THE ESSENTIAL AMINO ACIDS

METHIONINE Sources: Methionine is an essential amino acid found in beef, chicken, sh, pork, egg, soybean, cottage cheese, and yogurt. General Information: Methionine, along with cysteine, are amino acids that contain a principal source of sulfur. Methionine is particularly important because it is also a methyl donor, meaning it gives up terminal methyl groups to choline. This is important, since the methyl group or CH3 (carbon-hydrogen) molecule is imperative in many chemical processes in your body, particularly the synthesis of RNA and DNA. Methionine is also an important antioxidant, being particularly effective in combating the free radicals caused by alcohol consumption. Other functions include assisting gall bladder function, detoxifying heavy metals in the body, and even strengthening hair follicles. Deciency: Methionine deciency has been shown to decrease protein synthesis, so consuming enough in your diet is of key importance. By guiding your clients to consume complete protein sources regularly, adequate intake of methionine is normally attained. ! Although possible, deciencies of methionine are very rare. Needs/Benets: While the importance of methionine to support protein synthesis is well documented the bulk of this research has been done with persons contending with severe trauma or burns, which does not support the need for athletes to take supplemental methionine. Addressing your clients overall protein requirements in the nutritional planning stage will ensure ample amounts of this essential amino acid are supplied. Dosage: Methionine supplementation should not be required for clients that follow the nutrition planning guidelines set forth in chapter (xx).

PHENYLALANINE: Sources: Phenylalanine is an essential amino acid that is found in cottage cheese, soybeans, sh, meat, poultry, almonds, pecans, brazil nuts, sesame seeds, chickpeas, and lentils. General Information: There are three forms of phenylalanine: D-phenylalanine, Lphenylalanine, and the man made chemical mixture called DL-phenylalanine. D-phenylalanine is

not an essential amino acid, and its function in human nutrition is not known. This section refers to L-phenylalanine (phenylalanine) the essential amino acid that is the only form of phenylalanine found in dietary protein. Phenylalanine is a unique amino acid because its converted into many other amino acids, which are the precursors for important biochemicals. Phenylalanine is converted into tyrosine, the parent compound for the manufacture of L-dopa, which is further converted into hormones dopamine, norepinephrine, and epinephrine. These hormones, classied as Catecholamines, act as neurotransmitters which are chemical messengers in the body. Catecholamines cause general physiological changes that prepare the body for physical activity (ght-or-ight response), and control a variety of processes, such as heart rate and output, arterial blood pressure, oxygen consumption, blood glucose levels, and fat metabolism (ref). Because it functions to support a multitude of endogenous (originating from within), chemical messengers in the body, Phenylalanine has shown to play a role in appetite suppression, and muscle force production. Phenylalanine can trigger the release of a chemical called cholycystokinin (CCK), which cause feelings of fullness, whereas an increase in catecholamines has been linked to improvements in muscle force. Phenylketonuria A cautionary note for trainers, however, is understanding some people suffer from a genetic condition called phenylketonuria. Those aficted, Phenylketonurics, lack the enzyme phenylalanine hydroxylase, and cant convert this amino acid into tyrosine. What results are dangerously high levels of phenylalanine in the brain, ultimately causing psychotic or schizophrenic behavior. Phenylalanine and aspartic acid form to make aspartame, which is why you see this warning on a product labels containing aspartame: WARNING Phenylketonurics: Contains Phenylalanine

Deciency: Deciencies of this amino acid could increase the chances of developing or amplifying mood disorders, including depression,, Other symptoms of deciencies include bloodshot eyes and cataracts. Needs/Benets: Phenylalanine may support an overall sense of well-being, normalize appetite and support healthy responses to exercise perfomance. L-phenylalanine supplements have been considered as a treatment for depression, but currently no studies provide sound scientic results,. Currently there not double-blind, placebo - controlled studies using phenylalanine for depression, and without such evidence we can't be sure that the supplement is actually effective in this arena.

