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Science of Muscle Protein Synthesis - 4 part expose

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Science of Muscle Protein Synthesis - 4 part expose

Post by Canuck Singh on Mon Mar 08, 2010 2:24 am

It's all about Amino Acids
Skeletal muscle actively collaborates and participates in all amino acid exchanges with other tissues throughout the body, both at rest and during exercise.7,9,12,13 The proteins which make up the adult body are in a continuous state of flux, being broken down into free amino acids and reincorporated back into protein (protein turnover). And, amino acids absorbed from the diet are kinetically indistinguishable from those already present in the body’s amino acid pools (muscle).7 This is a vital piece of information as the presence, or more precisely, abundance of certain amino acids dramatically increases muscle protein synthesis and turnover,2,5,7 the prerequisite of net increases in muscle.1,5,7

Effects of Exercise
Major and rapid changes occur in muscle amino acid pools during exercise.13 In skeletal muscle, rates of energy production and therefore flux of energy substrates and intermediates increase more than 80-fold in the few minutes going from rest to exercise.13 The understanding of these mechanisms that produce this massive increase within seconds after the start of exercise is one of the most complex academic challenges of biochemistry this decade.13

AA Kinetics
Recent amino acid kinetic studies involving the impact of heavy weight training exercise demonstrate this point.1,2,3 Specifically, heavy resistance training is the most potent stimuli to produce the precise hormonal and metabolic responses 2,4,5 necessary to effect the changes we all desire, whether you’re male or female. Intense weight training increases amino acid transport and protein synthesis rates (the over riding mechanism that builds muscle) up to 100% for up to 24 hours after a workout.4,5 However, these dramatic increases still do not result in net gains in muscle.1,2,3 The catabolic (muscle breakdown) response induced by resistance training almost counteracts, or equals the increases in protein synthesis rates.1,2,3 Weight training restrains net muscle protein loss over time. However, it needs to interact with other factors such as feeding to promote net increases in muscle.1,2,3

Amino Acid Pool's
There are two distinct amino acid pools or reservoirs within the body. Both are located in skeletal muscle.7,10 The first is the smaller "free" pool, around 1%. The other is the larger bound amino acids in body proteins. 99% 7,10 However, the body views both amino acid stores as one single homogenous entity and any metabolic toll on one directly effects the other.1,7,9,13

The amount of amino acid moving through this free pool each day is many times greater than the actual free pool size.9 The small amounts of amino acids in the free pool appear to be responsible for the metabolic influences of all amino acids in the body.10

Protein Synthesis
The dramatic increases in protein synthesis and amino acid transport to the active site occur regardless of the protein source.1,7,10 The increase in amino acid transport rates witnessed as a result of weight training are provided initially by the free pool.1,9 However, the size of this small free pool is tightly regulated and never altered.1,7,9 Its immediate and constant replenishment is thought to be by continuous degradation of muscle tissue.1,7,10 This tells us that without precise nutritional supplementation during recovery, you are merely robbing one muscle group to pay another1and obviously going nowhere in terms of muscle growth.
Recent invivo investigations of amino acid transport and metabolism in man demonstrates that muscle is far more active than previously recognized, even at rest.13 Human limb amino acid exchange rate studies demonstrate that muscle releases far more glutamine (up to 48% of total amino acid release) and alanine (up to 32%) than their concentrations would indicate.9,13 This means that even before the variable of exercise is introduced, skeletal muscle is in "turbo mode" synthesizing and exporting these critical amino acids to supply all organ demands as fast as it can.

On the other hand, the branch chain amino acids (BCAAs) leucine, isoleucine, and valine escape gut and liver metabolism due to the low aminotransferase activity in these tissues.13 And they are taken up at three times as fast as other amino acids.9,10 BCAAs have a 19% concentration in muscle protein, however, they are released very sparingly by muscle and in much smaller amounts than their muscle concentration would indicate.13 Also, glutamate is taken up ravenously by skeletal muscle despite a >50 fold concentration gradient maintained between muscle and blood (substantial amounts are extracted from blood) 24 hours a day.12
- End of Part 1
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Re: Science of Muscle Protein Synthesis - 4 part expose

Post by Canuck Singh on Mon Mar 08, 2010 2:24 am

Muscle Synergy
Reviews on energy metabolism show that the amino acids in skeletal muscle also play a critical role in the production pathways of every energy system. From aerobic (utilizing oxygen) through to the lactate and phosphate anaerobic (without oxygen) energy systems, metabolism of certain amino acids have a far greater role in maintaining energy levels (ATP) than previously thought.

