Tag Archives: protein

What Protein is Best?


Omega-3 protect kidneys

Bodybuilding lowers temporarily renal function. Omega-3 have the opposite effect on urine protein excretion.

The effect of n–3 long-chain polyunsaturated fatty acid supplementation on urine protein excretion and kidney function:
meta-analysis of clinical trials

Am J Clin Nutr 2009;89:1937–45.

Edgar R Miller III, Stephen P Juraschek, Lawrence J Appel, Madhavi Madala, Cheryl AM Anderson, Joachim Bleys, and

Background: Chronic kidney disease is a major worldwide problem.
Although epidemiologic and experimental studies suggest that
n–3 long-chain polyunsaturated fatty acid (n–3 LCPUFA) supplementation
may prevent or slow the progression of kidney disease,
evidence from clinical trials is inconsistent.
Objective: The objective was to combine evidence from controlled
clinical trials to assess the effect of n–3 LCPUFA supplementation
on the change in urine protein excretion (UPE) and on glomerular
filtration rate (GFR).
Design: We performed a meta-analysis of clinical trials that tested
the effect of n–3 LCPUFA supplementation on UPE, a marker of
kidney damage, and on GFR, a marker of kidney function. A randomeffects
model was used to pool SD effect size (Cohen’s d) across
Results: Seventeen trials with 626 participants were included in the
meta-analysis. Most trials focused on patients with a single
underlying diagnosis: IgA nephropathy (n ¼ 5), diabetes (n ¼ 7),
or lupus nephritis (n ¼ 1). The dose of n–3 LCPUFAs ranged from
0.7 to 5.1 g/d, and the median follow-up was 9 mo. In the pooled
analysis, there was a greater reduction in UPE in the n–3 LCPUFA
group than in the control group: Cohen’s d for all trials was 20.19
(95% CI: 20.34, 20.04; P ¼ 0.01). In a patient with 1 g UPE/d , this
corresponds to a reduction of 190 mg/d. Effects on GFR were
reported in 12 trials. The decline in GFR was slower in the n–3
LCPUFA group than in the control group, but this effect was not
significant (0.11; 95% CI: 20.07, 0.29; P ¼ 0.24).
Conclusions: In our meta-analysis, use of n–3 LCPUFA supplements
reduced UPE but not the decline in GFR. However, small
numbers of participants in trials, different methods of assessing
proteinuria and GFR, and inconsistent data reporting limit the
strength of these conclusions. Large, high-quality trials with clinical
outcomes are warranted.

Source: michaelgundill.com

Protein Myths

Exposing the Myths About Protein
from the Hypertrophy-Specific Nutrition Series by Bryan Haycock, M. Sc.

Myth #1: High protein intakes will not affect muscle protein synthesis.
Fact: Greater availability of amino acids means more protein synthesis within muscle cells.

I will concede that experiments have been performed that indicate that a lab animal can survive on a very limited protein intake assuming that fat and carbohydrate intake is adequate. Simply put, the body begins to reduce that amount of amino acid oxidation in order to spare nitrogen containing compounds. Yet can we really apply this kind of example to adult humans trying to build muscle? I think not.

When the body begins getting stingy with amino acids because of low protein intake, non essential functions, such as skeletal muscle protein synthesis, drop to minimal levels. Other functions within the body such as the immune system, which uses glutamine primarily of muscle origin for fuel, also begins to suffer.9 This cripples the body’s ability to cope with the stress and tissue damage induced by intense training. Researchers even believe that currently recommended protein intakes may actually predispose people to illness because of the limited reserve of amino acids. Here’s what they have to say about current recommendations for protein intake: “…It seems reasonable to conclude that the lowered rate of whole-body and perhaps muscle protein turnover that appears to occur in healthy adult subjects when intakes of indispensable amino acids approximate the current international figures, would probably diminish the individuals capacity to withstand successfully a major stressful stimulus. Again, for those reasons, we view the significant reduction in the rate of body protein turnover in healthy adults, which permits them to more closely approach or even achieve amino acid balance at currently accepted amino acid requirement intakes, as an accommodation. Thus we further conclude that these international requirement intakes are probably not sufficient to maintain a desirable or adapted state.”(Young VR., Marchini JS. Mechanisms and nutritional significance of metabolic responses to altered intakes of protein and amino acids, with reference to nutritional adaptation in humans. Am J Clin Nutr 1990;51:270-89) Emphasis added.

Research clearly shows that by increasing blood levels of amino acids you increase protein synthesis in skeletal muscle. It has also been shown that you can maintain a positive nitrogen balance for extended periods of time and that nitrogen accretion will tend to continue as long as protein intake is high.10 Clearly if you want to maximize your gains in the gym you’ve gotta get more protein than the average Joe.

Myth #2: You can only assimilate 30 grams of protein at one sitting.
Fact: The body has the ability to digest and assimilate much more than 30 grams of protein from a single meal.

Speaking of high intakes of protein, people have been perpetuating the myth that you can only assimilate ~30 grams of protein at a time, making protein meals any greater than a 6 oz. chicken breast a waste. This is anything but true. For example, the digestibility of meat (i.e. beef, poultry, pork and fish) is about 97% efficient. If you eat 25 grams of beef, you will absorb into the blood stream 97% of the protein in that piece of meat. If, on the other hand, you eat a 10 oz steak containing about 60 grams of protein, you will again digest and absorb 97% of the protein. If you could only assimilate 30 grams of protein at a time, why would researchers be using in excess of 40 grams of protein to stimulate muscle growth?1

Critics of high protein intakes may try to point out that increased protein intake only leads to increased protein oxidation. This is true, nevertheless, some researchers speculate that this increase in protein oxidation following high protein intakes may initiate something they call the “anabolic drive”.13 The anabolic drive is characterized by hyperaminoacidemia, an increase in both protein synthesis and breakdown with an overall positive nitrogen balance. In animals, there is a correspondent increase in anabolic hormones such as IGF-1 and GH. Though this response is difficult to identify in humans, an increase in lean tissue accretion does occur with exaggerated protein intakes.14,15

The take home message is that, if you are going to maximize muscle growth you have to minimize muscle loss, and maximize protein synthesis. Research clearly shows this is accomplished with heavy training, adequate calories, and very importantly high protein consumption. This means that meals containing more than 30 grams of protein will be the norm. Not to worry, all that protein will certainly be used effectively by the body.

Myth #3: Protein must be rapidly digested to build muscle.
Fact: Both rapidly and slowly digested proteins offer significant benefits to athletes.

Recent research has brought up the notion of “fast” and “slow” proteins.11 They are designated as such according to the rate at which they raise blood levels of amino acids after they are consumed. Whey protein for example is considered a fast protein and causes a rapid increase in amino acid levels. Casein on the other hand is considered a slow protein.

Both rapid and slow proteins offer benefits to someone trying to build muscle. Research has shown that proteins that enter the blood stream rapidly significantly increase protein synthesis. Proteins that enter the blood stream slowly have a pronounced effect on protein breakdown, significantly inhibiting it even at low quantities.

By using a combination of proteins that exhibit both fast and slow properties one should be able not only to jump-start protein uptake into muscle cells during a grueling workout, but also ensure that protein synthesis is jump started and that protein break down is kept at a minimum during the hours following their workout. Take the fast protein before training, and a slow protein after for maximum anabolic effect.

In summary, it is a mistake to say that a “fast” protein is better than a “slow” protein. Both types of protein should be used in strategic fashion to alter protein metabolism in favor of net protein deposition (i.e. muscle growth).

Myth #4: A protein must have added peptides of specific molecular weights to effectively build muscle.
Fact: The body¹s digestive tract makes its own variable molecular weight peptides from the whole proteins you eat.

As soon as protein hits the stomach it is attacked by powerful stomach acids. This acid, along with an enzyme called pepsin, serves to change or denature the proteins structure preparing it for further digestion in the small intestine. In the small intestine several other enzymes work to break down the protein into various molecular weight peptides and free amino acids. Each enzyme acts on a specific part of the amino acid chain cleaving it in the appropriate place. Whether you¹ve just eaten a steak, scrambled eggs or a glass of whey protein, the end result of digestion is the same, a full spectrum of molecular weight peptides and a moderate amount of free amino acids perfectly suited for absorption into the body.

