Researched and Composed by Jacob Wilson
Introduction
Recently,
Paddon-Jones et
al. (2004)
listed the
primary requirements needed to optimize an amino acid supplement.
First the supplement should stimulate a superior anabolic
response when compared to consumption
of a normal meal. Second, the supplement must have a greater protein
efficiency rating, while avoiding any form of interference with the
anabolic response to normal meal ingestion. In this context, the
protein efficiency rating can be defined as the amount of tissue growth
which occurs to a given dose of amino acids or protein mixture (Brody,
1999). Further interference provided by a supplement can come in the
form of hyperinsulemia leading to insulin resistance (Henry et al.,
1996, Iozzo et al., 2001, Yki-Järvinen et al., 1987), an anorexic or
satiation effect which lowers normal caloric intake in a compensatory
fashion (Bohe et al., 2003, Wilson, 2004), or downgrading of a normal
meal’s ability to stimulate muscular protein synthesis (Millward et al.,
1988, Tipton et al., 1999). Through extensive research, the scientists
of Champion Nutrition have developed a rich essential amino acid formula
which meets each of the above criteria, and elicits an anabolic response
unmatched by any other formula in its class. The purpose of this paper
was to provide a literature review of the ingredients contained in the
new Amino Acid Shooter formula. An added emphasis was placed upon
research pertaining to the importance of Essential Amino acids in
protein synthesis.
The Role of Essential
Amino Acids in Protein Synthesis
Lean
tissue is comprised of essential amino acids (EAAs) and non essential
aminoacids (NAAs). There are 20 amino acids in total used to form
proteins. Twelve are known as non essential amino acids and can be
synthesized by the body, while the remaining eight are known as
essential amino acids and must be provided exogenously through diet.
Numerous lines of research suggest that EAAs are the rate limiting
nutrient that must be provided through diet for muscle tissue growth to
occur (Millward et al. 1996; Wolfe & Miller, 1999, Tipton et al.,
1999). In this context, Børsheim et al. (2002) investigated the effect
of the ingestion of 6 grams of EAAs compared to 6 grams of mixed NAAs
and EAAs on protein synthesis post exercise. Comparison of protein
synthesis among conditions found double the rate of protein synthesis in
the EAA condition than the mixed amino acid condition. The authors
concluded that the NAAs were already provided in adequate amounts
endogenously. This finding was also supported by
Volpi and
colleagues (2003) who found that 18 grams of EAAs increased protein
synthesis equally to a mixture of 18 grams of EAAs with additional
ingestion of 22 NAAs.
The Role of
Essential Amino Acids in Hormone Regulation
Research has shown that a combination of the essential amino acids
Histidine, Lysine, Methionine and Phenylalanine may stimulate the
natural release of growth hormone, insulin, and other anabolic hormones
(Kreider, 1993). This ensures maximum benefit for any athlete. Histidine,
for example, plays an important role in protein synthesis, while Lysine
not only contributes to growth hormone release, but also plays a crucial
role in the fast-acting metabolic energy pathway. By supplementing with
Lysine, athletes will find an increase in energy production when they
need it most during an intense workout.
Champion Nutrition’s scientists have also decided to include
L-Phenylalanine into the Amino Shooter. Phenylalanine is a very
versatile amino acid. If needed, it can be converted into epinephrine
and norepinephrine, two important hormones that athletes need to perform
at their best. Research indicates that Phenylalanine can block some of
the effects of serotonin. By doing so, Champion Nutrition’s Amino
Shooter can help the athlete avoid the sensation of being tired during a
workout.
Anabolic Response of
an Essential Amino Acid Mixture in Comparison to a Normal Meal
Paddon-Jones et al. (2004) investigated the ability of a normal mixed
protein meal to stimulate muscle protein synthesis in comparison to a
supplement with a base of 15 grams of EAAs. While the normal meal
contained an equal amount of EAAs as the supplement, its anabolic
response was lower than the EAA supplement. The authors suggested that
the slower digestion rate of the normal meal did not elicit the rapid
rise in extra cellular amino acids as the EAA supplement did. In
support of this suggestion
Bohé and
colleagues (2003) elevated EAA levels and found that protein synthesis
increased linearly up to an 80 % increase in extra cellular EAA levels.