Only six of the 20 amino acids found in human tissue are metabolized directly in muscle.
    1. leucine,
    2. isoleucine,
    3. valine,
    4. alanine,
    5. aspartate and
    6. glutamate.6,14
There is an emerging acceptance that skeletal muscle is the central, pivotal organ of all inter-organ amino acid transport and exchange,10,11,12,17 especially during any form of exercise. These particular amino acids are metabolized at an enormous rate during, and as a result of exercise.14 However, they are also the major contributors to muscle anabolism and their cellular levels dramatically impact muscle growth.

Recent studies reveal that during repeated bouts of high intensity exercise (like weight training - anaerobic), muscle energy (ATP) is increasingly regenerated via aerobic energy pathways.4 In fact, it appears all energy pathways interact with one another with incredible precision to re-synthesize and maintain ATP levels.4

Another recent view is the unsuspected importance of these six amino acids as intermediates that regenerate the aerobic-TCA energy cycle.14 Therefore, no matter what type of exercise you perform, there is an apparent and constant struggle between muscle and all other organs during delegation of these indispensable, but limited amino acids. The result, however, always favors 1.energy production and then 2. recovery. Muscle anabolism (3) pathways always run a distant third!

The changing concept of the glucose-alanine cycle.

Different amino acids are metabolized at vastly different rates.
• For example, alanine is produced and oxidized at a very high rate due mainly to the alanine aminotransferase reaction in muscle.
This reaction establishes and maintains high concentrations of TCA-aerobic cycle intermediates for at least the first 10-30 minutes of exercise.12 Until recently, this pathway has been greatly under-estimated in terms of energy production.11

This reaction rapidly converts the glutamate carbon into TCA-cycle intermediates resulting in an increase in a-ketogluterate- an essential, rate limiting aerobic cycle intermediate that is increasingly devoured during exercise.15 This alanine aminotransferase reaction accounts for the large efflux of alanine from muscle.12,13 Alanine’s role is thought to be mainly a glucose precursor, (a gluconeogenic amino acid) taken up and utilized by the liver.12,13 However, during exercise, as intensity increases, muscle alanine output is progressively matched and exceeded by splanchic uptake of alanine.2,12 Most important, a recent review14 confirms previous work11,12,15,17 that the alanine aminotransferase reaction has been modified to include branch chain amino acids (BCAAs) as major amino acid donors for the formation of alanine at rest and during exercise and proportion of utilization is correlated to intensity of exercise.15 It is concluded that BCAAs play a pivotal role in formation of alanine in muscle.14

BCAAs - their pivotal role in energy metabolism and muscle growth.

During exercise the transaminiation (donation and transfer of the amino group—NH2) of the three BCAAs occurs via the same enzyme.6,10 Human in vivo studies utilizing [15N]-leucine tracers have shown BCAAs directly supply the nitrogen groups to build and export the large concentrations of alanine and glutamine produced by muscle.6,10,11,12 However, it is the BCAA leucine that appears to have the greatest metabolic significance during exercise. Transaminiation is more than doubled in the transfer of leucine nitrogen to alanine in the alanine aminotransferase reaction. While BCAAs are shown to be integral to maintaining all TCA-cycle intermediates,15 leucine is the only amino acid that can enter and be completely oxidized in the TCA-aerobic cycle via acetyl-CoA- the substrate of the aerobic cycle.15

Increased oxidation of BCAAs during exercise increases flux through the BCAA aminotransferase step and, in leucine’s case, the carbon skeleton is oxidized to three acetyl-CoA molecules and uses a-ketogluterate as an amino group acceptor. Because leucine is an essential amino acid (cannot be synthesized by human tissue) this complete oxidation during exercise puts a net carbon drain on the TCA-aerobic cycle.12 This has been demonstrated in glycogen depleted muscle16 and it is also documented that muscle and plasma BCAA concentrations are lowered as a result of any form of aerobic (30%) or anaerobic/aerobic (8-20%) type work.10

