Time and time again though, examining scientific journals instead of the latest muscle magazine proves to produce the best results? Why? Because the information presented in these scientific studies is based on actual data and observations and not from the local gym guru. In this article, we will examine a scientifically backed nutrition and supplement plan designed to promote an anabolic environment that will ensure growth and advancement.
Before we discuss the dietary blueprint for anabolism, an understanding of how muscle grows and gets stronger must be gained. All tissue of the body (skin, hair, muscle, etc.) goes through a process of turnover, or renewal. With skin, old tissue dies off and is replaced with new skin. This renewal process is accelerated if the tissue experiences a form of stimulus or overload. Concerning skin, a guitar player's fingers serve as a fine example.
When some people first begin to play the guitar, the tips of their fingers are soft. This makes playing against steel strings painful. Frequent playing causes the skin at the tips of the fingers, where they come in contact with the guitar strings, to become hard and calloused. The old, soft skin has been replaced by a tough, durable layer of skin, allowing the guitar player to play with ease and comfort. Without turnover taking place, new skin would not have formed. The same process applies to muscle tissue.
Muscle tissue, just like skin, is constantly being turned over. The rate at which this turn over occurs is governed by protein synthesis and protein breakdown. In turn, protein synthesis and protein breakdown are regulated by ones diet, lifestyle (sedentary verses active), and genetics . Just as the guitar player must apply a stimulus (the steel strings), an athlete must stimulate their muscles with exercise to accelerate this process.
The purpose of exercise, especially resistance training, is to increase this protein turnover. This includes both protein synthesis and breakdown. When a weight lifting exercise is performed, the muscle cells used to create the force needed to achieve the desired movement can become damaged. By progressively increasing the weight lifted and the force needed to move the weight, the body becomes programmed to think it must prepare itself for heavier workloads. Therefore the damaged muscle cells are removed and replaced with new, stronger muscle. This process continues while the exercise bouts continue. When the exercise bouts cease, so will the process of replacing the old, weaker muscle with new, stronger muscle.
Going back to the guitar player example, when a guitar player stops playing the guitar for a period of time, the callouses that were formed fade away. The body senses there is no longer a need for the tough layer of skin and replaces it with weaker skin. The exact thing happens with muscle tissue. That is why when one stops lifting weights, their muscle stop growing and actually decreases in size and strength. This is just a brief overview of protein turnover. For the purpose of this article, we do not need to get into transcription and translation.
It should be clear that in order to continuously prep the body to create new, stronger muscle, one must overload the muscle. But what happens when overload occurs and there are not adequate materials to create the new muscle? Muscle is lost!
If the amount of muscle broken down exceeds the amount that can be replaced, protein turnover is negative and there is a net loss of muscle. This is counterproductive to what the athlete is trying to accomplish with training. To ensure that an athlete's hard work and time spent exercising is not wasted, protein turnover must remain positive. To accomplish this, precise nutritional requirements must be meet.
Protein - Learn More
The word protein comes from the Greek word meaning "of prime importance." The naming of this nitrogen-containing macronutrient is extremely fitting, especially when considering its need during strenuous periods, such as exercise. Proteins are the most abundant organic compounds in the body . The primary function of protein is growth and repair of body tissue (anabolism). Proteins can also be used as energy through catabolic reactions, such as gluconeogenesis. Amino acids are the "building blocks" of protein. Amino acids are made up of an amino radical (NH2) and a carboxyl group (COOH). What make amino acids different are their side chains.
A protein molecule is made up of long chains of amino acids bonded to each other by amide bonds, or peptide linkages. An almost endless combination of amino acid bonds can exist. The combination of amino acids governs the protein's properties.
Amino acids can be divided into many groups based on their physical properties. For the purposes of our discussion there are two that are relevant: essential amino acids (EAA) and nonessential amino acids (NEAA). EAA must be consumed through ones diet, because they cannot be synthesized in the body at a sufficient rate to meet demands . NEAA can be synthesized in the body from other protein and non-protein nutrients.
|Essential Amino Acids||Nonessential Amino Acids|
Amino acids have a very strong impact on muscle growth. Specific amino acids and amino acid combinations also have special properties. Combinations of different carbohydrates also create special properties.