The quicker digestion rate and subsequent increase in EAA extra cellular
concentration elicited by the supplement was therefore postulated to
serve as a higher amplitude trigger for protein synthesis.
The Effect of
Frequency of Protein Feedings on Protein Synthesis
Net muscle tissue
accretion (hypertrophy) over a 24-hour period is determined by periods
of net protein degradation and periods of net protein synthesis (Bohé et
al., 2003). When summed, if protein synthesis is greater than protein
degradation, then muscle tissue accretion will occur. This has led to
the suggestion of high meal frequency (Antonio, 2003). In light of
this, Dangin et al. (2001) compared single feedings of protein to
multiple smaller feedings of protein and found the latter to be superior
in promoting muscle protein synthesis.
The Effect of an Essential Amino
Acid supplement on the Anabolic Response of a Normal Meal
For
performance effects, a diet should contain a proper balance of
carbohydrates, complete proteins, dietary fats, as well as vitamins and
minerals. These nutrients should be provided in an individual’s normal
meals. However, as has been suggested post absorptive states elicit a
state of muscle tissue catabolism. Evidence suggests that
supplementation can act as a buffer, and dampen these post absorptive
states (Paddon-Jones et al., 2004). However, if the supplement is too
rich in caloric content it can also dampen the anabolic response of a
normal meal. For example, chronically high insulin levels from too high
a frequency of particularly carbohydrate based supplements can lead to
down regulation of insulin receptors in peripheral tissue, lower glucose
tolerance and promote insulin resistance (Henry et al., 1996, Iozzo et
al., 2001, Yki-Järvinen et al., 1987). Bohé et al. (2003) found that an
EAA supplement, while raising protein synthesis did not significantly
raise insulin levels, further supporting their use between meals.
Supplementation can also increase satiety, and lower calorie consumption
in normal meals. Lowered caloric consumption can dampen the response of
muscle tissue anabolism to training. As an illustration Singh et al.
(2000) investigated the effect of a multinutrient supplement to elderly
participants in addition to their normal feedings to see if it affected
the amount of calories consumed during those meals. It was found that
the participants lowered the calories they consumed in their normal
feedings as a compensatory mechanism. In contrast
Paddon-Jones and colleagues (2004) found that the addition of an EAA
supplement between meals did not alter the caloric consumption in normal
meals. Taken together, the above evidence suggests that an EAA
supplement can augment protein synthesis in a post absorptive state
without negatively affecting the anabolic response of normal feedings.
The Effect of
Nutrient Timing on Protein Accretion and Lipid Oxidation
Research strongly suggests that there is a temporal aspect of nutrient
ingestion in relation to optimizing protein accretion (Knowlden, 2004).
Therefore in order to optimize the anabolic response of training, an
amino acid supplement should be ingested at key intervals relative to a
given training session (Knowlden, 2004). In this context Tipton et al.
(2001) found that ingestion of an amino acid supplement prior to
training increased muscular protein synthesis six fold, as well as
skeletal muscle blood flow. When compared to only ingesting EAAs after
exercise, it was found that a pre workout ingestion of EAAs had a
greater anabolic response, both during and one hour after exercise.
However, while there is a significant improvement in muscle protein
synthesis following an exercise bout, protein degradation will also be
higher. Further, in a recent review Wolfe (2000) provided great
evidence that amino acid uptake following exercise as well as protein
synthesis are greatly enhanced, suggesting that an amino acid supplement
prior to and following exercise can optimize protein balance in favor of
anabolism.
For athletes interested in muscular hypertrophy, with little increase in
adipose tissue content, the lipid oxidation effects of exercise are of
extreme importance.