To make matters even more intriguing, recent research shows the greatest decreases in BCAA concentrations occur via anaerobic exercise such as weight training.9 In a double blind, placebo-controlled study, strength training athletes on a daily protein intake of 1.26 gm/kg/day could not prevent highly significant declines in plasma BCAA levels during five weeks of training9 and, more specifically, large decreases (30%) in leucine were observered.9

This presents a real problem because high cellular leucine levels are crucial to building muscle yet leucine's oxidation rate during exercise,5 even at low intensity, is much higher than the other BCAAs.10

Leucine is shown to be one of very few amino acids to stimulate protein synthesis in muscle within the body.7,8 More importantly, leucine's absence greatly retards protein synthesis rates.1 The smaller free amino acid pool within the body is tightly regulated and never altered.3,10 The rate of turnover of individual amino acids in this free pool differs enormously. Most free amino acids have relatively large and stable, free pool half-lives of ~5-10 hours. Leucine is much more metabolically active. It has the shortest half-life of all amino acids in the free pool- a mere 45 minutes!10 It is constantly being oxidized instead of being utilized for protein synthesis!

To support this view, Hagg et al5 used infusion techniques of trace amounts of leucine to consistently show that it is oxidized during exercise as an energy source and because of this its use for protein synthesis decreases. Also, the better conditioned you are the more leucine you oxidise.10 If the majority of your dietary leucine is being oxidized, this leaves little room for protein synthesis.

Leucine
Leucine has been shown by many researchers to be critical to protein synthesis and skeletal muscle turnover.1,6,7,8 For these reasons, several researchers, while examining amino acid kinetics, have suggested that the recommended dietary intake (RDI) for leucine for the general population be increased from 14 to 30 mg/kg of body weight per day to optimize rates of whole body protein synthesis!17 Hood and Terjung6 indicate that a minimum three to four-fold increase in the RDI for leucine should be adopted, (a minimum of 45mg/kg body weight/day) even for sedentary individuals!

Mero10 reviewed all forms of exercise and the impact it has on leucine levels. Generally, in virtually every form of exercise, leucine levels decline while alanine levels increase. The large differences witnessed during intense exercise indicate that the alanine-glucose aerobic cycle is also highly activated in anaerobic (weight training) exercise.11,12 Also, skeletal muscle leucine levels are shown to be precariously low in trained individuals,10 leaving little room for error regarding the immediate physiological impact of exercise training.

Maintaining high leucine levels may significantly impact protein synthesis and ultimately muscle growth.
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Re: Science of Muscle Protein Synthesis - 4 part expose

Post by Canuck Singh on Mon Mar 08, 2010 2:24 am

Glutamine
The only difference between glutamine and glutamate is amino group (NH2) attached to the a-carbon atom in the glutamine molecule. Loss of this group means the molecule becomes glutamate, or glutamic acid in solution (same thing).

While high muscle glutamine concentrations are absolutely vital for muscle growth and preservation, research continues to demonstrate an immense inability of the body to achieve and maintain these high concentrations, especially during intense training programs.1,3,6 Tracer studies in man confirm that glutamine is even more important than alanine as a gluconeogenic precursor and as a vehicle for transport of all protein-derived carbon and nitrogen from muscle for metabolism by all other organs in the body.3

While consistent findings among amino acid metabolism literature are rare, studies predominantly show that during and after exercise there is a large reduction in skeletal muscle and plasma glutamate.1-7 This finding is far more consistent than research performed on glutamine.

