• Leucine (branched chain amino acid) used as a source of energy
• Helps reduce muscle protein breakdown
• Modulates uptake of neurotransmitter precursors by the brain as well as the release of enkephalins, which inhibit the passage
of pain signals into the nervous system
• Promotes healing of skin and broken bones
• Isoleucine (branched chain amino acid) readily taken up and used for energy by muscle tissue
• Used to prevent muscle wasting in debilitated individuals
• Essential in the formation of hemoglobin
• Valine (branched chain amino acid) is not processed by the liver, rather actively taken up by the muscle
• Influences brain uptake of other neurotransmitter precursors (tryptophan, phenylalanine and tyrosine)
WHAT ARE BCAAs :
The combination of these three essential amino acids make up approximately 1/3 of skeletal muscle in the human body, and play an
important role in protein synthesis. BCAAs make up 40% of the free amino acids in food. Dietary requirements for the three BCAAs
amount to about 35% of the total requirements of essential amino acids.
WHAT DOES IT DO :
BCAAS are both anabolic and anti-catabolic because of their ability to significantly increase protein synthesis, facilitate the
release of hormones such as growth hormone (GH), IGF-1 and insulin, and help maintain a favorable Testosterone to Cortisol ratio.
BCAAs are reported to limit protein degradation and loss of muscle mass, spare lean body mass during weight loss, and promote tissue
health and muscle protein synthesis, and growth process (anabolism). BCAAs alone may provide a distinct advantage because they
contribute minimal calories and neither stimulate sugar (glucose) biosynthesis in the body cells nor contribute excess nitrogen for
clearance by the kidneys, which can be expected with other amino acids or following a high protein diet. During times of low caloric
intake (pre-contest diets), the use of BCAAs is strongly recommended because there is a greater risk of muscle loss due to a decrease
in the rate of protein synthesis and an increase in proteolysis, which is the hydrolytic breakdown of proteins into simpler, soluble
substances such as peptides and amino acids, as occurs during digestion.
WHY COMBINE L-LEUCINE, L-ISOLEUCINE AND L-VALINE?
As the strongest of the BCAAs, L-Leucine is what's known as a "limiting nutrient", you must have enough L-Leucine in proportion to
other amino acids in order for your body to make use of what you eat. If you suffer from L-Leucine deficiency, your body will not be
able to make use of the protein that you give it, no matter how much protein you consume. And, unless you have enough L-Leucine the
money you spend on quality food and dietary supplements will be wasted. Only an individual deficient in protein would become deficient
in BCAAs, because most food sources of protein supply BCAAs.
Although it is clear that L-Leucine is the most important of the BCAAs in stimulating protein synthesis, L-Leucine supplementation
alone is not recommended. This is because this can cause an amino acid imbalance, and although the other two BCAAs are less important,
inhibiting them by increasing L-Leucine intake may have negative consequences. Research has shown that increasing dietary leucine or administration of
leucine alone lead to decreases in valine and isoleucine plasma concentrations and a BCAA imbalance (Shirmomura et al., 2004), and keeping a dietary balance
of BCAAs is particularly important when compared to other amino acids.
Ingestion of supplemental free-form glutamine or glutamine peptides is oxidized by the intestinal tract or taken up by the liver and kidney, all of which
is beneficial but supplementing with BCAA can cause de novo synthesis of glutamine inside skeletal muscle (Houston, 2001).
REFERENCES :
1. Blomstrand E,Eliasson J, Karlsson H K R and Kohnke R (2006).
"Branched-Chain Amino Acids Activate Key Enzymes in Protein Synthesis after Physical Exercise". American Society for Nutrition J. Nutr. 136:269S-273S, January 2006.
2. Rutten E PA, Engelen M PKJ, Wouters E FM, Schols A MWJ and Deutz N EP (2006).
"Metabolic effects of glutamine and glutamate ingestion in healthy subjects and in persons with chronic obstructive pulmonary disease ". American Journal of Clinical Nutrition, Vol. 83, No. 1, 115-123.
3. Holecek M (2002).
"Relation between glutamine, branched-chain amino acids, and protein metabolism". Nutrition. 2002 Feb;18(2):130-133.
HEALTH PRECAUTIONS :
Courtesan Girls BCAAs may support muscle nutrition when combined with a sensible diet, physical training or an exercise program.
BCAAs are not a sole source of nutrition and should be consumed with a nutritious diet and adequate fluid intake.
Before consuming seek advice from a health care practitioner if you are unaware of your current health condition of have any
pre-existing medical conditions. This information is not intended to diagnose, treat, cure of prevent any disease.
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