Dosage: Our work suggest the two primary uses clients looking to take supplemental Phenylalanine have in mind are; 1) appetite suppression and 2) mild depression (the blues). In these instances, reminding your client that Phenylalanine, like other amino acids that are neurotransmitter precursors are more effective when taken at least 30-minutes before meals containing protein. This is so the single amino acids are not competing to to initiate neurotransmitter production with amino acids being broken down from food. For appetite suppression or mild depression; 500-mg per dose, before meals. For increased dosages, clients should be advised to use no more than 500-mg increments.

THREONINE Sources: Threonine is found in meats, eggs, various beans, seeds and nuts. Most grains have little or no threonine. Threonine is generally low in the diets of vegans and vegetarians. Therefore, when counseling clients on these diets it is important to advise them to include; soy protein (concentrated/isolated), peanuts, adzuki beans, black beans, sunower seeds and pumpkin seeds, which are rich sources of Theronine. Lack of threonine in the diet may compromise protein synthesis in the same way as Methionine (see above). General Information: Aside from its requirement for protein synthesis, the physiological roles of this essential amino acid are not well understood. Deciency: Deciencies can result in decreased protein synthesis, primarily in your clients that which to exclude animal proteins in their diet.

Needs/Benets: Although threonine is lacking in most vegetable proteins, there is no need to advise your non-vegetarian clients to take supplemental amounts. Dosage: As directed through dietary protein intake. TRYPTOPHAN Sources: Tryptophan is contained in most protein-based foods and ready-to-drink or powdered protein supplements. Foods that deliver high levels of tryptophan also include; milk, yogurt, cottage cheese, red meat, eggs, sh, poultry, chocolate, oats, dried dates, sesame, chickpeas, sunower seeds, pumpkin seeds, spirulina, bananas, and peanuts. General Information: Tryptophan is an essential amino acid that like phenylalanine above, functions as the biochemical source material that makes several hormones and neurotransmitters the can directly impact your clients well-being. Through an enzyme called tryptophan hydroxylase, our body uses tryptophan to make 5hydroxytryptophan (5-HTP) an intermediate and naturally occurring compound that can then be turned into the critical neurotransmitter serotonin. Subsequently, serotonin can be converted into the neurohormone melatonin through yet another set of enzymatic reactions. Research shows Tryptophan, along with the amino acid tyrosine, play a big role in regulating your energy or excitatory levels. Why? Both amino acids compete to cross your blood-brain barrier rst. If tryptophan crosses rst, youll be relaxed and ready for a nap. If, however, tyrosine wins the race, youll be alert and ready to roll. When tryptophan crosses the blood-brain barrier and enters your brain, Vitamins B3 and B6 convert it to the sleep-energy regulating transmitter serotonin. Whats more, carbohydrates, or more specically, the insulin surge released when carbs are consumed, are necessary to carry tryptophan across the blood-brain barrier. Tryptophan is also partly responsible for manufacturing niacin in your body. Deciency: As with many other amino acids, a deciency in tryptophan can lead to edema, liver damage, and weakness, as well as a loss of muscle and fat. Needs/Benets: Tryptophan can be useful for clients that have trouble winding down to sleep, and possibly food cravings. These features are driven by Tryptophan's ability to boost serotonin levels, which can become depleted through low carbohydrate diets.

Dosage: As a natural relaxant: 1,000-mg per dose. Take on an empty stomach 20-minutes prior to last meal or bedtime. For food cravings: 1,000-mg per dose. Take on an empty stomach 20-minutes prior a meal For increased dosages, clients should be advised to use no more than 500-mg increments. HISTORICAL FACTS Even if you are very young, many trainers have heard about the tryptophan scare. In 1989, where tryptophan products were pulled form the market because they were thought to have caused a rare disease called eosinophilia-myalgia syndrome. The disease was traced to a contaminated batch of tryptophan manufactured in Japan, but the FDA has yet to reverse its decision and allow the sale of tryptophan because of this and other quality issues with its manufacturing.