Glutamate is central in all amino transferase reactions in muscle. This means the amino groups of all six amino acids metabolized in muscle are interchangeable and are donated in the formation of glutamine.5 In muscle, there is a continuous uptake of glutamate and release of glutamine, with glutamate uptake accounting for about half of all glutamine release.5

Large increases in glutamine plasma levels are witnessed immediately after intense exercise.1,6

Influence of High Intensity Exercise
In skeletal muscle, ammonia production (NH3) is gradual during moderate exercise. However, a completely different situation exists at high intensity exercise.1,6

ATP, adenosine tri phosphate, is not merely broken down to ADP, adenosine di phosphate (the breakage and release of energy of one phosphate bond). ADP is also broken down to AMP, adenosine mono phosphate, and IMP - inosine mono phosphate.5 This last reaction is complete rupturing and breakdown of the adenine nucleotide, an extremely hard molecule to break. This quickly produces massive amounts of ammonia in muscle.6 Muscle has to release this ammonia quickly as even moderate amounts alter muscle pH levels (producing fatigue) and high levels are toxic.1,3,6,7 This glutamate-glutamine exchange cycle is the primary mechanism of ammonia export or scavenging from muscle during high intensity exercise. 1,3,6 The ammonia is carried and removed in the form of glutamine.

High intensity exercise has a severe impact on the immune system and repeated sessions lower plasma glutamate and glutamine levels7. This leads to a negative impact on immune and organ function4. Extreme results are chronic over training syndrome, chronic fatigue syndrome, and muscle loss.7

It appears Glutamine intake of high levels is critical to maintaining high levels of both glutamine and glutamate.
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Re: Science of Muscle Protein Synthesis - 4 part expose

Post by Canuck Singh on Mon Mar 08, 2010 2:25 am

Dynamics of Skeletal Muscle
1. Research now demonstrates skeletal muscle is not some inert reservoir from which the building blocks of protein and enzymes are obtained. Skeletal muscle is dynamic, it is the central organ that actively collaborates and participates in all amino acid transport and exchange with other tissues throughout the body. This occurs via two amino acid "pools" in skeletal muscle, one bound in muscle proteins and the much smaller "free-form" amino acid pool.

However, the body views these two reservoirs as one single homogenous pool as they are constantly interacting. Large amounts of amino acids move through this small pool each day, although the size of this pool never alters. This is because it is the initial supply of amino acids that meet all metabolic demands. The impact of exercise draws enormous amounts of amino acids from this free pool to the active site (exercised muscle). However, as the size of the small free pool is never altered, it’s constant, continuous replenishment occurs via breakdown of the larger pool, muscle! This is the reason muscle is extremely difficult to build and why many do not achieve the results they desire from their training.

2. Major and rapid changes occur in muscle amino acid pools during all exercise. It is now confirmed that muscle occupies a central place in the production of energy (ATP), especially during exercise. Not as a direct fuel competing with fatty acids, blood glucose and muscle glycogen, but as precursors for the synthesis of anaerobic and aerobic energy cycle intermediates.

The aerobic energy cycle is also known by many names. Many texts refer to it as the Krebs cycle, TCA cycle or the Citric Acid Cycle, confusing I know, however they all mean the same thing! While the anaerobic and aerobic pathways represent opposite ends of the energy production spectrum, during exercise constant ATP (energy) regeneration is maintained via interplay of all energy pathways.

The view that all energy systems integrate to regenerate ATP levels no matter what the exercise is revolutionary. Most experts think they can keep use of different energy systems separated nicely when designing training protocols. However, this is not the case. An impact on one energy system has an impact on every other energy pathway, either directly or indirectly via utilization of its precursors - the material needed to power these systems.

3. Because of this tremendous impact, certain amino acids are metabolized in far greater amounts than previously suspected. It has been demonstrated that the branch chain amino acids (leucine, valine and isoluecine), glutamine and glutamate play vital roles as precursors to virtually all energy pathways. These are also the same amino acids that appear to be absolutely critical to muscle growth. Or more precisely, the amount of these particular amino acids retained in muscle appears to determine net muscle loss and gains. Research clearly demonstrates that most forms of exercise utilize these amino acids at such a phenomenal rate, little or nothing is left to affect mechanisms of muscle growth! In fact, there is research that demonstrates without supplementation of the precise materials of muscle growth, training on a regular diet produces muscle loss!10

Putting Science on Your Side.