Carbohydrates - Learn More
Carbohydrates are organic, water-soluble substances. The formula for a carbohydrate is (CH2O)N, where N can be three to seven carbon atoms. Glucose is the body's primary energy source. It can be directly used by the cell for energy, stored as glycogen for later use, or converted to fat and stored as energy. More specifically, glucose is a monosaccharide, meaning it cannot be broken down into simpler units. Other monosacaccharides include fructose and galactose.
The bonding of two simple sugars creates a disaccharide. Examples of disaccharides are sucrose (glucose and fructose), maltose (glucose and glucose), and lactose (glucose and galactose). These monsaccharides and disaccharides are known as simple sugars. when three or more sugars bond together, a polysaccharide is formed. Examples of polysaccharide, or complex carbohydrates, are fiber, glycogen, and starch. Glycogen is not present in large amounts in the foods we eat, so it must be created.
Glycogen is formed of glucose molecules lined together in chains. These chains can contain hundreds (over even ten thousand plus) of glucose molecules. The glycogen in our bodies is created from the glucose we consume in our diets. This glucose becomes "trapped" in the liver and muscles, where it is synthesized or stored for later use as glycogen. The liver can hold around 100 grams of glycogen, while around 325 grams of glycogen is stored in muscle. The amount of unstored glucose circulating in the blood is only around 15 to 20 grams [24,35]. This process of creating glycogen in the liver is called glycogenesis. When glucose is needed as an energy source, the glycogen stored in the liver is reconverted to glucose through a process called glycogenolysis.
When glycogen stores are low, glucose can be derived from other nutrients, such as protein. This creation of glucose from non-glucose nutrients is called gluconeogenesis. Gluconeogenesis is regulated by the catabolic hormone cortisol, which is one of an athlete's worst enemies. Many changes take place in the body during exercise. In order to create the most anabolic environment, we have to understand these changes, which includes the release of cortisol.
What Happens During A Workout?
I'd like to note that my reference to exercise will be dealing with strength training and not endurance training. The effects of endurance training on protein turnover are somewhat different than the effects from strength training.
After completing an exercise session, two main things have occurred. One is the depletion of muscle glycogen. And the other is an increase in protein breakdown . Protein synthesis has decreased , experienced no change  from its pre-workout status, or slightly increased . Remember when one lifts weights, muscle cells are damaged. When these cells are damaged, they are removed. Because of the elevated level of protein breakdown and the almost unchanged level of protein synthesis, protein turnover is negative, meaning one is in a catabolic state . Low glycogen levels can also put one in a catabolic state.
Exercise causes glycogenolysis to take place. The glycogen stored in the liver and muscle is released when it is needed for production of adenosine triphosphate (ATP), or energy. ATP is the body's fuel for all energy-requiring processes. ATP is made up of one molecule of adenine and ribose (together called adenosine) and three phosphates (consisting of phosphorus and oxygen atoms).
Energy is stored in the bonds that link the two outermost phosphates. When the outermost phosphate--phosphate bond is broken, energy is released. What is left is a molecule called adenosine diphosphate, which has one adenosine molecule and two phosphates. This ADP molecule can become ATP by using energy from foodstuffs and the ATP-PC system (creatine-phosphate). For example, the energy created by splitting the bonds between glucose molecules can be used to regenerate ATP from ADP. The body only stores around 85 grams of ATP at any given time . Because of this limited storage, the demand for glucose to create ATP is accelerated when lifting weights.
Strength training is a form of anaerobic exercise, meaning energy-releasing reactions happen without oxygen. Without oxygen present, the body must rely on the ATP-PC system and anaerobic glycolysis to obtain the energy needed to regenerate ATP. The problem is, the ATP-PC energy system is very limited. It provides energy for muscular contraction during short, high intensity bursts of exercise, usually lasting less than five seconds .
Therefore the energy demands for regeneration of ATP during weight training primarily come from the anaerobic glycolysis system, meaning muscle glycogen is an athlete's primary fuel during intense exercise . This elevated need for glucose leads to extreme depletion of muscle glycogen stores and blood glucose. Studies show that intense strength training depletes muscle glycogen stores much more than had previous been thought [28, 39, 45, 46].