The small intestine has special transporters which actively pull peptides across the brush border membrane and into intestinal cells. All the various peptide transporters have yet to be clearly identified. As a result of these transporters, peptides can be actively absorbed faster than free amino acids. Within intestinal cells, peptides are further broken down into individual amino acids by enzymes called protease (prote = protein, ase = to split or cleave). It has been shown that a very small percent of digested peptides can enter the blood stream by squeezing between intestinal cells. Even though some peptides make it into the blood stream intact, they are quickly broken down by proteases on the surface of liver and muscle cells. If by some small chance peptides actually make it all the way into these cells, they are rapidly broken down by proteases within the cell.

So you see, all this talk about adding various molecular weight peptides simply means that they predigested an already easily digestible protein. This simply adds to the expense of manufacturing the protein. The added cost, of course, is passed on to the consumer.

Myth #5: Arguments over whose protein scores highest on various methods of protein assessment will make or break your success in the gym.
Fact: As protein intake increases the influence of protein quality decreases. In other words, high quantity can significantly make up for low quality.

The quantity of protein in the diet may in fact add importance to the scoring assessment of a given protein. In fact, if you only eat 35- 45 grams a protein a day you better make sure you chose the highest quality protein you can find. On the other hand, if you eat quantities of protein common among bodybuilders, say 1.6 – 1.8 grams per kilogram, the large amount of amino acids overcome slight differences in scoring. Once you achieve a certain levels of quality in a protein supplement, increasing it further will not significantly change it¹s effectiveness when consumed in quantities sufficient to pack on muscle.

Here is a quick overview of the various methods used to determine protein quality. Keep in mind that tests used to determine protein quality use the lower threshold of protein requirements. This creates a metabolic environment far different from that seen in a well fed bodybuilder or athlete.

Chemical Scoring
The most obvious way to determine the quality of a given protein is to break it down into it’s individual amino acids. This amino acid profile is then compared to a standard profile. Egg protein is the standard that is used in a Chemical Scoring scale for protein quality and has a rating of 100. Take for example a protein that has a limited amount of a specific amino acid. This amount is then com-pared to the amount found in egg protein. If the amount in the test protein is 75% of that found in egg then the test protein gets a rating of 75. From this you would assume that if you could feed a person an amount of this protein that is exactly his requirement, you would see nitrogen excreted in the urine in the amount of 25 percent of the nitrogen fed.

Although it is relatively easy and inexpensive to do a chemical scoring of any protein, it does not always accu-rately predict how well the body can utilize it. So the ad-vantages of chemical scoring in determining the quality of protein are that it is easy and inexpensive. It’s drawback is that it cannot tell you anything about the digestibility of the protein. Chemical scoring also involves a procedure that may destroy certain amino acids and this may lead to inaccurate values. It is also insensitive to substances in a given protein that can adversely effect digestibility. To discover this variable the test would have to utilize living animals.

Biological value (BV)
Biological value (BV) scoring does utilize in vivo testing. To determine the actual amount of a given protein that will be used by the body it is necessary to measure not only urinary, but also fecal losses of nitrogen when that protein is fed to human beings. This method is used inter-nationally.

When measuring the BV of a protein source, two nitrogen studies are done. The first study determines how much nitrogen is lost from the body even when no protein is fed. This amount of nitrogen loss is assumed to be inevitable and that the body will naturally lose it regardless of the amount of nitrogen in the diet. In the second study an amount of the protein is fed that is slightly below what is required. As before, the nitrogen losses are then measured, but this time they are compared to the amount of nitrogen consumed. To determine the actual BV of the protein the re-sults are then derived using this formula:
NPU = (N retained / N intake) x 100

This method often involves animal test subjects and is more frequently used. It’s draw backs are that if a low NPU is obtained, it is impossible to know if it is because of a poor amino acid profile or low digestibility.

Protein efficiency Ratio (PER)
Protein Efficiency Ratio (PER) is the best known procedure for evaluating protein quality and is used in the United States as the basis for regulations regarding food labeling and for the protein RDA. This method involves rats who are fed a measured amount of protein and weighed periodically as they grow. The PER is expressed as: PER = weight gain (g) / protein intake (g)

The benefits of this method are it’s expense and simplicity. It’s drawbacks are that it is time consuming; the amino acid needs of rats are not those of humans; and the amino acid needs of growing animals are not those of adult animals (growing animals and humans need more lysine, for example).

The PER is used to qualify statements about daily pro-tein requirement in the United States. You are assumed to eat protein with a PER that is equal to or better than that of the milk protein casein; if the protein’s PER is lower, you must eat more of it to meet the RDA. Food labels have to take protein quality into consideration, using the PER of casein as a reference point. If a food has a protein quality equal or better than that of casein, the RDA is 45 grams. If the protein quality is less than casein you need 65 grams for the RDA.

You may be wondering if it makes any difference if you eat your protein from a supplement or from food. Remember that by the time it gets absorbed into the blood stream, all your body knows is how much of each amino acid was present in the food you ate. If you have the money, it is certainly convenient to just drink down a high quality protein supplement. Beyond that, it makes no difference in what form you get your protein from as long as its a complete protein and sufficiently digestible.

Protein digestibility-corrected amino acid score (PDCAA)
As outlined above, protein quality can be measured by the quantity of indispensable amino acids they contain. If a protein contains all the amino acids essential for life, it is called a complete protein and is given a high score. Because some proteins are not as efficiently digested there arose a need to not only test for the amino acid composition of proteins but also for digestibility. This type of testing is called protein digestibility-corrected amino acid score (PDCAA). It is now a federally accepted standard for determining protein quality for preschool aged children.

Some foods however, contain anti-nutritional factors. These factors sometimes occur naturally like in some beans, or are a result of heating and/or cooking, and inhibit the ability of the body to digest and thus absorb certain amino acids. Research has shown the PDCAA method of scoring protein often over estimates the quality of foods containing anti-nutritional factors.12

The take home message from all this is that arguments about who¹s protein scored highest on this test or that test are really meaningless to the average well fed athlete.

Certainly exposing these myths about protein leaves advertisers with less fodder to bombard you with. Nevertheless, getting rid of these misconceptions will only benefit you the consumer. Knowing the truth about protein will not only save you money but may also open up new opportunities for muscular gains. Knowledge is the key to effective supplementation with protein or any other supplement. Don¹t let your purchasing decisions be controlled by false claims and misleading pseudo science. A wise man once said, ³…know the truth, and the truth shall set you free.² In this case, the truth will give you the freedom to make educated decisions about protein supplementation and the freedom to discern between marketing hype and honest manufacturers offering quality products.

1. Tipton K., Ferrando A., Phillips S., Doyle, JR D., Wolfe R. Post exercise net protein synthesis in human muscle from orally administered amino acids. Am. J. Physiol. 276: E628-E634, 1999

2. Bennet, W. M., A. A. Connacher, C. M. Scrimgeour, and M. J. Rennie. The effect of amino-acid infusion on leg protein turnover assessed by L-[15N]phenylalanine and L-[1-13C]leucine exchange. Eur. J. Clin. Invest. 20: 37-46, 1989

3. Castellino, P., L. Luzi, D. C. Simonson, M. Haymond, and R. A. DeFronzo. Effect of insulin and plasma amino acid concentrations on leucine metabolism in man. J. Clin. Invest. 80: 1784-1793, 1987

4. Fryburg, D. A., L. A. Jahn, S. A. Hill, D. M. Oliveras, and E. J. Barrett. Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms. J. Clin. Invest. 96: 1722-1729, 1995

5. McNulty, P. H., L. H. Young, and E. J. Barrett. Response of rat heart and skeletal muscle protein in vivo to insulin and amino acid infusion. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E958-E965, 1993

6. Mosoni, L., M. Houlier, P. P. Mirand, G. Bayle, and J. Grizard. Effect of amino acids alone or with insulin on muscle and liver protein synthesis in adult and old rats. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E614-E620, 1993

7. Newman, E., M. J. Heslin, R. F. Wolf, P. T. W. Pisters, and M. F. Brennan. The effect of systemic hyperinsulinemia with concomitant infusion of amino acids on skeletal muscle protein turnover in the human forearm. Metabolism 43: 70-78, 1994

