KIC is clearly the most important BCKA and some feel there’s every reason to believe that KIC will prove to be of value to serious athletes, including bodybuilders.

Maximum Human Performance (MHP) was born out of a friendship between a world-class bodybuilder Gerard Dente and Vincent Giampapa, MD, a specialist in hormone replacement therapy and age management medicine. Although MHP is a relatively fresh player in the field of sports supplements, they have produced some innovative products for serious athletes. In this article, I will discuss their latest product, A-Bomb.

A-Bomb

MHP feels that A-Bomb triggers muscle-building machinery from multiple pathways and synergistic anabolic actions. A-Bomb’s ingredients work through nonhormonal signal transduction by manipulating the key muscle growth regulators mTOR, PKB, p70s6k, 4E-BP1, FOXO and MAFbx. A-Bomb affects these processes through two pathways. The first pathway is the nutrient dependent pathway, where A-Bomb uses specific amino acids and other nutrients. The second pathway is the insulin dependent pathway, where A-Bomb has the ability to increase the secretion of insulin without raising blood sugar. Let’s examine some science behind A-Bomb’s main actives.

Branched-chain Amino Acids
The branched-chain amino acids (BCAAs) leucine, isoleucine and valine are so named because they have a carbon chain, which deviates or branches from the main linear carbon backbone. They are unusual in that they are catabolized mainly in skeletal muscle. There’s evidence that BCAA supplementation before exercise decreases the breakdown of muscle proteins during exercise in humans and that leucine strongly promotes protein anabolism in skeletal muscle. Furthermore, it’s been reported that BCAA supplementation prior to resistance training decreased delayed onset muscle soreness and muscle fatigue occurring for a few days after exercise, suggesting BCAA supplementation may be useful for muscle recovery following exercise. Finally, there’s some evidence suggesting that BCAA supplementation may delay central fatigue during prolonged exercise.

The key BCAA leucine acts as a nutrient signal to stimulate muscle protein anabolism. Leucine affects muscle protein metabolism by decreasing the rate of protein degradation, most likely via increases in circulating insulin. In addition, leucine activates key molecules involved in the regulation of protein synthesis, which has been shown to occur even in the absence of an increase in circulating insulin concentrations. Simply put, insulin and leucine allow skeletal muscle to coordinate protein synthesis with physiological state and dietary intake.

Ketoisocaproic Acid
Ketoisocaproic acid (KIC) is a keto acid of leucine. Branched-chain keto acids (BCKAs) are very similar to branched-chain amino acids (BCAAs). In fact, the only difference is the presence of a keto group instead of an amino group. Thus, BCKAs can be viewed as ammonia-free sources of BCAAs. KIC is clearly the most important BCKA and some feel there’s every reason to believe that KIC will prove to be of value to serious athletes, including bodybuilders.

Although leucine can be converted to KIC (transamination) and both tend to increase parallel in the blood when leucine is used, there’s evidence that it has anti-catabolic (protein-sparing) properties separate from leucine. A 1984 rat study, published in Biochemical Journal, reported that leucine stimulated protein synthesis, but didn’t reduce protein degradation when leucine transamination was inhibited. So, the anti-catabolic effects of leucine, in contrast to its anabolic effects, required its transamination.

This study appears to confirm the results obtained from an earlier study that concluded KIC has anti-catabolic, but not anabolic, effects. That is, KIC reduced muscle protein degradation, but didn’t stimulate protein synthesis. Also, supplements containing KIC in relatively high doses have been shown to decrease the rate of 3-methylhistidine excretion by patients with Duchenne muscular dystrophy. Scientists use 3-methylhistidine as an indicator of contractile muscle degradation.

Finally, KIC may also increase anabolic drive via stimulation of insulin secretion. Both leucine and KIC have been shown to stimulate insulin secretion. Insulin increases transport of amino acids into the cells and thus, has both anabolic and anti-catabolic effects.

Beta-hydroxy-beta-methylbutyrate
Beta-hydroxy-beta-methylbutyrate (HMB) is derived from the amino acid leucine and its keto acid, alpha-ketoisocaproate (KIC). There’s evidence that HMB supplementation may play an important role in reducing muscle protein breakdown and/or increasing recovery of damaged muscle cells. I won’t review all the individual studies. Rather, I’ll focus on recent meta-analysis (i.e., quantitative statistical analysis applied to separate, but similar, experiments) published in the Journal of Applied Physiology (JAP) few years ago.

The purpose of this JAP meta-analysis was to quantify what dietary supplements augment lean mass and strength gains during resistance training. The investigators included peer-reviewed studies between the years 1967 and 2001 if they met a predetermined set of experimental criteria. A total of nine HMB studies qualified for analysis. All of them involved supplementation of HMB at 3 grams per day and resulted in a net increase in lean mass gain of 0.28 percent per week. Concerning the strength gains, HMB caused a net increase of 1.40 percent per week.

Other Ingredients

A-Bomb also contains alpha-ketoglutarate (AKG), alanine, N-(aminoiminomethyl)-N-methyl glycine and phenylalanine, as well as some DNA remodeling agents (e.g., Uncaria tomentosa).

The author of this article has no financial relationship with MHP. This article does not constitute or imply endorsement of any MHP product.

References:
1. Shimomura Y, Yamamoto Y, Bajotto G et al. Nutraceutical effects of branched-chain amino acids on skeletal muscle. J Nutr, 2006;136:529S-532S.
2. Manninen AH. Hyperinsulinaemia, hyperaminoacidaemia and post-exercise muscle anabolism: the search for the optimal recovery drink. Br J Sports Med, 2006;40:900-5.
3. Nair KS, Schwartz RG, and Welle S. Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. Am J Physiol Endocrinol Metab, 1992; 263:E928934.
4. Karlsson HK, Nilsson PA, Nilsson J, Chibalin AV, Zierath JR, Blomstrand E. Branched-chain amino acids increase p70S6K phosphorylation in human skeletal muscle after resistance exercise. Am J Physiol Endocrinol Metab, 2004;287: E17.
5. Norton LE, Layman DK. Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. J Nutr, 2006;136:533S-537S.
6. Crowe MJ, Weatherson JN, Bowdeen BF. Effects of dietary leucine supplementation on exercise performance. Eur J Appl Physiol, 2005;29:1-9.
7. Pasquale MG. Amino Acids and Proteins for the Athlete-The Anabolic Edge, Boca Raton, FL: CRC Press, 1997.
8. Blomstrand E, Eliasson J, Karlsson HK, Kohnke R. Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. J Nutr, 2006;136:269S-73S.
9. Garlick PJ. The role of leucine in the regulation of protein metabolism. J Nutr, 2005;135:1553S-6S.
10. Nissen SL, Sharp RL. Effect of dietary supplements on lean mass and strength gains with resistance exercise: a meta-analysis. J Appl Physiol, 2003;94:651-9.