In this context
Bouthegourd
et. al. (2002) compared the effects of a glucose solution, whole milk
solution, and a whey protein solution to weight gain and lipolysis
during exercise. It was found that lipolysis was inhibited in the
glucose condition. It was also found that weight gain occurred in all
groups, with the primary weight attributed to fat tissue gain in the
whole milk and glucose conditions, while lean muscle tissue was the
primary cause of weight gain in the whey protein condition. This
suggests that a protein, or amino acid supplement prior to exercise
increases anabolism, while preserving lipid oxidation during exercise.
Branched Chain Amino
Acids Spare Lean Tissue
Champion Nutrition’s Amino Acid Shooter has a rich concentration of the
three branched chain amino acids (BCAAs) leucine, isoleucine, and valine.
BCAAs are essential amino acids, and make up greater than one third of
muscle protein (Harper et al., 1984).
Substrate utilization during exercise is derived from glucose, fatty
acids, as well as amino acids. Evidence suggests that BCAAs are
preferentially oxidized when amino acids serve as substrates, and that
exercise greatly increases this process (Rennie, 1996, Wagenmakers et
al., 1989, Shimomura et al., 1995). BCAA supplementation prior to
exercise can increase fuel substrate availability thereby prolonging
time to exhaustion and enhancing performance (Blomstrand et al, 1991,
Madsen et al., 1996, Mittleman et al., 1998). Further, by encouraging
the oxidation of the exogenous BCAA supply, a sparing effect of lean
tissue will occur (MacLean et al., 1994, Nosaka, 2003). In this context
MacLean et al. (1994) found that the ingestion of BCAAs before exercise
lowered muscle protein degradation, while Nosaka (2003) found that BCAA
supplementation before and after exercise lowered muscular soreness.
Branched Chain Amino
Acids and the Central Fatigue Hypothesis
Champion Nutrition’s Amino Acid shooter excludes the essential amino
acid Tryptophan. Tryptophan is an amino acid which binds to albumen in
the blood. During exercise, free fatty acid concentration increases
(Huffman, 2004). The free fatty acids displace Tryptophan causing
plasma concentrations of the amino acid to rise. Concurrently as BCAAs
are oxidized, the ratio of Tryptophan to BCAAs is increased (Blomstrand
et al, 1991, Madsen et al., 1996, Mittleman et al., 1998). When
Tryptophan crosses the blood brain barrier it is utilized for the
formation of Serotonin, a hormone which contributes to the onset of
fatigue experienced during exercise (Huffman, 2004). This is the basis
for the Central Fatigue Hypothesis. BCAAs are able to compete for
transportation with Tryptophan across the blood brain barrier, therefore
attenuating fatigue. For this reason their supplementation prior to
exercise appears to significantly enhance performance, and delay fatigue
in numerous exercise protocols (Blomstrand et al, 1991, Madsen et al.,
1996, Mittleman et al., 1998).
Additional
Ingredients in the Amino Acid shooter
While an emphasis has been placed on EAAs, the Amino Acid Shooter
formula also includes electrolytes, glucuronolactone, and creatine.
The importance of electrolytes to maintain proper fluid balance has been
documented in several studies to be a critical component to optimizing
performance (Wilson, 2003). Further, investigations on performance
drinks which include glucuronolactone have been shown to enhance
concentration, reaction time, and cognitive performance ( Alford et al.,
2001, Horne et al., 2001, Seidl et al., 2001 ), suggesting that
glucuronolactone may enhance exercise performance. The evidence
supporting the ergogenic effects of creatine are numerous. In fact, in
a recent meta analysis on creatine supplementation Branch (2003)
concluded that Millions of man hours and thousands of researchers over
the past 40 years are all coming to the same conclusions – creatine
supplementation increases lean body mass, decreases body fat and
enhances recovery.