Low glycogen levels have been shown to cause decreased intensity, mental focus, and performance during exercise [2, 3, 18, 25, 26, 29, 32, 44, 54, 58, 59]. The exact opposite occurs when sufficient glycogen is present, as endurance increases . Of more concern to weightlifters is that low muscle glycogen levels mean reduced strength [19, 22]. Even worse is the fact that low glycogen levels increase muscle protein breakdown [9, 57]. These findings hold true for both endurance and strength training [3, 29, 32, 44]. This increase of protein breakdown is on top of what is caused by the exercise itself.
During exercise, catabolic activities cause proteins and muscle tissue to be broken down. The greater the intensity of the workout, the greater the catabolic response. This is due to the increase in production of catecholamines and glucocorticoids. Of prime concern to us is the glucocorticoid cortisol.
Cortisol is a very catabolic hormone as it increases muscle protein breakdown [15, 38]. Cortisol regulates glucose synthesis from amino acids through the process of gluconeogenesis . Cortisol has been shown to increase protein breakdown by 5-20%! Another reason why exercising with low glycogen levels is a bad idea is lean muscle tissue will be lost. This loss in muscle is due to the intracellular pool of amino acids being depleted. In order to maintain this pool, muscle tissue most be broken down .
Cortisol also negatively affects certain hormones. Cortisol can inhibit growth hormone levels by activating the release of somatostatin, an antagonist of growth hormone. It has also been shown to reduce IGF-1 expression. IGF-1 is one of the most anabolic hormones in the body. Any decrease is unwanted. Cortisol also inhibits thyroid-stimulating hormone (TSH) . This can cause a decrease in ones metabolic rate, making it harder to lose body fat. In order to recover adequately from exercise, cortisol levels must be controlled.
From the above, it should be obvious that during training we need to:
- Reduce the depletion of glycogen stores
- Reduce muscle protein breakdown
- Significantly increase protein synthesis
How can this be done? By using a scientifically backed nutrition plan. Studies have shown that in the absence of food, protein breakdown exceeded protein synthesis after a workout [7, 33, 34]. Most athletes know the positive effects of consuming a post workout meal. The body is primed for nutrient uptake after a workout. So one way, and the most popular, to accomplish the above is to consume a post workout shake.
There are many commercial powders available for this purpose. This is a good start, but I am here to show you one of the most efficient workout nutritional setups. Not only will this setup promote extreme anabolism, but it will also stop catabolism dead in its tracks before it even starts. This workout nutritional setup involves consuming three shakes: a pre-workout shake, during workout shake, and a post workout shake.
In order for these shakes to be effective, they need to contain both protein and carbohydrates; and not just any type of protein or type of carbohydrate, but specific forms.
Amino Acids & Exercise
Only six of the 20 amino acids are directly metabolized by muscle. These six amino acids are: alanine, aspartate, glutamine, isoleucine, leucine, and valine [21, 57]. These six amino acids are metabolized at accelerated rates during exercise . They are also imtermediates that regenerate the aerobic-TCA energy cycle [57.] During exercise, the carbon atoms from these amino acids are unbidden by protein degradation. The Brain Chain Amino Acids (BCAA) and glutamine are then used to synthesize intermediates for use in the TCA cycle.
This is not good for muscle anabolism because the cellular levels of these amino acids greatly impact growth. Therefore when the supply is depleted, growth significantly suffers. Of these six amino acids, alanine, aspartate, and glutamine are nonessential, but isoleucine, leucine, and valine are the essential branch chain amino acids (BCAA), which serve an even greater role in energy metabolism and muscle growth.
BCAA are of extreme importance. BCAAs are absorbed directly into the circulatory system, bypassing the liver, which allows them to be used for rapid protein synthesis. Studies have shown that BCAA directly supply the nitrogen needed to create and export concentrations of alanine and glutamine produced by muscle [21, 30, 55, 56]. Because of this, BCAA concentrations are lowered from any type of exercise. One study showed that BCAA concentrations were decreased by 30% from aerobic exericise and 8-20% from anaerobic/aerobic exercise . The largest decrease in BCAA concentrations were seen in anaerobic exercise, such as weight training . Of the three BCAA, leucine is of greatest importance during exercise.