8. Watt, P. W., M. E. Corbett, and M. J. Rennie. Stimulation of protein synthesis in pig skeletal muscle by infusion of amino acids during constant insulin availability. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E453-E460, 1992

9. Newsholme, A.E., Parry-Billings M. Properties of glutamine release from muscle and its importance for the immune system. JPEN. 14 (4) supplement S63-67

10. Oddoye EA., Margen S. Nitrogen balance studies in humans: long-term effect of high nitrogen intake on nitrogen accretion. J Nutr 109 (3): 363-77

11. Boirie Y, Dangin M, Gachon P, Vasson M-P, Maubois J-L, and Beaufrère B. Slow and fast dietary proteins differently modulate postprandial protein accretion (amino acid turnover / postprandial protein anabolism / milk protein / stable isotopes) Proc. Natl. Acad. Sci. USA Vol. 94, pp. 14930-14935, December 1997

12. Sarwar G. The Protein Digestibility-Corrected Amino Acid Score method overestimates quality of proteins containing antinutritional factors and of poorly digestible proteins supplemented with limiting amino acids in rats. J. Nutr. 127: 758-764, 1997

13. Millward, D.J. Metabolic demands for amino acids and the human dietary requirement: Millward and Rivers (1988) revisited. J. Nutr. 128: 2563S-2576S, 1998

14. Fern EB, Bielinski RN, Schutz Y. Effects of exaggerated amino acid and protein supply in man. Experientia 1991 Feb 15;47(2):168-72

15. Dragan, GI., Vasiliu A., Georgescu E. Effect of increased supply of protein on elite weight-lifters. In:Milk Protein T.E. Galesloot and B.J. Tinbergen (Eds.). Wageningen The Netherlands: Pudoc, 1985, pp. 99-103″

Source: hypertrophy-specific.com

Protein Cycling for Maximum Gains

Protein Cycling for Maximum Gains
by Marcus R. Jones, MD

We’d like to take the opportunity to introduce one of the notorious “Gang of Five.” His name is Dr. Marcus R. Jones and he’s a practicing physician in Virginia Beach, Virginia. Marcus is not only a doctor with extensive clinical interests in endocrinology, he’s also former nationally-qualified bodybuilder. And, if he doesn’t mind us saying so, he’s the resident mad scientist of the group. Don’t get us wrong, he doesn’t give questionable advice. Hardly. Instead, he introduces theories that definitely go against the grain of conventional bodybuilding thinking. As radical as some sound, they definitely work. This is his first article for Testosterone. Let us know what you think.

What if I told you that bodybuilders eat too much protein? What if I told you that the key to perpetual growth, without plateaus, was within your reach and all you had to do was to cut down on your protein intake? Would you petition the AMA to revoke my license to practice medicine, or would you hear me out? Hopefully, it’s the latter and not the former.

With that in mind, let me dive right into my seemingly preposterous concept.

Protein metabolism is complex and a truly complete overview is beyond the scope of this article but I’ll deliver some relevant highlights so that you’ll have a general idea of why cycling protein intake is so rife with possibility.

Protein has many physiologic roles. The most important to us, as bodybuilders, is that protein is the substrate for the synthesis of muscle. It’s also important for muscle hypertrophy and remodeling. These mechanisms, again, do not warrant discussion in detail at this juncture (it would take too long, and it would undoubtedly put you to sleep). Protein also serves as a precursor for gluconeogenesis (carbohydrate creation) and ketogenesis (fat and ketone creation). You knew that already, of course, because many of us obtain a large portion of our energy needs from protein?but this is not necessarily a beneficial or intelligent thing to do?and we’ll discuss that in greater detail in a minute.

Protein has a plethora of other roles, too. It’s an important player in the modulation of immunity as well as being a precursor for plasma protein synthesis (SHBG, THBG, etc.). And, protein also is the substrate for the synthesis of many cell components as well as being the precursor for peptide hormone synthesis, among other things.

Whew! Now let’s talk more about the down side of protein consumption and metabolism. There are several toxic metabolites of protein that damage multiple organ systems. This includes damage and functional compromise of the central nervous system (brain), circulatory system, as well as renal functions. The most important and well-understood toxins are ammonia, homocysteine, and uric acid. Ammonia is a product, formed in large quantities, during amino acid deamination (the process, which modifies aminos to become substrates for carb and fat synthesis?referred to earlier) and is very, very toxic?especially to the brain. Ammonia is the reason people with liver failure get encephalopathic (brain damaged) and is an etiologic factor in their deaths.1

Normally, the liver converts ammonia to urea but this conversion subjects the liver to a great deal of stress under many circumstances and can cause liver hypertrophy. The liver may also commonly be subclinically overwhelmed such that there are no overt symptoms of encephalopathy, just slow brain damage?but we bodybuilders are supposed to be dumb anyway, right? Yeah, maybe in more ways than one. Needless to say there are many, many more sequelae of ammonia but you get the idea.

Another toxic metabolite of protein is homocysteine. This metabolite is a free radical of sorts and is notorious for scarring blood vessels and thus predisposing us all to atherosclerotic plaque formation.2 Just think, we all thought it was only the fat and cholesterol responsible for our early heart attacks and strokes! One thing I’ve learned is that science and medicine will always throw you a curve ball when you least expect it.

Although there are many other protein-derived toxins, the last one I’ll discuss is uric acid. This chemical is the culprit in gout (you know?the “swollen, red big toe” disease). Anyway, uric acid can also get deposited in the kidneys as crystals, which cause poor function, damage, and occasionally, in those predisposed, kidney stones. We won’t even begin to discuss the link between excessive protein and cancer because it would take up too much space…3

By now, you must be saying” What the HELL is this guy’s problem?there is no way I’m giving up MY protein!” Well I don’t want you to give it up?for too long. And, even though I think giving up protein for awhile would be a good idea, health-wise, it could also have some really, really, dramatic effects on your overall physique.

Haven’t you ever wondered why so many guys claim that a protein intake of greater than 400 grams/day is the only key to growth? Well, the reason is that they aren’t all that smart. You see, most of us take in so much protein that our bodies have gone into a constant state of panic! I just illustrated how physiologically stressful a huge protein load can be. The body has had to up-regulate every protein destroying and detoxifying enzyme it can synthesize to keep from getting poisoned?literally. In the face of a chronically high protein load, the body also becomes entirely too efficient at disposing of and shunting protein as waste rather than utilizing it for anabolism.

One of the shunting pathways of protein just happens to be muscle synthesis but overloading your system with protein has to be one of the most archaic and unintelligent ways to achieve growth ever used. The key to intelligent protein use is forcing the body to become efficient at protein storage (muscle is the prime storage depot) rather than protein shunting and disposal (muscle is a secondary shunting destination). This is easily done with a little manipulation? which is the whole point of this article.

First of all, before proceeding, I must say that I’m at a definite advantage with respect to understanding and applying anabolic theory for at least three reasons:

• I’m one sharp cookie (and modest too).

• I’ve authored and published legitimate scientific research and thus have learned how to objectively investigate a hypothesis.

• Most importantly, I am a legitimate bodybuilder, and I have a physique that many readers are still trying to achieve (approximately 230 lean, muscular pounds at a height of 5’10” while working 110 hours/week).

Now that I’m finished blowing my own horn, let’s cut to the chase. Natural and assisted (a euphemism for “juiced to the hilt”) bodybuilders will benefit immensely from cycling protein because of all the physiologic adaptations that can be achieved by “tricking” the body in the manner I am about to outline. Protein cycling, by my definition, is the use of periods of low protein intake to cause the body to become extraordinarily efficient at storage, as well as tricking it to become very sensitive to protein’s anabolic effects. If the body is chronically overloaded with protein it begins down-regulating protein storage enzymes secondary to anticipating excess protein. The body also initiates other adaptive changes including decreased absorption and increased excretion of protein (definitely counterproductive).

The body can be fooled into thinking that it is becoming protein deficient during periods of low protein consumption even in the face of normal caloric intake. Of course, when this idea is taken to an extreme it results in a condition of malnutrition called KWASHIORKOR.

