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BCAA - Branch Chain Amino Acids

AMINO ACIDS

BCAA - Branch Chain Amino Acids - BCAA - Pro Series Aminos - Branch Chain Amino Acid Tablets. Pro Series Amino Acid Supplements. Pro Aminos for MAXIMUM MUSCLE GROWTH . BCAA Branched chain amino acids are muscle have bodybuilding essentials not just for bodybuilders but also strength & endurance athletes . Amino acids are the chemical units, or “building blocks” that make up human muscle tissue. Protein quality is measured by the amount of the specific amino’s within it. BCAA - Power Packed Amino Acid Tablets BCAA's (branched chain amino acids) L-leucine, L-isoleucine and L-valine are undoubtedly the single most important group of amino acids for athletes. Around 33% of muscle protein consists of BCAA’s. Even moderate exercise causes levels of BCAA’s to drop rapidly which results in muscle tissue breakdown (catabolism), fatigue, and a drop in testosteronelevels. Research shows that athletes who supplemented with BCAA’s during tests experienced increased muscle growth and strength, overall increases in energy, and improved muscle power output. The BEST BCAA Tablets are HARDCORE BIG RED SHARK BCAA's. These full strength tablets with an RRP of £24.99 are currently on SPECIAL OFFER!

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• Maximises Lean Muscle Growth
• Optimises post-workout recovery
• Maintenance of cells
• Maintenance of tissues
• Helps avoid muscle degeneration
  
  Amino acids are essential to the human body. Bodybuilders can especially benefit from supplementing amino acids because they aid in repair, growth, and development of muscle tissue. The body, through assimilation of amino acids, produces over 50,000 proteins and over 15,000 enzymes. Amino acids are not only responsible for the production of all the body's enzymes (including digestive enzymes), but they also play a key role in normalizing moods, concentration, aggression, attention, sleep, and sex drive. After protein is consumed, it is broken down into amino acids. Then, individual amino acids are used to create necessary body proteins and enzymes. Digestive enzymes break down the proteins a person consumes into amino acids.
  
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BCAA - Branch Chain Amino Acids

Take 2-4 Tablets per day. On Training days take 2-3 Tablets 45 minutes before training and 2-3 Tablets within 30 minutes of finishing training.

BCAA's (branched chain amino acids) - The Bodybuilding Essentials BCAA's are undoubtedly the single most important group of amino acids for athletes. Around 33% of muscle protein consists of BCAA’s. Even moderate exercise causes levels of BCAA’s to drop rapidly which results in muscle tissue breakdown (catabolism), fatigue, and a drop in testosterone levels. Research shows that athletes who supplemented with BCAA’s during tests experienced increased muscle growth and strength, overall increases in energy, and improved muscle power output.

Maximises lean muscle growth
Optimises post-workout recovery
Essential for anabolism to occur
Help muscle growth
Maintenance of cells
Maintenance of tissues
Helps avoid muscle degeneration

Amino acids are essential to the human body. Bodybuilders can especially benefit from supplementing amino acids because they aid in repair, growth, and development of muscle tissue. The body, through assimilation of amino acids, produces over 50,000 proteins and over 15,000 enzymes. Amino acids are not only responsible for the production of all the body's enzymes (including digestive enzymes), but they also play a key role in normalizing moods, concentration, aggression, attention, sleep, and sex drive. After protein is consumed, it is broken down into amino acids. Then, individual amino acids are used to create necessary body proteins and enzymes. Digestive enzymes break down the proteins a person consumes into amino acids.

There are 22 amino acids, without them, all of the metabolic processes necessary to spark and sustain human life would simply not be possible. Long chains of amino acids combine to form up to 55,000 different proteins, and each protein is used to produce the enzymes, neurotransmitters, and hormones that support normal growth and functioning of all bodily organs, including the heart, brain, liver, kidneys, and sex organs.

Amino acids come in two distinct types - essential amino acids and nonessential amino acids. Essential amino acids cannot be manufactured in the body (you get these by eating foods that contain protein), and nonessential amino acids are manufactured within the body by combining two or more essential amino acids. However, adequate amounts of dietary protein are needed to form all 22 amino acids. If you don’t get enough protein your body won’t have the 9 essential amino acids it needs to make up the other 13 nonessential amino acids. This is why we always recommend a full spectrum protein supplement to muscle building bodybuilders.