Transaminiation of leucine's nitrogen to alanine is doubled during exercise . Leucine is the only amino acid that is capable of being completely oxidized in the TCA-aerobic cycle. Because leucine is an EAA, this oxidation capability is not good for muscle growth, as it can quickly deplete leucine levels. Leucine has been shown to directly stimulate protein synthesis and muscle turnover [43, 53], and without leucine, protein synthesis rates are impaired . To make matters worse, leucine has the shortest half-life of all amino acids in the free pool of 45 minutes. This is compared to the 5-10 hour half lives of the other amino acids . It is constantly being oxidized, leaving little for protein synthesis. Leucine levels need to be increased before protein synthesis can excel.
It should be obvious from examining the above information that the protein source used must contain large amounts of EAA, especially BCAA, and with even more emphasis on leucine. Mero showed that consuming a BCAA supplement, with 30-35% leucine, before or during exercise decreased the rate of protein breakdown, improved both mental and physical performance, and had a sparing effect on muscle glycogen levels .
To meet the need for amino acids during exercise, a supplement containing high amounts of EAA and especially BCAA is needed. In order for this protein to be as effective as possible, it needs be a fast absorbing protein. Therefore, protein powders such as casein and milk isolate are discouraged because of their slow digestion rates. Egg protein is another option, but it is still absorbed too slow. These slow digesting protein can create an environment in the intestines that competes with the muscles for blood flow.
Though this competition for blood is not substantially strong it still exists. That leaves us with whey protein. The quickest absorbed of the whey family is hydrolyzed whey. Hydrolyzed whey is one of the most rapidly digested proteins available.
Hydrolyzed whey has an excellent amino acid profile. Here is the amino acid profile of 25 grams of a typical (some will vary) hydrolyzed whey protein powder:
|Amino Acid Name||Amino Acid Profile|
|Total Amio Acids:||23639.25 mg (23.63925 grams)|
|Total EAA:||10753.75 mg (10.75375 grams)~ 45.5%|
|Total NEAA:||12885.5 mg (12.8855 grams)~ 54.5%|
|Total BCAA:||5125 mg (5.125 grams)~ 21.7%|
As you can see, hydrolyzed whey protein is close to 50% EAA and 50% NEAA. In order to get the amount of EAA and BCAA that we need to ensure growth, a large serving of this whey needs to be consumed. This poses a problem because consuming a large amount of protein activates the release of the hormone glucagon, which causes protein to be broken down and converted to glucose.
NEAA Are Not Needed
Research studies have shown time and time again that NEAA are not needed to stimulate protein synthesis when EAA are consumed [8, 42, 52]. A study showed that consuming NEAA did not increase protein synthesis while consuming EAA did in fact increase protein synthesis . A single six-gram serving of EAA is more than twice as effective as two, six-gram servings of mixed amino acids (EAA and NEAA) in increasing protein synthesis [1, 52]. A 200% increase in protein synthesis was observed due to EAA available after resistance exercise .
It has been shown that exercising after ingestion of an EAA drink maintained intracellular levels of NEAA. This showed that NEAA availability did not limit protein synthesis. The intracellular pool of amino acids were increased with EAA supplementation, but not with supplementation of EAA + NEAA , meaning when EAA are consumed, they go into the cells. This is in part due to EAA absorption speed.
EAA are the fastest absorbed of all amino acids . All these facts show that half of the amino acids we consume from the whey protein are needed for increased anabolic activity. All these benefits were seen just with the ingestion of 6 grams of EAA. All of this happens irrelevant of carbohydrate consumption, but when combined with the proper fuel source, you are able to train at even higher levels without risking the loss of the precious EAA.
Upregulation Of Glut-4 Receptors
In order for certain nutrients and molecules to diffuse across cellular membranes (i.e. glucose into muscle), they must be transfer by a transporter protein. We will be discussing the hexose transporters, or glucose transporters; specifically the Glut-4 transporter. In order for glucose to be metabolized, it must diffuse into a cell through a transporter. Glucose uptake in skeletal and cardiac muscle, and fat cells is regulated. Transport across the membrane into these regulated cells occurs via Glut-4 transporters.
These Glut-4 transporters have a high affinity for glucose. These Glut-4 transporters are in turn regulated by insulin. Secretion of insulin causes Glut-4 receptors to translocate from intracellular storage sites to the cell membrane, allowing glucose to enter. Insulin is not necessary for this translocation during exercise.