You’re probably thinking that none of this sounds too great so far. Well, here’s one major benefit that will get your attention. During these periods of decreased protein consumption the body’s growth hormone production can increase to TEN TIMES THE NORMAL LEVEL! That’s not a misprint. Ten times the normal level of GH! Do I have your attention yet? This level remains elevated for greater than a month after the readdition of protein to the diet. In some cases GH can remain at levels 100% above normal levels twenty-five days after increasing protein consumption.4

This is only one beneficial physiologic adaptation. There are other adaptations that occur during protein restriction that result in explosive growth during the high protein phase of protein cycling. One such adaptation to the low protein phase is decreased production of protein degrading enzymes and gluconeogenic enzymes. This decrease in enzyme production occurs along with an increase in protein storing enzymes.

Think about this concept for a second. You can create an environment in which there is increased circulating GH, decreased protein degrading enzyme production, decreased enzymes for protein conversion to energy, and a huge increase in protein storage enzymes (where muscle is the prime storage depot). Are your eyes getting wide yet? Well, there’s even more but it requires a little more explanation…

Gaining muscle through massive consumption of protein is a “live by the sword, die by the sword” kind of concept. Let me explain. The body, in an attempt to dispose of excess protein, will shift metabolic gears, so to speak, and preferentially use protein via gluconeogenesis and ketogenesis for energy. This may sound tolerable (even though we just discussed the associated toxicity) but what happens if, God forbid, you miss a meal or two? Guess what?all those enzymes sitting around chewing up all that excess protein for energy are still there, turned on full blast, using muscle for fuel at nearly the same rate that you were consuming your protein. Your gains will soon disappear via the adage “easy come, easy go.”

Most of us have experienced this, especially when dieting (Hey, didn’t I just see some lights come on?) but couldn’t figure out what happened. Protein cycling eliminates that trap completely! What happens is that cycling protein minimizes the mechanisms for protein degradation during the low protein phase such that by the time the body begins to gear them back up again during the high protein phase (4-6 weeks later), you’ll have already made enormous gains.

Then, you can start dropping your protein again, thus avoiding the cascade of catabolism FOREVER. You see, the reason I’m able to say “forever” is that each time you complete a cycle of protein manipulation you create a new “MUSCLE SETPOINT,” so to speak, and become immune to the catabolic sequelae of a diet chronically high in protein.

Other benefits of protein cycling include more efficient function of the liver and kidneys and a decrease in organ size. We all know that a smaller liver is great, especially to those of us with protruding guts secondary to liver hypertrophy.5 A diet with excessive protein is one of the major culprits in hepatic hypertrophy (along with exogenous GH and oral anabolic agents, etc.). The biggest benefit is the continual and exceptional gains that can be achieved while using a lot less protein (and spending a lot less money, too). Let’s recap the benefits of cycling protein:

• HUGE increases in natural GH production?up to ten times normal
• Extraordinary decreases in protein degradation
• Exceptional reductions in protein waste and use for energy
• Massive increases in protein storage as muscle
• Improved liver function?probably translating into increased IGF-1 elaboration and GH sensitivity
• Decreased liver size (with decreased gut protrusion likely)
• A new “MUSCLE SETPOINT” more resistant to catabolism
• Perpetual growth without plateaus

If you’re smart, you’re now drooling to hear the exact program. Well, here we go. It’s simple! First, protein is gradually decreased by 50% each week. As the protein is decreased, the calories are replaced by carbohydrate, but not completely. Only one half to two-thirds of the protein calories should be replaced (metabolically, protein and carbohydrate do not provide the same amount of energy, and this concept could take an entire article so just trust me on this point).

The protein should be decreased each week until protein intake is only 40 grams per day (even though I suspect 20 grams per day may cause a more beneficial metabolic compensation). Keep the 40-gram/day protein intake for one month. During the low protein period of the cycle, increasing repetitions can cause an increase in glycogen storage enzymes in muscle. This increase in repetitions (50% more than usual) is not necessary, but why waste the opportunity to teach the muscles to overfill?

Hey, don’t be afraid of losing muscle and wimp out…many of our current ideas about building muscle are stupid and based on the ideas of peons and pencil necks. For instance, I have discovered, in the literature and through self-experimentation, that muscle can be built during complete starvation…but that’s another topic for another day.6 Anyway, after 4 weeks of 20-40 gm of protein per day it will be time to shock the body into growth explosion! Protein should suddenly be increased to 1 gram per pound body weight divided into four to six meals daily. See? Nothing too radical or complex there, either.

Hopefully, you’ll have cash for some new clothes because I guarantee a growth spurt unlike any you’ve ever experienced. The high protein phase is the period that you’ll realize that I have taught you how to use protein like a drug rather than just food. When I first tried this cycle out after theorizing it, my attending physician (boss/evaluator/employer) ran a prescription check just to see if I had indulged in a little anabolic script writing…no joke. I actually made drug-like gains without drugs. If you do happen to be “juiced to the hilt”, you might be doing the Nationals this year after adding this regimen to your stack…I’m not kidding. Oh well, you get the point.

Continue the high protein phase for four to eight weeks, depending on when you begin to plateau (usually around week 8). Do not increase protein to overcome your plateau phase, it defeats the purpose of changing your metabolism. Cycle your protein down again and start over. The difference this time will be that you will continue to gain…trust me. I promise you eternal gains with less physiologic damage and more cash in the pocket…think about it, no one has anything to gain in any way with this program but you! Let’s recap:

• Decrease protein by 50% per week until a goal of 20-40 gm of protein per day is reached.
• Replace only 1/2 to 2/3 protein calories with carb calories unless weight loss is noted.
• Remain at 20-40 gm or protein per day for four weeks.
• Increase protein to one gram per pound body weight per day immediately after four weeks of low protein intake.
• Continue this for four to eight weeks and then start over.

Here are a few pointers that I have found to be helpful through trial and error as well as solid research:

1) Consume your protein immediately after training to minimize muscle loss during the low protein phase.

2) Increase carbs during low protein phase if weight loss is noted to persist for more than four days.


4) Skip the vitamin B supplements during the low protein phase?many B vitamins increase protein use for fuel which could crush you during this phase.

5) DON’T PANIC IF YOU SMOOTH OUT A LITTLE during the low protein phase?the edema resolves after two weeks or so.

The beauty of this program is that it appears basic but is grounded in an enormous base of research. Do me a favor and photograph your results. Don’t forget, if you think I’m full of it, then write or call about seeing my pics…I’d be glad to prove I’m all that I claim to be. Train hard.



1) Hyperammoniaemia. Batshaw-ML. Curr-Probl-Pediatr. 1984 Nov; 14(11): 1-69
2) Homocysteine and coronary atherosclerosis. Mayer-EL. J-Am-Card. 1996 Mar 1; 27(3): 517-27
3) Diet and nutritional factors in…CA. Sain-MS. Anticancer-Res. 1987 May-Jun; 7(3): 293-300
4) Guyton text of Physiology.
5) Differential effects…on visceral organs…in lambs. Wester-TJ. J-Anim-Sci. 1995 Jun; 73(6): 1674-88
6) Effect of food restriction on rat muscle hypertrophy… Brown-CR. Comp-Bioch- Physiol-A. 1990; 95(3): 321-4
7) Role of alpha-1 and alpha-2 adrenergic receptors in GH and prolactin response…in man. Tatar-P. Neuroendocrinology. 1984 Sep; 39(3): 275-80

PUBLISHED 07-17-98 00:00

Source: tmuscle.com

Complementary article: Protein Cycling Revisited -by Marcus R. Jones, MD

The Top 10 Post Workout Nutrition Myths

The Top 10 Post Workout Nutrition Myths
by David Barr

The Revolution has come, are you ready?

The world of strength training is obviously full of contradiction and confusion. Just pick up any standard bodybuilding magazine and you’ll see different people with drastically diverse views, all telling you that they have the one method to help you achieve your goals. But through all of this crap, every now and then we find certain principles that we can take to the grave and apply universally.

Examples include: “lift heavy weights and you’ll get big,” “cardio helps with weight loss,” and “Canadian men are hung like moose.”

Another such principle is the post workout nutrient window, which states that during the time immediately post workout, our bodies are in a state of shock and physical disarray, resulting in an opportunity for enhanced nutrient absorption and accelerated recovery. In fact, it’s pretty safe to say that since its inception a decade ago, this scientifically “proven” idea has revolutionized the way we look at nutrition.