Summary
Essential Amino acids have been shown to be rate limiting nutrients in
muscle protein accretion. Evidence suggests that supplementation
between meals can attenuate post absorptive protein degradation without
impairing the anabolic response of normal feedings. Further, EAA
supplementation prior to and following exercise provides an optimal
environment for the stimulation of protein synthesis. The Amino Acid
Shooters are enriched in BCAAs, and exclude Tryptophan. This
combination can increase performance, decrease central fatigue, spare
lean tissue, and decrease muscular soreness. Finally the inclusion of
creatine, electrolytes, and glucuronolactone further enhance the
applicability of this formula.
References and
Sources Cited
Alford C, Cox H, Wescott R. The effects of red bull energy drink on
human performance and mood. Amino Acids. 2001;21(2):139-50.
Horne JA, Reyner LA. Beneficial effects of an "energy drink" given to
sleepy drivers. Amino Acids. 2001;20(1):83-9.
Seidl R, Peyrl A, Nicham R, Hauser E. A taurine and caffeine-containing
drink stimulates cognitive performance and well-being. Amino Acids.
2000;19(3-4):635-42.
Blomstrand ES, Hassmen P, Eckblom B, and 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 63: 83–88, 1991.
Madsen K, MacLean DA, Kiens B, and Christensen D. Effects of glucose,
glucose plus branched-chain amino acids, or placebo on bike performance
over 100 km. J Appl Physiol 81: 2644–2650, 1996
Harper, A. E.,
Miller, R. H. & Block, K. P. (1984) Branched-chain amino acid
metabolism. Annu. Rev. Nutr. 4: 409–454
Mittleman KD, Ricci MR, and Bailey SP. Branched-chain amino acids
prolong exercise during heat stress in men and women. Med Sci Sports
Exerc 30: 83–91, 1998
Rennie, M.
J. (1996) Influence of exercise on protein and amino acid metabolism.
In: Handbook of Physiology, Sect. 12: Exercise: Regulation and
Integration of Multiple Systems (Rowell, L. B. & Shepherd, J. T., eds.),
chapter 22, pp. 995–1035. American Physiological Society, Bethesda, MD.
Wagenmakers, A.J.M.,
Brookes, J. H., Coakley, J. H., Reilly, T. & Edwards, R.
H. (1989) Exercise-induced activation of the branched-chain2-oxo acid
dehydrogenase in human muscle. Eur. J. Appl. Physiol. 59: 159–167.
Shimomura, Y.,
Fujii, H., Suzuki, M., Murakami, T., Fujitsuka, N. & Nakai,
N. (1995) Branched-chain  -keto
acid dehydrogenase complex in rat skeletal muscle: regulation of the
activity and gene expression by nutrition and physical exercise. J. Nutr.
125: 1762S–1765S
Nosaka,
K. (2003) Muscle soreness and amino acids. Training J. 289: 24–28.
MacLean, D. A.,
Graham, T. E. & Saltin, B. (1994) Branched-chain amino acids augment
ammonia metabolism while attenuating protein breakdown during exercise.
Am. J. Physiol. 267: E1010–E1022
Brody, T. (1999).
Nutritional Biochemistry. (2nd ed.) California
Berkeley: Academic Press.
Paddon-Jones, D.
Melinda Sheffield-Moore, Asle Aarsland, Robert R. Wolfe, and Arny A.
Ferrando. (2005) Exogenous amino acids stimulate human muscle anabolism
without interfering with the response to mixed meal ingestion Am J
Physiol Endocrinol Metab, 288: E761 - E767.
Iozzo, P.,
Thonchai Pratipanawatr, Hanno Pijl, Christoph Vogt, Vineeta Kumar, Ruben
Pipek, Masafumi Matsuda, Lawrence J. Mandarino, Kenneth J. Cusi, and
Ralph A. DeFronzo (2001) Physiological hyperinsulinemia impairs
insulin-stimulated glycogen synthase activity and glycogen synthesis Am
J Physiol Endocrinol Metab,; 280: 712 - 719.