When a muscle contracts, calcium is released. This increase in calcium concentrations stimulates the translocation of the Glut-4 receptors, allowing glucose uptake in the absence of insulin. While the effects of insulin and exercise on Glut-4 translocation are additive, they are independent . Exercise alone can cause a 35% increase in plasma membrane Glut-4 content .
Phosphorylation of Akt, a signaling intermediate for Glut-4 translocation was shown to increase by 280% from a bout of exercise . These increases have been observed in the post exercise recovery period as well. This increase in Glut-4 content means that more glucose will be absorbed directly by the muscle, allowing for greater glycogen replenishment and recovery.
Pre-Workout Better Than Post Workout?
These results were seen when precise nutrients and environments were created post exercise. When these nutrients and environments were created pre-workout, the results were even greater! Tipton et al  found that consuming amino acids before exercise resulting in greater delivery of these amino acids than when consumed after exercise.
This greater delivery is due to increased blood flow to the working muscles. At rest, about five liters of blood are being circulated per minute, with only 15-20% going to skeletal muscle. During exercise, blood flow is increased to 20-25 liters per minute, with 80-85% of the blood going to skeletal muscle. This occurs through autoregulation. Autoregulation causes the smooth muscles surrounding the arteries to contract, which causes the arterioles to constrict. This decreases blood flow to organs that do not need it.
When the muscles become active, they need the blood the most, so it is sent to them . Due to this increased blood flow, by consuming EAA before and after your workout, there was an increase in protein synthesis for the rest of the day ! Consuming a shake pre-workout will not decrease the effectiveness of a post workout shake or retard the elevation in lipid oxidation after a workout, but rather enhance them.
Summary of Protein Synthesis Rates When Compared to Rest:
- 50% increase from hyperinsulinemia 
- 50-100% increase from resistance exercise 
- 150% increase from EAA availability 
- 200% increase from EAA availability after resistance exercise 
- 400% increase from hyperinsulinemia and amino acid availability after resistance exercise 
- >400% increase from hyperinsulinemia and amino acid availability before resistance exercise 
* In all these studies, EAA alone were used as a protein source! Smith et al demonstrated that a single dose of EAA stimulated protein synthesis, whereas NEAA had no effect !
* MAA is a protein containing both NEAA and EAA
In order to isolate the EAA, and receive the greatest benefit from them, they must be consumed in free form. Free form amino acids do not need to be digested. This means that they bypass the liver. The liver is the "gate keeper" of the body. It decides what nutrients get sent into the peripheral circulation and what nutrients get broken down and secreted or stored. When amino acids are consumed, their peptide bonds must be broken in order to be digested. When glycogen levels are low, many of the amino acids consumed end up as glucose and never make it to the peripheral blood circulation, which means they never make it to the muscle! By using free form EAA, we bypass the liver, sending the amino acids straight into the peripheral circulation. This also diminishes the need to direct blood away from the muscle to the intestines to aid in digestion. Most importantly, we increase protein synthesis!
The positive benefits of consuming EAA with gycemic carbs before, during, and after exercise are numerous! To create the most muscle growth possible, we must take advantage of these findings. Below I have outlined what I call the Anabolic Ammunition Arsenal, or A-cubed. I am not claiming to have invented this setup, as companies and other people have recommended similar setups. But I have based this setup around the research presented in the scientific studies as stated above.
*Note: Due to FDA regulations and it's sedentary effects, the EEA tryptophan should not be included in your EAA mix.
The Anabolic Ammunition Arsenal (A3)
These meals should be consumed in liquid form because solid foods take longer to digest . The preworkout and during workout shakes are of prime importance. These two meals are what insure anabolism. The post workout shake is the icing on the cake as its benefits are secondary to the two prior shakes.
Note: An auto-calculator for your bodyweight is below.