Unfortunately, this principle has become so engrained in our subculture that much of it has mutated and become dogmatic in scope. While the general principles remain, many of the studies on which they are based were done on populations that aren’t completely applicable to us, such as animals or endurance athletes.

Despite the emergence of new, more applicable science, we’ve had a very difficult time in adapting our thinking to these current and better-suited ideas.

Making the situation worse is the fact that everyone seems to have their own input about what post workout nutrition should be! This stems from what I like to call the “telephone-chain effect” (derived from the lesson-yielding children’s game), which illustrates how easily messages can change when passed through a chain of people.

How it works is that one person will dictate something to another, who in turn tells this same information to someone else, who then repeats it to another, and so on. By human nature, each person will subtly alter the message, by leaving out some parts, embellishing others, etc. to the extent that by the time you get to the tenth person, the original statement of “Hey sugar, could you mop up the mess in the pantry with the Swiffer?” becomes warped to something like “Shugart is a messed up panty sniffer.”

True as it may be, obviously the point of the latter statement does not even remotely resemble the original.

But since this article is not entitled “The Top Ten Things Wrong With Our Post Workout Information,” let’s get to the myths that have developed, and the current reality.

1. Replenishing Glycogen Needs to be a Focus of PWO.

I’m not just suggesting that glycogen resynthesis is not important following exercise, I’m flat out saying that for strength training it’s not even a concern! This is because it’s just really easy to get our glycogen levels back up, and timing is generally not an issue.

Although one study showed that following endurance exercise, glycogen levels were replenished more rapidly when carbohydrates were consumed shortly after the exercise (Ivy, 1988), this is really of little concern to most of us. Unless we’re subscribers to Runners World, athletes in competition, or doing 2 a day workouts, why do we care so much about rapid glycogen restoration? After all, we’re mostly concerned with muscle growth, fat loss, and getting stronger.

The most common argument is that the subsequent cellular hydration and swelling will have an anticatabolic effect on muscle. I don’t believe that this is possible because cellular hydration to the extent that we get with creatine supplementation has little effect on muscle protein synthesis or breakdown in healthy men or women (Louis et al., 2003).

Then there’s the suggestion that if we don’t replenish post exercise glycogen right away, we’ll miss a window of opportunity to do so. This is largely hyperbole, exploded from bits and pieces of endurance training studies, and a perfect example of the telephone game effect.

Surprisingly, one study showed that consuming carbohydrates after strength training only increased muscle glycogen by 16% more than when water was consumed (Pascoe et al., 1993)! With this information and the huge amount of carbs that we consume on a daily basis, we should have little doubt that glycogen levels will be maximized within 24 hours of the workout.

Now these may be irrelevant points, because in the effort of keeping our focus where it ought to lie—on maximizing protein synthesis— we’re going to quickly stimulate our glycogen restoration anyway. This is because we consume rapidly absorbed carbohydrates along with our protein and amino acids, which has been shown to enhance muscle protein anabolism (Rasmussen et al., 2000).

In other words, muscle glycogen will be restored whether we make it a priority or not. This way, even those who can’t escape the dogma of having to rapidly restore glycogen get their fix, while at the same time, unknowingly assisting with muscle protein recovery.

2. Pre workout Nutrition will divert blood flow away from muscles during exercise.

One of a plethora of excuses made in an attempt to resist preworkout nutrition; this myth actually makes a lot of sense…until you become familiar with the physiology of hormones. Looking deeper, we can find that the insulin stimulated by food intake, actually enhances blood flow and subsequent nutrient delivery to muscles (Coggins et al., 2001).

Applying this principle, liquid pre workout meal consumption dramatically increases muscle blood flow and protein synthesis (Tipton et al., 2001). This elevation in muscle growth is at least twice that observed with the same drink taken post workout (Tipton et al., 2001)! In fact, this effect even lasts for an hour after the workout, so it’s like having 2 drinks for the price of 1! If you want more detail on this topic check out the article on Arginine blood flow stimulators.

Fortunately, early resistance to this research is falling by the wayside, and people are finally starting to reap the benefits that this practice has to offer. While “pre workout nutrition” just doesn’t sound as sexy as “post workout nutrition,” actually doubling our muscle growth should seem pretty damn sexy to everyone!

3. The post workout meal is the most important meal of the day.

I have to admit that with all the hype on post-workout meals over the past few years, I got tangled up in this myth, too. Realistically though, as great as they are, a single post-workout meal will have minimal impact compared to what can happen if your nutrition is completely optimized. Of course it’s heresy to say that these days, but that’s a result of the myth building on itself more than any factual data. For example, as discussed in the myth #2, pre-workout meals can be 200% more effective for stimulating muscle growth compared to post-workout (Tipton et al., 2001).

Perhaps even more important than the pre-workout meal is the old standard: breakfast. No this article isn’t part of a conspiracy by MABB (Mom’s Against Bad Breakfasts) to promote the importance of this meal. Just think about it: being essentially fasted for 8-10 hours is incredibly destructive for muscle -yes even if you eat cottage cheese before bed.

This is especially true in trained individuals like us, because we have higher rates of muscle breakdown (Phillips et al. 2002) The faster we can stop this catabolism once we wake up, the better. In fact, one could even argue that the amount of muscle protein spared from this first meal would be equal to, or even greater, than that gained by a post workout meal.

Also, consuming a high quality slow protein before bed, like Low-Carb Grow! with micellar casein, will largely mitigate the catabolic effect induced by nocturnal fasting. Taking this one step further, nighttime eating will actually put your muscle into anabolic overdrive, by supplying even more amino acids to stimulate this metabolic process.

Finally, a second post workout meal can be even better for protein synthesis than the first, but I’ll get to that one in a bit.

Mini-Summary: Nocturnal feedings, breakfast, preworkout meals, and multiple post workout meals can be more beneficial for muscle growth than a single post workout meal.

4. There’s a one-hour window of opportunity for protein synthesis following a workout.

You may be wondering: is this a myth because the real window is half an hour? Two or 3 hours? Maybe 6 hours? Sadly, in the past 2 weeks I’ve read different articles, all suggesting that the “window” is one of the above lengths of time.

It’s not surprising that with this type of inconsistency that this is probably the most pervasive myth in bodybuilding today! Worse yet, it stems directly from the scientific research itself. The most often cited research on the protein synthetic post workout window, used elderly subjects (Esmark et al., 2001) and cardio exercise findings (Levenhagen et al., 2001) to make their predictions. While this is a completely acceptable practice when these are the only data we have to go on, there are a couple noteworthy problems.

Elderly individuals digest and absorb protein differently than healthy adults. In fact, they digest and absorb whey protein in a similar manner as they do casein (Dangin et al., 2003); in other words they have slow digestion and absorption for whey. Elderly also benefit from having 80% of their daily protein consumed at a single sitting (Arnal et al., 1999), in contrast to the benefits of our multiple feedings.

Additionally, the traditionally referenced Esmark et al. (2001), study showed that consuming the post workout meal just 2 hours after working out actually prevented any improvements induced by the training! Figure that one out and you get a prize.

Secondly, with regards to cardio…well, let’s just say that there’s an obvious difference between how our muscles respond to the two forms of exercise. Bear in mind that with regard to carbohydrate metabolism following a workout, there might not be much of a difference—we just don’t know, but certainly the long-term protein metabolism differences can be seen.

So now what are we supposed to base our nutrition on? Enter the most underrated scientific paper in the last 5 years. Tipton and colleagues (2003) examined responsiveness of protein synthesis for a day after a workout, and found it to reflect a 24 hour enhanced level. That’s right folks, a FULL DAY! This means that having a morning shake will have the same impact on muscle protein synthesis as one consumed following the workout!

These results shouldn’t be too surprising because we’ve known for over a decade that postworkout protein synthesis is jacked up for this long (MacDougall et al., 1995), but if you’re discovering this for the first time, then it’s pretty exciting!

Some research suggests that even 48 hours after the workout our protein synthesis levels can be elevated by ~33% (Phillips et al., 1997), giving us an even longer period during which we can maximize our muscle growth with protein drinks.

Strike one for the one hour post workout window.