Today’s modern Western- style diet is composed largely of processed foods which often lack in quality protein, for this reason a good full strength amino acid supplement as listed above is essential for optimum performance and muscle building

What Are Branched-Chain Amino Acids?
The BCAA Are A Group Of Three Essential Amino Acids:

1. Leucine
2. Isoleucine
3. Valine

The BCAA are different from the other 17 amino acids in that they are primarily metabolized in skeletal muscle (Layman, 2003) and metabolized at a much lower rate in the liver (Norton, 2005). The rate limiting enzyme in BCAA catabolism is Branched Chain Keto Acid Dehydrogenase, which is much more active in skeletal muscle than in the liver (Norton, 2005).

Point blank, exercise promotes increased BCAA oxidation (Shirmomura et al., 2004). This increased degradation of BCAA helps maintain energy homeostasis by providing carbon as a direct energy source and glucose homeostasis by providing substrates for the citric-acid cycle and gluconeogenesis.

Amino acids are categorized as glucogenic, ketogenic, or a combination of glucogenic and ketogenic. A glucogenic amino acid when metabolized gives rise to pyruvate or other TCA cycle intermediates that can be used for the production of glucose through gluconeogenesis.

A ketogenic amino acid is metabolized via the fatty acid pathway and gives rise to actyl-CoA, a fatty acid precursor. Leucine is completely ketogenic, valine is completely glucogenic, and isoleucine is both glucogenic and ketogenic. Valine and isoleucine can both be used to produce intermediates for glucose production via gluconeogenesis.

Due to leucine's metabolic properties (discussed below), increasing attention is being given to it and its metabolism. Research has shown plasma leucine levels to decrease during both aerobic and anaerobic exercise (Mero, 1999).

According to Freund and Hanani (2002), "Complete oxidation of leucine in the muscle yields more adenosine triphosphate molecules on a molar basis than complete oxidation of glucose." So leucine can provide skeletal muscle with more ATP than an equal amount of glucose, which is due to leucine being completely ketogenic and metabolized via the fatty acid pathway.

In order to meet the increased demand for BCAA during exercise the body breaks down muscle tissue to supply additional BCAA. By supplying the body exogenous BCAA during exercise, one can  meet the increased demand for BCAA oxidation without breaking down muscle tissue to supply the needed BCAA.

Because BCAA serve as a "fuel" for skeletal muscle, supplementing with additional BCAA during your workout improves your performance without the added calories or insulin spike (which can lead to fat storage) caused by carbohydrates.

Leucine Stimulates Leptin Expression through mTOR activation in Adipocytes

Intake of leucine stimulates expression of the hormone leptin in adipocytes (the primary site of leptin secretion) through activation of the mTOR pathway (Meijer and Dubbelhuis, 2003). Leptin is a very complicated hormone; the gist of it is involved in the regulation of metabolism, body weight, and appetite.

Leptin secretion is linked with body fat levels; higher body fat is associated with higher leptin secretion and lower body fat is associated with lower leptin levels. When you diet and lose fat, the amount of leptin you secrete decreases, which makes your body "crave" food in an attempt to bring your body fat level back up to where the body is comfortable (known as the body fat "set point").

Leucine has the ability to activate leptin expression and will cause the body to think it is "fed" or receiving "adequate" calories, which will keep things running (specifically your metabolism) smoothly.

BCAA and the Glucose-Alanine Cycle

The BCAA's are involved in maintaining glucose homeostasis through the glucose-alanine cycle (see figure 1). The glucose-alanine cycle involves pyruvate (derived from glucose/glycogen) being transaminated in muscle to form alanine, with the BCAA serving as the main nitrogen source (donors) for the synthesis of alanine (Holecek, 2002).

The newly synthesized alanine is released in the blood stream and sent to the liver where it is converted into glucose through gluconeogenesis. This glucose can then be sent from the liver back to the working muscle to be used as fuel. Supplementing with BCAA allowing your body to create glucose to use for fuel without the added calories or insulin spike (which can lead to fat storage) caused by carbohydrates.

L-Glutamine

Glutamine is a glucogenic (glucose creating), nonessential amino acid that has multiple roles in the body. Glutamine is synthesized mainly in skeletal muscle and the liver and acts as a "nitrogen shuttle" between organs, a fuel for cells of the immune system and intestines, and a precursor for nucleotide synthesis (Holecek, 2002).

Glutamine is also a powerful cell volumizer (Haussinger et al. 1993). An increase in cell volume, also called cell swelling, stimulates anabolic pathways (synthesis of proteins and glycogen) and inhibits catabolic pathways (protein degradation) (Haussinger, 1993).