VALINE Sources: Foods that are high in valine include sh, beef, lamb, poultry, soy our, cottage cheese, brown rice, and various nuts, as do most good protein powders and meal-replacement powders (MRPs). General Information: Valine, an essential amino acid, is also known as a branched-chain amino acid or BCAA, which also include leucine and isoleucine. Theyre called branched-chain amino acids because of the conguration of the molecule: the CH3 (methyl) groups branch out and interlock. Aside from their somewhat unusual molecular conguration, BCAAs play an important role in protein synthesis and/or minimizing protein breakdown. The trouble is, not much is known about valine or how it works. We do know, however, that intense exercise eats up valine. It, along with the other BCAAs, are substrates for two other amino acids, glutamine and alanine. Furthermore, BCAAs are used directly for fuel by muscles, and this task spares other amino acids from being used up during exercise.4 Research on the amount of valine needed is mixed at this point, but based on protein requirements active individuals should be consuming 3 to 5 grams daily and is met following the nutrition planning guidelines set forth in chapter (xx). Needs/Benets: Use of supplemental valine is covered in the section on BCAA's (page here).

Dosage: Valine requirements are met following the nutrition planning guidelines set forth in chapter (xx). ISOLEUCINE Sources: Foods that are high in isoleucine include sh, beef, lamb, poultry, soy our, cottage cheese, and various nuts, as well as most good protein powders and MRPs. General Information: In many ways, isoleucine is similar to valine: Theyre both branchedchain amino acids, and until recently (ADD HERE) neither of them seemed to have any specic therapeutic value. Of course, they both serve as a precursor for glutamine and alanine, and they can be used for fuel by muscle cells, thereby sparing other amino acids from being burned up. We do know this though, all three BCAAs play an important role in protein synthesis and minimize protein breakdown.5 Needs/Benets: Use of supplemental isoleucine is covered in the section on BCAA's (page here). Dosage: Isoleucine requirements are met following the nutrition planning guidelines set forth in chapter (xx). LEUCINE Sources: Leucine is contained in every complete protein such as meat, eggs, protein powders and meal replacement drinks. General Information: Together, leucine and the other two BCAAs make up one-third of muscle protein, and leucine is used up at the highest rate of all three. In fact, theres evidence that even sedentary people require much more leucine than the RDA handbook recommends.19 Like the other BCAAs, leucine is required to ensure high protein synthesis rates and to minimize protein breakdown. Recently, numerous studies have shown leucine is actually the silver bullet that triggers muscle protein synthesis (MPS), and in turn muscle growth. Leucine initiates the metabolic pathway called, mammalian target of rapamycin or mTOR which is primarily responsible for the magnitude and duration of protein synthesis. Leucine's role initiating protein synthesis is a key learning for trainers and coaches who formulate nutrition plans for active individuals. Muscle protein synthesis underwrites everything from rebuilding worn out tissues, to recovering from

injury, to increasing muscle size and maintaining resting metabolic rate through muscle maintenance.

Needs/Benets: An essential amino acid, Leucine plays a key role in human nutrition, and supports the synthesis of muscle protein, which is essential to the body's ongoing need to grow, repair, and maintain its skeletal muscle groups. Dosage: To stimulate muscle protein synthesis, research supports intakes of 2-3 grams of leucine per meal. This can be attained through 20-35 grams of complete protein, including animal sources, and vegetarian friendly, soy protein.

LYSINE Sources: Dietary sources of this essential amino acid include sh, chicken, beef, lamb, and other high quality, whole-protein sources. Many vegetable proteins are lacking in lysine, with notable exceptions being beans, namely; lentil, black, kidney and garbanzo. General Information: Lysine is an essential amino acid that your body uses to make carnitine, an amino acid that plays a role in transporting fatty acids into muscle cells, where they can be used as a source of energy. Lysine is also of interest because it may interfere with viral replication; specically, in herpes infections. During a herpes infection, some researchers suggest taking 1,500mg of lysine (along with gram of Vitamin C). However, be sure to keep arginine intake low, because arginine often causes herpes infections to worsen (ref).

Needs/Benets: Lysine is the limiting, or decient amino acid in the majority of all non-animal sourced proteins. For your vegetarian clients it is important to emphasize meals that include lentil, black, kidney and garbanzo beans. For clients who express cold sores on the mouth, or the virus herpes simplex, supplemental lysine and removing supplemental arginine products in the diet may prove benecial. Dosage: For herpes infections, an extra 1,000 - 1,500mg of lysine a day, taken in divided doses throughout the day with Vitamin C, has shown some promising results.