5. Consuming the drink immediately following the workout will elicit the greatest protein synthesis.

It’s amazing to see how more advanced, and often experienced, people behave in the gym when it comes to getting their post workout meal. Some guys even sit there, right after their last set, and slug back a drink! In fact I’ve even heard “as soon as the weight hits the floor” touted as the war cry for the hardcore. While this is actually a sub-optimal practice for muscle growth and recovery, not to mention borderline obsessive compulsive, it’s good to see their heart is the right place.

Comparing research that used drinks consumed immediately after a workout (Tipton et al., 2001) versus those ingested an hour after training (Rasmussen et al., 2000), the results are surprising: it seems that post workout meal ingestion actually results in 30% lower protein synthesis rates than when we wait! So every time we thought that we were badass for drinking “as soon as the weight hit the floor, we were actually short changing ourselves. [NOTE: This isn’t suggesting that you wait a full hour before drinking, it’s simply when the measurements were taken.] Not a big deal, that’s why we read research reviews like this. Let’s just learn, adapt, and move on.

Strike two for the one hour post workout window.

6. The best meal to consume following a post workout meal is a good SOLID meal.

This is where we can start to apply some of the novel information presented above. While we know that our post workout window (is it really even a window any more? 24 hours is more like a giant garage door) lasts for at least 24 hours, we can’t assume that the responses to repeated meals will all be the same.

This is where research by Borsheim and pals (2002) comes in. This landmark research shows that the best thing to consume after our post workout meal is… another protein shake! In fact, if we time it right, we’ll get the same huge increase in protein synthesis. Talk about a double whammy for our muscle growth! Now considering how crazy people get when it comes to a single post workout meal, imagine how they’ll react when you tell them that they can double that effect!

Also, for those who have a hard time accepting the reality explained in myth #5, you’ll get an even bigger response from the second drink, compared to what you get from the first.

7. Insulin sensitivity is enhanced for an hour following a resistance training bout.

The term insulin sensitivity gets thrown around in the strength-training world, as only the most vague of concepts. From here on, lets universally define it as: the inverse of the quantity of insulin required for an effect of a given magnitude. In other words, high insulin sensitivity requires low levels of insulin to do the job. Make sense? Now that we have a working definition, we need to destroy the myth of the one-hour post workout window once and for all!

We know that both endurance exercise and strength training will enhance insulin sensitivity in the long term. This is a good thing. Unfortunately, with all of the hype surrounding the post workout window, people have started throwing out numbers related to how long insulin sensitivity is altered. While we know that heavily damaging eccentric exercise will actually reduce insulin sensitivity (Asp et al., 1996), this should be an extreme condition and not our regular response. So if you’ve overdone it a bit, back off and heal up!

The more common response to strength training is an increase in insulin sensitivity (Fujitani et al., 1998; Miller et al, 1984), and brand new data show even the acute effect from a single bout lasts for over 24 hours (Koopman et al., 2005). So while we’ll have an enhanced whole body insulin sensitivity following resistance training, this effect is even greater for 24 hours following exercise!

Steeerike THREE for the one hour post workout window!

8. Whey is a “fast” protein, ideal for post workout.

Back when it first came out, whey protein was pretty kick ass because it was discovered to be very high quality. Then research came out that made it even more kick ass, because we could classify it as a “fast” digesting protein compared to casein (Boirie et al., 1997).

You know what? This research stands today, because compared to casein, whey protein really is fast! Then again, a tortoise is also fast compared to a snail, but that doesn’t mean we want to take a tortoise to a greyhound park. In other words, we’ve been considering whey a “fast” protein only because we’ve been comparing it to something incredibly slow. When we compare the digestibility of whey to the gold standard of amino acids, on which we base nearly all of our post workout nutritional data, whey flat out sucks.

This is incredibly frustrating because all of the ways to maximize protein synthesis we’ve been discussing have used amino acids. So we need to either use pure amino acids or use something that closely resembles their absorptive properties. This is where whey protein hydrolysate comes in. The protein is already broken up into large peptides, so we get a rapid absorption with peak levels reaching the blood at around 80 minutes (Calbet and MacLean, 2002), compared to 60 minutes for pharmaceutical grade amino acids (Borsheim et al., 2002).

Unfortunately, even the highly touted whey isolate is completely useless for our timing purposes here, because it just takes too long to get taken up by the gut (Dangin et al., 2002). This is all discussed in more detail in the official product review of Surge, complete with graphs of blood amino acid profiles.

In light of these data and the growing body of literature contradicting the versatility and usefulness of whey protein, it should henceforth be classified as “moderate” or “intermediate” speed protein, with only whey hydrolysate and amino acids existing as truly “fast.”

It may be difficult to adjust our thinking, but this is simply more dogma that needs to be destroyed in order to bring us up to date with the proper application of research.

9. Using antioxidants post workout enhances recovery.

Here’s another myth that just makes sense: we work out, cause all kinds of damage to our bodies, then we use antioxidants to help clean up the mess. Simple and sweet. The reality? Neither simple or sweet. In fact, it may not surprise you to find that there is a clear lack of data on antioxidant supplementation following exercise.

Taking a step back to look at the basis for the theory, it’s been shown that damaging eccentric exercise didn’t change the normal levels of our body’s antioxidants (Child et al., 1999). In other words, our body has a natural antioxidant defense capability, and this was not stressed at all despite the exercise and the subsequent muscle damage.

This is contradicted by other data showing that there is an impact of exercise on natural antioxidant levels (Lee et al., 2002; Goldfarb et al., 2005), but clearly the case is not closed. With this conflicting research, you’d have to wonder if antioxidant supplementation would have any effect at all! Oh it does, my oxidized friend, but the effects are not what we’d expect!

Once again, here’s one of the most underrated research papers of the last 5 years—take note folks because this is one of those studies you need to know about. This groundbreaking research by Childs and buddies (2001) examined the impact of post workout antioxidant supplementation on subsequent muscle damage and healing.

You’ll be shocked to know they found that this practice actually increased muscle damage and delayed recovery! That’s right, the microtrauma experienced by the muscle cells was exacerbated by the antioxidants. With this, the greater the damage, the more time it takes to repair.

It seems that there are pro-oxidant effects happening here, meaning that the “antioxidants” actually started causing the damage they were meant to clean up! While this effect is thought to occur with excessive antioxidant use, it’s surprising that these effects were seen at a Vitamin C dosage of ~1100mg and ~900mg N-Acetyl Cysteine per day, for a 200 lb guy, neither of which are all that incredibly high. To my knowledge, this is the only study to investigate antioxidant supplementation after strength training. This makes the findings incredibly powerful because they are directly applicable to us!

On a personal note, I was pretty blown away when I read this paper because I’d been using Vitamin C post workout for years. While these data aren’t strong enough to make me swear off antioxidants altogether, they clearly show that we can overdo it quite easily with these supplements. More importantly, these data help us rethink the post workout window dogma.

10. Aspirin and ibuprofen are good anti-inflammatories for muscle recovery.

The topic of muscle inflammation is pretty hot these days because it’s thought that minimizing this natural response will enhance recovery. By allowing us to hit the gym or get back on the field quicker, we can once again stimulate our bodies with a hard training session.

While the theory holds some water, we need to be careful how far we take it. For example, the use of traditional pain relievers, like aspirin and ibuprofen, has been increasingly common, because most people just don’t like the feeling of muscle soreness (T-Nation readers excepted because we’re hardly “most people”).

A common effect of these pain relievers is that they exert a powerful anti-inflammatory effect. This fact has excited some budding pseudo-scientists, because they reason that using these common drugs will reduce muscle inflammation and enhance recovery. Great theory, poor applicability.

Early research showed that post workout use of these drugs inhibited our natural production of a chemical necessary for muscle growth and repair (Trappe et al., 2001). Further investigation showed that sure enough, muscle protein synthesis was completely shut down when these drugs were combined with strength training (Trappe et al., 2002). As a final kick in the teeth, using these drugs resulted in no effect on either inflammation (Peterson et al., 2003), or muscle soreness (Trappe et al., 2002).

Essentially we get the worst of all worlds when combining nonsteroidal anti-inflammatory drugs (NSAIDS) like aspirin and ibuprofen, with strength straining. Having said that, it is important to note that there are several different ways of affecting inflammation, some may be good, others are clearly bad. Keep in the back of your mind that limiting inflammation is a good idea, but certainly be aware that it is not universally beneficial.

Update: The acute effects of NSAIDS do not appear to have long-term consequences for muscle growth.