Henry, RR,
Ciaraldi T, Mudaliar S, Abrams L, and Nikoulina SE. Acquired defects of
glycogen synthase in cultured human skeletal muscle cells. Influence of
high glucose and insulin levels. Diabetes 45: 400-407, 1996
Yki-Järvinen, H,
Helve E, and Koivisto VA. Hyperglycemia decreases glucose uptake in type
I diabetes. Diabetes 36: 892-896, 1987
Bohe J, Low A,
Wolfe RR, Rennie MJ. (2003) Human muscle protein synthesis is modulated
by extracellular, not intramuscular amino acid availability: a
dose-response study. 552(Pt 1):315-24.
Wilson, G. (Venom)
(2004) An Investigation of the Satiety Mechanism: A Research
Initiative. The Journal of HYPERplasia Research.
Millward, DJ, and
Rivers JP. (1988) The nutritional role of indispensable amino acids and
the metabolic basis for their requirements. Eur J Clin Nutr 42: 367-393
Tipton, KD,
Ferrando AA, Phillips SM, Doyle D, Jr, and Wolfe RR. (1999) Postexercise
net protein synthesis in human muscle from orally administered amino
acids. Am J Physiol Endocrinol Metab 276: E628-E634
Millward DJ,
Fereday A, Gibson NR & Pacy PJ (1996). Post-prandial protein metabolism.
Baillieres Clin Endocrinol Metab 10, 533-549
Wolfe RR , &
Miller SL (1999). Amino acid availability controls muscle protein
metabolism. Diabetes Nutr Metab 12, 322-328
Tipton, KD, Gurkin
BE, Matin S, and Wolfe RR. Nonessential amino acids are not necessary to
stimulate net muscle protein synthesis in healthy volunteers. J Nutr
Biochem 10: 89-95, 1999
Borsheim E, Tipton
KD, Wolf SE, Wolfe RR. (2002) Essential amino acids and muscle protein
recovery from resistance exercise. Am J Physiol Endocrinol Metab.
283(4):E648-57.
Volpi E,
Sheffield-Moore M, Rasmussen BB, and Wolfe RR. (2001)Basal muscle amino
acid kinetics and protein synthesis in healthy young and older men. JAMA
286: 1206–1212.
Antonio, J. (2003)
Fast and Slow Dietary Proteins Strength and Conditioning Journal:
Vol. 25, No. 6, pp. 70–71.
Dangin M, Boirie
Y, Garcia-Rodenas C, Gachon P, Fauquant J, Callier P, Ballevre O,
Beaufrere B. (2001) The digestion rate of protein is an independent
regulating factor of postprandial protein retention. Am J Physiol
Endocrinol Metab. Feb;280(2):E340-8.
Fiatarone Singh
MA, Bernstein MA, Ryan AD, O'Neill EF, Clements KM, Evans WJ. (2000)
The effect of oral nutritional supplements on habitual dietary quality
and quantity in frail elders. J Nutr Health Aging. 2000;4(1):5-12.
Tipton KD,
Rasmussen BB, Miller SL, Wolf SE, Owens-Stovall SK, Petrini BE, Wolfe
RR. (2001) Timing of amino acid-carbohydrate ingestion alters anabolic
response of muscle to resistance exercise. Am J Physiol Endocrinol
Metab. 281(2):E197-206.
Bouthegourd JC,
Roseau SM, Makarios-Lahham L, Leruyet PM, Tome DG, Even PC. (2002) A
preexercise alpha-lactalbumin-enriched whey protein meal preserves lipid
oxidation and decreases adiposity in rats. Am J Physiol Endocrinol
Metab. Sep;283(3):E565-72.
Huffman DM, Altena
TS, Mawhinney TP, Thomas TR. (2004) Effect of n-3 fatty acids on free
tryptophan and exercise fatigue. Eur J Appl Physiol. 2004
Aug;92(4-5):584-91. Epub 2004 Mar 30.
Knowlden, A. (2003) A Scientific Investigation into the Rationality of
Post Workout Carbohydrate Consumption. The Journal of HYPERplasia
Research
© ABC Bodybuilding Company. All rights reserved.
Disclaimer |