1. Amino acids absorbed from the diet are kinetically indistinguishable from those already present in the body’s muscle amino acid pools.6
2. The dramatic increases in protein synthesis and amino acid transport in exercised muscle occur regardless of the protein source.2

These two facts are important, they suggest that if the correct building materials (such as amino acids) are present, they will be utilized and incorporated into muscle

Large protein intakes not immediately required for cell anabolism (growth) are predominantly oxidized (burnt), used for other metabolic processes within the body.6 Remember, the size of the small free amino acid pool is tightly controlled and regulated.6,11 However, directly after training a large supply of quickly digested protein (amino acids) are needed to get to the active site to offset the dramatic 100% increases in amino acid transport and protein synthesis rates produced within the first 2 hours after weight training.5

If an external source of amino acids does not get there at precisely the right time, the result is an enormous drain on the small free amino acid pool and a subsequent breakdown of neighboring muscle proteins, all to keep replenishing the free pool and provide amino acids for the tremendously accelerated transport rates.2,3,4,6,11 A number of studies by Boilo and colleagues2,3,4 confirm this.

If an abundance of certain amino acids get to the active site directly after weight training, the result is a dramatic increase in MPS and turnover (the prerequisite mechanisms of building muscle) that produce net gains in muscle.2,3 While these studies utilized amino acid infusions, not oral supplement intake, the facts remain the same. If the correct building material gets there at precisely the right time, dramatic gains are witnessed.3 If they do not, the result is zero net gain in muscle.2 These results have been demonstrated in mammals a long time ago using oral intake of precisely formulated protein peptides (bonded amino acids). 13

It has been recognized for some time that intracellular concentrations of certain amino acids profoundly regulate muscle breakdown and stimulate muscle anabolism.7,12 More precisely, it appears that the amount of particular amino acids retained within the muscle cell actually determines whether growth (anabolism) or breakdown (catabolism) occurs and therefore, how much muscle protein is ultimately built.2,3,4,8,11

Directly after intense or prolonged training, intracellular concentrations of most amino acids are at their lowest and the presence of high concentrations of amino acids outside the cell, in the form of supplementation (hyperaminoacidemia), are shown to dramatically accelerate rates of amino acid transport into the muscle cell.9

Transport Systems
Investigations conclude that the most important amino acids for building muscle actually have their own, exclusive cellular transport systems attached to the muscle cell membrane.14 However, studies with other mammals show that even within physiological (normally occurring) concentrations, muscle amino acid transport systems are not saturated.9,14 There is a lot of "room" for manipulation to stimulate these transporters to accelerate their uptake rates! Simply by increasing substrate (amino acid) availability to the muscle cell at the precise time can stimulate or turbo charge amino acid transport systems to drive amino acids into muscle cells to the upper limits of physiological concentrations.9

Accelerated inward amino acid transport directly stimulates significant increases in protein synthesis.3 The higher physiological concentrations of amino acids inside the cell also dramatically stimulate protein synthesis rates.4,7 Increasing leucine and glutamine content within muscle stimulates protein synthesis profoundly.1,7 These factors combined, trigger dramatic increases in muscle cell volume (water content).7 This is the most potent muscle building mechanism there is!8 Increasing cell volume ensures a positive nitrogen balance and net muscle protein deposition.7,8
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Re: Science of Muscle Protein Synthesis - 4 part expose