Ten Take Home Points

—glycogen restoration is all too easy to achieve and may not be as critical as once thought

—protein synthesis needs to be the focus of our recovery intervention

—pre-workout meals actually enhance muscle blood flow and nutrient delivery during exercise

—pre-workout meals, nocturnal feeding, and multiple post workout drinks are more beneficial than a single post workout drink

—the “post workout window” lasts at least 24 hours

—consuming a protein shake immediately after training hinders optimal results

—strength training acutely enhances insulin sensitivity for at least 24 hours

—whey protein is generally only moderate speed, while whey hydrolysate and pure amino acids are “fast”

—antioxidants taken after exercise may increase muscle damage and delay recovery

—aspirin and ibuprofen can prevent the exercise-induced elevation in muscle protein synthesis thus hindering growth and prolonging recovery

Five Frequently Asked Questions

FAQ: If we don’t care about glycogen, then why would we use high glycemic carbs post workout?

A: Don’t forget that the main goal is to maximize protein synthesis, which is likely accomplished using quickly absorbed carbohydrates and greatly elevating insulin.

Update: Spiking insulin is neither required nor desirable for maximal muscle protein synthesis.

FAQ: In the study with the pre workout drink, what did they consume and when did they drink it?

A: Pure amino acids and sucrose were consumed immediately before training started.

FAQ: Doesn’t consuming carbs before a workout cause a blood sugar crash during the workout?

A: Usually no, our catecholamine response seems to keep out blood sugar elevated without problems. But if you’re just starting to try this, consume carbs during the workout or have them ready just in case.

FAQ: If there is a 24-hour post workout window, why do we care about consuming multiple drinks?

A: The multiple drink method is still the best way to maximize our anabolic response following training. We take advantage of this “window” by spiking our blood amino acid level as often as we can.

FAQ: If there is a 24-hour post workout window, why do we care about fast or intermediate speed proteins?

A: The multiple drink method can only be used when fast proteins or amino acids are consumed. It just doesn’t work with intermediate speed proteins.


It’s safe to say that we’ve been brought up to date with the current research regarding strength training and nutrition. Perhaps more importantly it’s clear that the post workout dogma has been destroyed. Unfortunately, with all of this destruction going on, there is a knowledge gap that needs to be filled, which will allow us to apply these new findings.

In other words, we need to figure out what all of this science stuff means, and how we can best use it to our advantage. In an upcoming article, I’ll introduce the Anabolic Index: a detailed blueprint for making use of this latest information, allowing us to maximize our anabolic potential.

Until then, Raise the Barr!

David Barr is widely recognized as an industry innovator, most recently for his work on developing The Anabolic Index. As a strength coach and scientist, he brings a unique perspective to the areas of diet, supplementation, and training. His research experience includes work for NASA at the Johnson Space Center, as well as studying the effect of protein on muscle growth. He holds certifications with the NSCA as well as USA Track and Field, and can be contacted through his website: http://www.RaiseTheBarr.net.


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8. Coggins M, Lindner J, Rattigan S, Jahn L, Fasy E, Kaul S, Barrett E. Physiologic hyperinsulinemia enhances human skeletal muscle perfusion by capillary recruitment. Diabetes. 2001 Dec;50(12):2682-90.

9. Dangin M, Boirie Y, Garcia-Rodenas C, Gachon P, Fauquant J, Callier P, Ballevre O, Beaufrere B. The digestion rate of protein is an independent regulating factor of postprandial protein retention Am J Physiol Endocrinol Metab 280: E340-E348, 2001

10. Dangin M, Guillet C, Garcia-Rodenas C, Gachon P, Bouteloup-Demange C, Reiffers-Magnani K, Fauquant J, Ballevre O, Beaufrere B. The rate of protein digestion affects protein gain differently during aging in humans. Physiol. 2003 Jun 1;549(Pt 2):635-44.

11. Esmarck B, Andersen JL, Olsen S, Richter EA, Mizuno M, Kjaer M. Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans. J Physiol. 2001 Aug 15;535(Pt 1):301-11.

12. Fujitani J, Higaki Y, Kagawa T, Sakamoto M, Kiyonaga A, Shindo M, Taniguchi A, Nakai Y, Tokuyama K, Tanaka H. Intravenous glucose tolerance test-derived glucose effectiveness in strength-trained humans. Metabolism. 1998 Jul;47(7):874-7.

13. Goldfarb AH, Bloomer RJ, McKenzie MJ. Combined antioxidant treatment effects on blood oxidative stress after eccentric exercise. Med Sci Sports Exerc. 2005 Feb;37(2):234-9.

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17. Levenhagen DK, Gresham JD, Carlson MG, Maron DJ, Borel MJ, Flakoll PJ. Postexercise nutrient intake timing in humans is critical to recovery of leg glucose and protein homeostasis. Am J Physiol Endocrinol Metab. 2001 Jun;280(6):E982-93.

18. Louis M, Poortmans JR, Francaux M, Berre J, Boisseau N, Brassine E, Cuthbertson DJ, Smith K, Babraj JA, Waddell T, Rennie MJ. No effect of creatine supplementation on human myofibrillar and sarcoplasmic protein synthesis after resistance exercise. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E1089-94.

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21. Pascoe DD, Costill DL, Fink WJ, Robergs RA, Zachwieja JJ. Glycogen resynthesis in skeletal muscle following resistive exercise. Med Sci Sports Exerc. 1993 Mar;25(3):349-54.

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23. Phillips SM, Tipton KD, Aarsland A, Wolf SE, Wolfe RR. Mixed muscle protein synthesis and breakdown after resistance exercise in humans. Am J Physiol. 1997 Jul;273(1 Pt 1):E99-107.

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Resistance-training-induced adaptations in skeletal muscle protein turnover in the fed state. Can J Physiol Pharmacol. 2002 Nov;80(11):1045-53.

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27. Tipton KD, Borsheim E, Wolf SE, Sanford AP, Wolfe RR. Acute response of net muscle protein balance reflects 24-h balance after exercise and amino acid ingestion. Am J Physiol Endocrinol Metab. 2003 Jan;284(1):E76-89.

28. Trappe TA, Fluckey JD, White F, Lambert CP, Evans WJ. Skeletal muscle PGF(2)(alpha) and PGE(2) in response to eccentric resistance exercise: influence of ibuprofen acetaminophen. J Clin Endocrinol Metab. 2001 Oct;86(10):5067-70.

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Effect of ibuprofen and acetaminophen on postexercise muscle protein synthesis. Am J Physiol Endocrinol Metab. 2002 Mar;282(3):E551-6.

Originally Published Tue, Jun 14, 2005 Testosterone.net

PUBLISHED 06-14-05 13:31″

Source: tmuscle.com

David Barr articles on tmuscle.com

The protein and the kidney monologue – CharlesPolquin.com and Jose Antonia

The Protein and the Kidney Monologue

Credit: CharlesPolquin.com and Jose Antonia, Ph.D.

By Jose Antonio, Ph.D.

One of my close friends is a professor at a fairly high profile Midwestern university (he’ll remain anonymous so as to avoid the wrath of his fellow protein-hating colleagues) and we were talking recently about how grossly misinformed many in academia are regarding dietary protein intake.

This is what you’ll often hear in the ivory towers.

“High protein diets are bad for your kidneys.”
“Protein dehydrates you.”
“Athletes get plenty of protein in their normal diets.”
“Protein is evil.”
Okay, maybe the last one is an exaggeration; albeit a slight one.

For whatever odd reason, some of the most educated individuals are also some of the most misinformed when it comes to dietary protein. First, let me set the record straight.

There is no evidence that high protein diets (which I’ll operationally define as 2-3 times greater than the ridiculously low RDA) is harmful to otherwise healthy individuals.(1)
There is evidence that in individuals with renal dysfunction may need to consume protein that even exceeds the RDA.(2)
The addition of protein to a sports drink does not dehydrate you and may in fact improve performance and recovery.(3)
Athletes do need more protein than couch potatoes.
Protein is not evil. (Sorry, no references).
What the heck is protein anyway?
Just as glucose serves as the building block of glycogen, so are amino acids, which are the building blocks of proteins. Proteins are arguably the most important component of your cells.