- 0.15-0.2 X bodyweight (kg) in EAA
- 0.4 X bodyweight (kg) in High Glycemic Carbs*
- 5 grams of EXTRA BCAA
- 0.15-0.2 X bodyweight (kg) in BCAA
- 0.4 X bodyweight (kg) in High Glycemic Carbs**
- 0.4 X bodyweight (kg) of Hydrolyzed Whey Protein
- 0.8 X bodyweight (kg) in High Glycemic Carbs***
- 5 grams of EXTRA BCAA
* = Preferably a combination of dextrose/maltodextrin or dextrose and sucrose
** = Preferably a combination of dextrose/maltodextrin or dextrose and sucrose
*** = Preferabley a combination of dextrose/maltodextrin
The reason for consuming the extra BCAA is as follows:
When blood levels of BCAA are high, a signal is sent to your brain that muscle is being broken down. In attempt to stop this catabolic act, the body releases insulin and reduces cortisol, thereby creating an anabolic environment ! Also a shown above, the BCAA are metabolized at an accelerated rate during exercise. I have shown that leucine is vital to protein synthesis and anabolism. Hood et al even recommended that a minimum of 45mg of leucine per kilogram of bodyweight be consumed each day . By including these extra servings of BCAA, we are also ensuring adequate leucine levels.
I suggest taking hydrolyzed whey instead of just EAA for economical reasons. Also, because we will be ingesting a large amount of carbohydrates with it, the negative effects of glucagon will be decreased.
Example For An 180 Pound Athlete
You can calculate the numbers for your weight down below.
0.15-0.2 X bodyweight (kg) in EAA= 12-16 grams
0.4 X bodyweight (kg) in High Glycemic Carbs= 33 grams
EXTRA BCAA= 5 grams
Total Grams = 50-54
0.15-0.2 X bodyweight (kg) in BCAA= 12-16 grams
0.4 X bodyweight (kg) in High Glycemic Carbs= 33 grams
Total Grams = 45-49
0.4 X bodyweight (kg) of Hydrolyzed Whey Protein= 33 grams
0.8 X bodyweight (kg) in High Glycemic Carbs= 65 grams
EXTRA BCAA= 5 grams
Total Grams = 103
Calculate Your Intake!
These liquid meals are the backbone of anabolism. In to order maximize utilization and prevent the chance of stomach distress, these drinks need to be diluted to a certain concentration. Ideally, the drink should be diluted to a solution of 4-8%. To calculate concentration, take the total number of grams in the shake and divide 10. Ten grams of total powder in one liquid is a 1% solution. Fifty grams, as seen in the example above, in one liter is a 5% solution.
One of the main benefits of this setup is you can structure your carbohydrate intake around your workout to ensure more energy for your training, while maintaining a moderate carbohydrate intake during the rest of the day. This is vital for those dieting and trying to maintain their hard earned muscle and strength, while trying to shed body fat. Bodybuilders often lose strength and muscle when dieting because their diets to not ensure proper nutrition surrounding their workouts. The meals consumed before and after a workout determine the results that will be seen.
Cost vs. Benefit
When it comes down to it, everyone is concerned with the cost of their supplements. Some are willing to pay a little extra for quality supplements, while others are not. Initially, people look at this setup and think it is not cost effective or they can get the same benefits by just taking whey protein. While whey protein is good, it should be clear that consuming free form EAA, especially BCAA, have many more advantages. Some also say that they can just increase the amount of whey protein they take to get more of the EAA and BCAA.
By doing this, you are now spending more money, which was your primary concern. In the end, one will get the most "bang for their buck" from this setup. Unlike other plans, this setup increases anabolism while decreasing catabolism. If performing at your full potential is important to you, then you will use what has been shown to work best. Why pay for something that will not deliver the best results?
Point Blank (Summary)
- Protein Turnover = Protein Synthesis - Protein Breakdown
- During a workout, glycogen is depleted and protein breakdown is increased.
- Low glycogen levels are detrimental to performance and recovery
- Cortisol is released during exercise and when glycogen levels are low; resulting in a decrease in the free pool of amino acids due to their conversion to glucose.
- EAA are extremely anabolic while the NEAA are not needed for protein synthesis.
- Consuming both EAA and glucose before and after your workout will ensure anabolism while decreasing catabolism through a variety of pathways.
Though these workout meals are liquid, during the rest of the day, one should consume high quality solid food meals or meal replacement powders when needed. This nutritional and supplement plan has been proven to increase anabolism and decrease catabolism. But, it can still be improved upon by the addition of certain supplements.
These supplements and their effects will be discussed in the future articles in this series. The next article in this series will discuss carbohydrate metabolism and its effects on exercise in more depth as well as how to manipulate other hormones in our favor, all of which will further support the outlined workout supplement protocol.
Also, check out my full bulking and cutting series where I show you my exact training, supplement and nutrition plans along with my progress pics!
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