Post by Canuck Singh on Mon Mar 08, 2010 2:25 am

References Part 1:
1. Bolio G, Tipton KD, Klein S and Wolfe RR. Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans. Am.J.Physiol. 1995:268, E514-E520
2. Bolio G, Maggi P, Williams PD, Tipton KD, Wolfe RR. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am.J.Physiol. 1997:273:E122-129
3. Bolio G, Flemming YRD, Maggi P, Wolfe RR. Transmembrane transport and intracellular kinetics of amino acids in human skeletal muscle. Am.J.Physiol 1995:268:E75-E84.
4. Chandler RM et al, Dietary Supplements affect the anabolic hormones after weight training exercise. J.Appl.Physiol. 1994;76(2):839-845.
5. Chesley A et al. Changes in human muscle protein synthesis after resistance exercise.J.Appl. Physiol. 1992;73 (4):1383-1388.
6. Evans WJ & Cannon JG. The Metabolic Effects of Exercise-Induced Muscle Damage.Exer.Sport Sci.Rev.1991;19:99-119.
7. Fern EB, Bielinski RN and Shultz Y. Effects of exaggerated amino acid and protein supply in man.Experimentia.1991;47:168-172.
8. Hack.V et al. Cystine levels, cystine flux, and protein catabolism in cancer cachexia, HIV/SIV infection and senescence. FASEB J. 1997;11:84-92.
9. Hood DA & Terjung RL, Amino acid metabolism during exercise and following endurance training. Sports Med. 1990:9 (1):23-35
10. Mero A, Leucine Supplementation and intensive training. Sports Med. 1999:27:(6):347-358
11. Schoenheimer R. The dynamic state of body constituents. Harvard University Press, Cambridge, Massachusetts 1942.
12. Walsh NP, et al. Exercise and immune function: links and possible mechanisms. Sports Med 1998:26(3):177-19
13. Wagenmakers AJM. Muscle amino acid metabolism at rest and during exercise: Role in human physiology and metabolism. Exercise & Sport Science Rev. 1998;26:287-314 619-621. 1996.


[size=85]References Part 2
1. Buse MG, Reid SS, Leucine: a possible regulator of protein turnover in muscle. J.Clin.Invest.1975:56:1250-61
2. Felig P, Warren J, Amino acid metabolism in exercising man. J.Clin. Invest 1971;50:2703
3. Fern EB, Bielinski RN and Shultz Y. Effects of exaggerated amino acid and protein supply in man. Experimentia.1991;47:168-172.
4. Hagg SA, Morse EL, Adibi SA, Effect of exercise on rates of oxidation, turnover and plasma clearance of leucine in human subjects. Am.J.Physiol 1982:242:E-407-10.
5. Greeehaff PL & Timmons JA. Interaction between aerobic and anaerobic metabolism during intense muscle contraction. Exercise & Sport Sci Rev.1998; 26:287-301
6. Hood DA & Terjung RL, Amino acid metabolism during exercise and following endurance training. Sports Med. 1990:9 (1):23-35
7. Sreekumaran Nair K, et al. Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. Am. J.Physiol.263:E928-E934.1992:
8. Tischler ME, Desautels M, Goldberg AL, Does leucine, leucyl-tRNA, or some metabolite of leucine regulates protein synthesis and degradation in skeletal muscle. J.Biol.Chem 1982: 257: 1613-219.
9. 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
10. Mero A, Leucine Supplementation and intensive training. Sports Med. 1999:27:(6):347-358
11. Van Hall G, et al. Mechanisms of activation of muscle branch chain a-keto acid dehydrogenase during exercise in man. J.Physiol.1996;494:899-905
12. Van Hall G, et al Deamination of amino acids as a source for ammonia production in human skeletal muscle during prolonged exercise. J.Physiol.1995;489:251-261
13. Walsh NP, et al. Exercise and immune function: links and possible mechanisms. Sports Med 1998:26(3):177-191
14. Wagenmakers AJM. Muscle amino acid metabolism at rest and during exercise: Role in human physiology and metabolism. Exercise & Sport Science Rev. 1998;26:287-314
15. Wagenmakers AJM and Van Hall G. Branch chain amino acids: nutrition and metabolism in exercise. Biochemistry of exercise IX. Champain, IL. Human Kinetics, 1996:431-443
16. Wagenmakers AJM et al. Carbohydrate supplementation, glycogen depletion and amino acid metabolism during exercise. Am.J.Physiol. 260:E883-E890.
17. Young VR, Bier DM, A kinetic approach to the determination of human amino acid requirements. Nutr Rev 1997:45:289[/size]