They’re involved in formation of contractile tissue or muscle, they make up a large part of the structural component of cells, they are a part of enzymes, antibodies, blood, etc. You name it, protein is part of it.

The main function of protein is to provide the needed amino acids for maintaining an anabolic (growth) or weight-stable state. However, recent data shows that additional protein promotes recovery and performance during exercise. (3, 4)

How much protein should you consume?
The easiest way to remember how much protein to consume is via the formula – 1 gram of protein per pound of body weight. Hence, a 200 pound individual needs about 200 grams of protein. And don’t be misled by the “carb-Nazis” who pontificate on the impending doom of your kidneys if you consume this much protein. If that were the case, gyms would be littered with strength-power athletes with failing kidneys.
In fact, according to Darryn Willoughby, Ph.D., of the International Society of Sports Nutrition and member of AXL’s Advisory Board, “the hazards of eating a high protein diet are as overblown as a big Texas hairdo. Now if you have damaged kidneys then the work that your kidneys need to perform to eliminate excess nitrogen would make it wise to avoid excess protein. Otherwise, enjoy that Porterhouse.”

Suffice it to say that the RDA of 0.8 grams per kilogram body weight per day is grossly inadequate for anyone whose activity levels exceed that of a La-Z-Boy recliner. Even though muscle protein degradation or breakdown increases during exercise, there is a significant increase in muscle protein synthesis for at least 24 hours after either resistance or endurance exercise. If you are not getting adequate protein during this time, then it would make sense that you probably will not gain lean body mass.

How much protein can I consume at one sitting?
Great question! Unfortunately, the scientific answer isn’t known. But I’ll give you the Midwestern common sense answer. Would your 75 year old grandma and the 250 lb, 25 year old martial arts fighter have the same limitations when it comes to digesting and absorbing protein? Obviously, the fighter needs more protein to assist with recovery and repair of muscles.

In all fairness, there are studies in which levels of 30 grams of protein are fed to subjects; and this amount produces a tremendous rise in blood amino acid levels. I’d imagine that 30 grams of protein per meal is a good starting point. If you eat 30 grams a sitting and you eat 6 times daily, that’s about 180 grams of protein.

For most “normal-weight” individuals, that should suffice. But imagine if you’re a 300 lb football player or bodybuilder? You’d either have to eat more protein per sitting or just eat more meals. The answer to this problem? Consume meal replacement powders as a protein supplement.

Protein and those with real kidney problems – the other viewpoint
A recent paper discussed two of the National Kidney Foundation Kidney Disease Outcomes Quality Initiative (K/DOQI) clinical practice guidelines for nutrition in chronic renal failure.

These guidelines recommended a dietary protein intake of 1.2 g protein/kg body weight/day for clinically stable maintenance hemodialysis (MHD) patients (Guideline 15) and 1.2 to 1.3 g protein/kg/day for clinically stable chronic peritoneal dialysis (CPD) patients (Guideline 16).

If you do the math, that is roughly 50% to 63% greater than the regular RDA or recommended daily allowance. But I thought eating protein was evil, evil, evil? Maybe not.

Scientists suggest that the possible mechanisms that require these increased protein needs include (a) the substantial quantity of amino acids, peptides, and proteins removed by the dialysis procedure and (b) the protein catabolic or anti-anabolic state caused by the uremic milieu, the inflammatory state, the oxidative and carbonyl stress, and the bio-incompatible dialysis materials to which MHD and CPD patients are exposed. In English, that means these individuals tend to be very catabolic and need to somehow replace the lost amino acids or protein. (2)

Protein types – the slow and the fast!
Cool work from France delineated the concepts of “slow” and “fast” proteins. In fact, this may play a greater role in muscle protein metabolism than the older concepts of biological value.

In essence, there are two proteins that many of us consume, which are digested at different rates (hence, slow and fast). In comparing whey to casein protein, whey is a faster protein, meaning it’s absorbed quickly into the bloodstream and remains elevated for about 3 to 4 hours. On the other hand, casein tends to clot in your stomach and in essence is “timed-released” such that you have significant elevation of blood or plasma amino acids for up to 7 hours.

Why are these distinctions important? First of all, whey is a very anabolic protein. However, inasmuch as you get a quick rise in plasma aminos, you also get quite a bit of oxidation of the protein (i.e. it is used for fuel). Casein however does not promote as much anabolism but is very anti-catabolic (i.e. inhibits protein breakdown). The “net” effect is that if you do a head to head comparison, casein beats whey over the long haul. Does that mean you should dump that bucket of whey into the trash bin? Hell no.

In fact, take advantage of whey’s easy and quick digestion/absorption qualities and consume it as part of your post-workout meal. Casein may be best if consumed as a single meal prior to bed (to sustain plasma aminos throughout the day).(5-9)

Protein and bone health
According to one study, protein intakes do not contribute to the wide variability in calcium absorption efficiency. (10) Or put another way, eating protein probably has no effect on bone mineral content.

Another investigation stated verbatim that “several recent epidemiological studies demonstrate reduced bone density and increased rates of bone loss in individuals habitually consuming low protein diets.” (10-12) So, one might argue that low protein intakes is the culprit. Either way, it would be wise to consume both adequate protein and calcium to maintain lean body mass and reduce body fat.

Adding protein to sports drinks
In a recent study that compared a traditional sports drink (water, carbs, and electrolytes) versus a sports drink that contained added protein, they found that cyclists rode 29% to 40% longer when they consumed the sports drink with protein than the one without.

Also, peak post-exercise plasma CPK (creatine phosphokinase) levels, an indirect measure of muscle damage, was 83% lower after consuming the sports drink plus protein. So don’t believe the baloney about protein dehydrating you (’cause if it did, these cyclists would not have performed better) or being unimportant during exercise. Even a small amount (~3-6 grams) during exercise might do wonders for you!(3)

The Moral of the Story

Consume 1 gram of protein per pound of body weight daily.
Spread it out over 6 meals.
Protein intake 2-3 times over the RDA is not harmful to your kidneys, bones, or anything else for that matter.
Adding a touch of protein to a sports drink may improve performance and speed up recovery.
Consume “fast” proteins after you exercise and “slow” proteins at the end of the day.
Listen to the Performance Nutrition Show at www.pnshow.com ; download the podcast and keep updated on the newest findings in sports nutrition!


Poortmans JR, Dellalieux O. Do regular high protein diets have potential health risks on kidney function in athletes? Int J Sport Nutr Exerc Metab 2000;10:28-38.
Kopple JD. The National Kidney Foundation K/DOQI clinical practice guidelines for dietary protein intake for chronic dialysis patients. Am J Kidney Dis 2001;38:S68-73.
Saunders MJ, Kane MD, Todd MK. Effects of a carbohydrate-protein beverage on cycling endurance and muscle damage. Med Sci Sports Exerc 2004;36:1233-8.
Flakoll PJ, Judy T, Flinn K, Carr C, Flinn S. Postexercise protein supplementation improves health and muscle soreness during basic military training in marine recruits. J Appl Physiol 2004;96:951-6.
Dangin M, Boirie Y, Garcia-Rodenas C, et al. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am J Physiol Endocrinol Metab 2001;280:E340-8.
Beaufrere B, Dangin M, Boirie Y. The ‘fast’ and ‘slow’ protein concept. Nestle Nutr Workshop Ser Clin Perform Programme 2000;3:121-31; discussion 131-3.
Boirie Y, Beaufrere B, Ritz P. Energetic cost of protein turnover in healthy elderly humans. Int J Obes Relat Metab Disord 2001;25:601-5.
Boirie Y, Broyer M, Gagnadoux MF, Niaudet P, Bresson JL. Alterations of protein metabolism by metabolic acidosis in children with chronic renal failure. Kidney Int 2000;58:236-41.
Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrere B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A 1997;94:14930-5.
Heaney RP. Dietary protein and phosphorus do not affect calcium absorption. Am J Clin Nutr 2000;72:758-61.
Kerstetter JE, O’Brien KO, Insogna KL. Low protein intake: the impact on calcium and bone homeostasis in humans. J Nutr 2003;133:855S-861S.
Kerstetter JE, O’Brien KO, Insogna KL. Dietary protein, calcium metabolism, and skeletal homeostasis revisited. Am J Clin Nutr 2003;78:584S-592S.”

Source: www.charlespoliquin.com