According to Houston (2001), "Glutamine content in skeletal muscle and other tissues appears to have a regulatory role in whole body protein synthesis." Glutamine levels inside muscle govern protein synthesis and nitrogen balance and therefore muscle growth (VanAcker et al. 1999).

Adequate glutamine concentrations are needed for optimal health and skeletal muscle hypertrophy. Therefore one would want to keep glutamine levels elevated, especially during/post exercise.

Glutamine Metabolism and Exercise

During times of stress, such as exercise, skeletal muscle glutamine levels are depleted. This glutamine released from skeletal muscle is derived from muscle proteins, the intramuscular free amino acid pool, and newly synthesized glutamine (VanAcker, 1999). The newly synthesized glutamine is created by using BCAAs obtained from muscle protein breakdown (Holecek, 2002).

Plasma and muscle glutamine levels are decreased post workout and it can take hours before they are restored (Rowbottom, 1996). A study examining the effect of free-form glutamine and glutamine peptide ingestion on muscle glycogen resynthesis found that plasma glutamine was decreased by 20% post workout with the ingestion of glucose only (control), showed no change with ingestion of whey protein or wheat protein hydrolysate plus glucose drinks, and a 200% increase with ingestion of free-form glutamine plus glucose drink (VanHall, 2000). Free-form glutamine supplementation was needed to elevate plasma glutamine levels post workout.

In addition to restoring and elevating plasma glutamine levels, oral glutamine supplementation increases muscle glycogen storage to the same capacity as glucose (Bowtell, 1999). Glutamine can replenish glycogen levels without the added calories or insulin spike (which can lead to fat storage) caused by carbohydrates.

Mammalian Target of Rapamycin (mTOR)

The Mammalian Target of Rapamycin (mTOR) is one of the body's protein synthesis regulators. mTOR functions as an energy sensor; it is activated when ATP levels are high and blocked when ATP levels are decreased (AMPK is activated when ATP decreases, which works antagonistically to mTOR).

The main energy-consuming process in the cell is protein synthesis. When mTOR is activated (high ATP levels sensed) protein synthesis is increased and when mTOR is suppressed (low ATP levels are sensed) protein synthesis is blunted.

MTOR activation is vital for skeletal muscle hypertrophy. Interestingly, mTOR is also a nutrient sensor of amino acid availability, specifically of leucine availability. Research has shown that regulation of mTOR by ATP and amino acids act independently through separate mechanisms (Dennis et al., 2001).

Research:

1. Biolo, G., B. D. Williams, R. Y. Fleming, and R. R. Wolfe. Insulin action on muscle protein kinetics and amino acid transport during recovery after resistance exercise. Diabetes 48: 949-957, 1999.
2. Borsheim, E., K. D. Tipton, S. E. Wolf, and R. R. Wolfe. Essential amino acids and muscle protein recovery from resistance exercise. Am.J.Physiol Endocrinol.Metab 283: E648-E657, 2002.
3. Levenhagen, D. K., J. D. Gresham, M. G. Carlson, D. J. Maron, M. J. Borel, and P. J. Flakoll. Postexercise nutrient intake timing in humans is critical to recovery of leg glucose and protein homeostasis. Am.J.Physiol Endocrinol.Metab 280: E982-E993, 2001.
4. Rasmussen, B. B., K. D. Tipton, S. L. Miller, S. E. Wolf, and R. R. Wolfe. An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise. J.Appl.Physiol 88: 386-392, 2000.
5. Roy, B. D. and M. A. Tarnopolsky. Influence of differing macronutrient intakes on muscle glycogen resynthesis after resistance exercise. J.Appl.Physiol 84: 890-896, 1998.
6. Tipton, K. D., A. A. Ferrando, S. M. Phillips, D. Doyle, Jr., and R. R. Wolfe. Postexercise net protein synthesis in human muscle from orally administered amino acids. Am.J.Physiol 276: E628-E634, 1999.
7. Tipton, K. D., B. B. Rasmussen, S. L. Miller, S. E. Wolf, S. K. Owens-Stovall, B. E. Petrini, and R. R. Wolfe. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. Am.J.Physiol Endocrinol.Metab 281: E197-E206, 2001.
8. Tipton, K. D., E. Borsheim, S. E. Wolf, A. P. Sanford, and R. R. Wolfe. Acute response of net muscle protein balance reflects 24-h balance after exercise and amino acid ingestion. Am.J.Physiol Endocrinol.Metab 284: E76-E89, 2003..

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