[size=85]References: Part 3
1. Robson PJ, Blannin AK, Walsh NP, et al. Effect of exercise intensity and duration on plasma glutamine response following exercise and the time course recovery in physically active men. [abstract] J.Physiol. 1998;506:118P-9P
2. Souba WW. Glutamine: a key substrate for the splanchic bed. Ann.Rev.Nutr. 1991;11:285-308
3. Nurjhan N,Bucci A, Perriello G, et al. Glutamine: a major gluconeogenic precursor and vehicle for interorgan carbon transport in man. J.Clin.Invest. 1995;95:272-7
4. Wagenmakers AJM. Discussion:overtraining, immunosuppression, exercise-induced muscle damage and anti-inflammatory drugs. In: Reilly T, Orme M, Eds. The clinical phamacology of sport and exercise. Amsterdam: Excerpta Medica/Elsevier, 1997:47-57.
5. Wagenmakers AJM. Muscle amino acid metabolism at rest and during exercise: Role in human physiology and metabolism. Exercise & Sport Science Rev. 1998;26:287-314
6. Walsh NP, Blannin AK, Clark AM, et al. The effects of high intensity intermittent exercise on the plasma concentrations of glutamine and organic acids of severe exercise stress. Eur.J.Appl.Physiol.1998;77:4234-8
7. Walsh NP, et al. Exercise and immune function: links and possible mechanisms. Sports Med 1998:26(3):177
[/size]
[size=85]Ok, so now that you read all that, you are probably wondering, where is the shabang, the juicy info to help you pack on kilograms of lean mass. Well, I'm sorry folks, If you didn't put 1 + 1 together already and still need hints, go back and look at the titles of the key sections. You need high amounts of glutamine, alanine, Leucine, BCAAs, EAAs post workout. The protein source with the highest amount of EAA (45%), BCAA (25%), and Leucine (10%), is Whey protein Isolate. You should be consuming at least 100g of this stuff a day, with 50g of it in the 2 hour post workout window.[/size]
[size=85]References Part 4:
1. Anthony JC et al. Leucine supplementation enhances Skeletal muscle recovery in rats following exercise.J.Nutri 1999; 129;1102-06
2. Bolio G, Tipton KD, Klein S and Wolfe RR. Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans. Am.J.Physiol. 1995:268, E514-E520
3. Bolio G, Maggi P, Williams PD, Tipton KD, Wolfe RR. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am.J.Physiol.1997:273:E122-129
4. Bolio G, Flemming YRD, Maggi P, Wolfe RR. Transmembrane transport and intracellular kinetics of amino acids in human skeletal muscle. Am.J.Physiol 1995:268:E75-E84.
5. Chesley A et al. Changes in human muscle protein synthesis after resistance exercise. J.Appl. Physiol. 1992;73 (4):1383-1388.
6. Fern EB, Bielinski RN and Shultz Y. Effects of exaggerated amino acid and protein supply in man. Experimentia.1991;47:168-172.
7. Haussinger D. et al.Cellular hydration state: an important determinant of protein catabolism in health and disease. Lancet;1993;34:1330-1332.
8. Haussinger D. et al. Functional Significance of Cell Volume Regulatory Mechanisms Physiol Rev. 1998 Vol78.#1:247-272. Mero A, Leucine Supplementation and intensive training. Sports Med. 1999:27:(6):347-358
9. Hundal HS, Rennie MJ and Watt PW. Characteristics of acid, basic and neutral amino acid transport in the perfused rat hindlimb. J.Physiol. 1989 (Lond) 391:1-11
10. Kinscherf R.et al. Low plasma glutamine in combination with high glutamate levels indicate risk for loss of body cell mass in healthy individuals: the effect of N-acetyl-cysteine.J.Mol.Med. 1996 vol 74:393-400
11. Mero A, Leucine Supplementation and intensive training. Sports Med. 1999:27:(6):347-358
12. Mortimer GE, Pogo AR, Kudowaki M and West JJ. Multiphasic control of protein degradation by regulatory amino acids: general features and hormone modulation. J.Biol Chem.1992;262;26:E584-596
13. Pollain MG, et al. Effect of whey proteins, their oligopeptide hydrolysates and free amino acid mixtures on growth and nitrogen retention in fed and staved rats. JPEN. 1989:vol13#4:382-386.
14. Rennie MJ. Influence of exercise on protein and amino acid metabolism. Handbook of Physiology,Section 12 Exercise: Regulation and integration of multiple systems. Oxford, UK: University Press.1996:995-1035[/size]
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