production of energy, stimulants to the upper brain and helping you to be more alert[12.].
In a recent study in the Nutritional Journal of Medicine, muscle breakdown (catabolism) in endurance athletes can be reduced when they supplement their diet with BCAA's. Other studies have also shown that after a strenuous strength-training session, even in well-trained athletes, muscle catabolism is increased for a period of roughly 4-14 hours, after which a phase of muscle-building (anabolism) takes place. If the anabolic phase is greater in scale and duration than the catabolic phase, improvements in muscle strength and size will take place[15.].
So any treatments that could reduce muscle catabolism might prove beneficial. A rapid influx of amino acids into the muscle cells immediately after training will theoretically have this effect by providing an alternative source of amino acids for utilization, thus protecting the precious muscle itself. A rapidly absorbed supplement of amino acids, taken immediately after training, might be extremely beneficial[15.].
A recent study carried out by researchers at Auburn University in the US compared blood levels of amino acids in 10 male subjects (average age 30 years) after each of three possible treatments: eating a mixture of amino acids in their easily absorbed form; eating the same total amount but as whole protein (cottage cheese); and eating a mixture of the two. Each treatment consisted of a similar wide range of amino acids, and totaled about 23g protein, 5g carbohydrate, 2g fat, and also included just 20ml water. Each subject's diet was also standardized prior to treatment[15.].
After just 15 minutes, the first and third treatments (i.e., those including individual amino acids) produced a much higher level of circulating amino acids than the whole protein treatment-although, as in many areas of nutrition, there were wide variations between individual responses. A promising finding was that the problem that had been feared- -of a correspondingly quick disappearance of the amino acids from the circulation via excretion from the body by the kidneys-did not take place. Notably, there was little difference between the amino acid concentrations observed as long as some of the amino acids eaten were immediately available for absorption -i.e., after treatments one and three[15.].
In practical terms, what can these findings mean to the athlete wishing to increase muscle mass and get the most out of the hard work put in during specific strength-training sessions? They could mean that those people who swear by amino acid supplements may have got it half-right. The use of such a supplement immediately after training may be beneficial, ideally in combination with an easily absorbed carbohydrate supplement, which can both supply the muscle cells with an alternative energy source and help raise insulin levels to encourage the transport of these nutrients into the cells.
But the other message is that only a small amount of each of these is considered necessary so long as the major post-training meal is not long delayed. Even if the protein in this meal is more slowly absorbed, the rapidly absorbed supplement should have done its job in raising blood levels quickly[15.].
Suitable amounts of carbohydrate and protein in the post-training supplement are 25g and 10g respectively, and could be prepared yourself as a drink or a mix to be taken as soon as you walk towards the locker rooms. Your normal meal immediately after training should take care of most of your nutritional needs, but getting that edge of instant nutrient supply may be just what you need to reduce muscle catabolism and to boost the training effects. And at a relatively low cost too, if supplements are used in this way. In other words, you get the most benefit from using the supplement at the right time, but without the expense of using them as the manufacturers normally suggest[12,13].
How & When To Take Branch Chains
For optimum results in supplement form, it is desirable to take your branch chains separately from the other amino groupings if for no other reason than the fact that they totally dominate the race for entry into the body systems. In fact, they account for upward to 90% of the total amino acid uptake in the three hour period following a meal.
Keeping in mind that the main component BCAA uptake is elevated blood sugar and insulin "spike"; taking BCAA's with each meal and before and after a workout is ideal. They should also be taken within 30-60 minutes preceding and following an intense workout to assist in muscle regenitive process and create premium anabolic conditions.
Are There Any Side Effects?
They are completely safe. There are no side effects.
Supplementing with BCAA's can result in measurable gains in both strength and muscularity. Taking branch chain amino acid before and during a work out will increase performance and delay fatigue. Since your body can not manufacture BCAA's, they must be supplied through your diet. These amino acids are needed for the maintenance of muscle tissue during physical stress and intense exercise. From the perspective of athletes, BCAA's function as anabolic agents, which allow the body to burn fat and not muscle. Therefore, branch chain amino acids are crucial in your quest for muscle growth.
- Blomstrand et al., Influence of Ingesting a Solution of Branched Chain Amino Acids on Perceived Exertion During Exercise, Clin. Sci.:87, 52, 1994.
- Carli et al., Changes in the Exercise Induced Hormone Response to Branched-Chain Amino Acids, Eur. J. Appl. Physiol.: 64, 272, 1992.
- Goldberg, A., The Regulation and Significance of Amino Acid Metabolism in Skeletal Muscle, Fed. Proc.: 37, 2301, 1978. [
- Goto, Masaru; Miyahara, Ikuko; Hayashi, Hideyuki., Crystal Structures of Branced-Chain Amino Acid Aminotransfease Complexed with Glutamate and Glutarate: True Reaction Intermediate and Double Substrate Recognition of the Enzyme. Biochemistry (American Chemical Society) v. 42 no. 14 (April 8 2003) p. 3725-33.
- Kelley, G., Nutrition: A Review of Selected Nutritional Supplements for Bodybuilders and Strength Athletes, Med. Rev.: 2, 184, 1997.
- McLean et al., Branched-Chain Amino Acids Augment Ammonia Metabolism While Attenuating Protein Breakdown During Exercise, Am. J. Physiol.: 267, E1010, 1994.
- Mero A, Leucine Supplementation and intensive training. Sports Med. 1999:27:(6):347-358
- Mero A, et al. Leucine supplementation and serum amino acids, testosterone, cortisol and growth hormone in male power athletes during training. J.Sports Med Phy Fitness 1997:37(2):137-45
- Mitchell, J., DiLauro, P., Pizza, F. & Cavender, D. (1997). The effect of pre-exercise carbohydrate status on resistance exercise performance. International Journal of Sport Nutrition, 7, 185-196.
- Nellis, Mary M.; Doering, Christopher B.; Kasinski, Andrea. Insulin increases branched-chain a-ketoacid dehydrogenase kinase expression in Clone 9 rat cells. American Journal of Physiology v. 283 no. 4 (October 2002 pt1) p. E853-60.
- Plaitakis et al., Pilot Trial of Branched-Chain Amino Acids in Amyotrophic Lateral Sclerosis, Lancet: i., 1015, 1988.
- Riazi, Roya; Wykes, Linda J.; Ball, Ronaold O. The Total Branched Chain Amino Acid Requirement in Young Healthy Adult Men Determined by Indicator Amino Acid by Use of L-(1-13C) Phenylalanine. The Journal of Nutrition v. 133 no. 5 (May 2003) p. 1383-9.
- Sapir, D., Nitrogen Sparing Induced early in Starvation by BCAA, Metabolism: 26, 301, 1977.
- Van Hall et al., Supplementation with Branched-Chain Amino Acids and Tryptophan and Effect on Performance During Prolonged Exercise, Clin. Sci.: 87, 52, 1994.
- William, Alun. Metabolic Effects of Ingestion of L-Amino Acids and Whole Protein. Journal of Nutritional Medicine, vol. 4, pp. 311-319, 1994).