Muscle Gains: The Bigger Picture

It has to be one of the most frustrating things an aspiring athlete can experience — the inability to build muscle or losing some of the muscles so assiduously gained despite training diligently and eating correctly.

Barring the obvious impact that an illness or serious injury can have, the major reason why we fail to make progress related to a phenomenon known as catabolism. The opposite of anabolism, which is the process of building tissue, catabolism is the process of tissue breakdown.


Altering the Anabolic and Catabolic Balance

It is our evolutionary misfortune that the human body is better at catabolic activities than anabolic ones. This is because catabolism is a survival mechanism — it provides energy while we exercise and is essential for the regulation of amino acid levels in plasma. What this means is that for every ounce of muscle you put on, your body is doing its dandiest to help take it to fright back off. Worse still, the harder you train, the more catabolic you become.

Elite endurance athletes, particularly cyclists, mountain bikers, marathon runners and triathletes, are all poster children for catabolism. Why is this so? Due to the extended duration of their training and racing, they are always operating at a net deficit in which the small amount of anabolism that they might induce is totally outweighed by the muscle breakdown their training causes.

Luckily, if you are more concerned with looking good and adding some muscle than you are with setting a new course record at the Ironman championships, there is a lot that you can do to push the anabolic and catabolic balance in your body toward anabolism.

Beyond the obvious influences of proper nutrition and the intake of sufficient calories, as well as an intelligently designed training program, there are a number of nutritional compounds that can put you into a much more anabolic state. Let us take a look at some of the ingredients that can make a difference between meagre gains and massive muscles.


Branched-Chain Amino Acid

During exercise, one of the major events that cause catabolism to occur is a drop in key plasma amino acids. Of particular importance are the amino acids leucine, isoleucine and valine, also called the branched-chain amino acids, or BCAAs.

Research shows that of all the amino acids your body utilises during muscular exercises, leucine is at the top of the list. Unfortunately, leucine is also one of the most prevalent and available amino acids in muscle tissues, so when your plasma leucine levels drop, your body begins to take apart muscle tissue to get at the needed leucine. In a study published in the American Journal of Physiology, researchers gave subjects 77 mg of BCAAs per kilogram of body weight and had them perform an hour of high-intensity exercise. Results demonstrated that the breakdown of muscle protein was suppressed during exercise by the BCAA supplementation.

Leucine seems to be less anti-catabolic and more anabolic when taken by itself — at least according to a study that found oral leucine supplementation to effectively induce recovery of muscle protein synthesis after exercise. From the study, the best BCAA strategy appears to be large, single doses are taken 30 to 60 minutes prior to exercise. Nearly all BCAA products on the market use a leucine/isoleucine/valine ratio similar to that found in human muscle tissue, which is also the ration used in the research.



HMB (beta-hydroxy-beta-methyl butyrate) is a metabolite of the amino acid leucine. After you eat a protein source containing leucine, it can be broken down first into ketosis caproate and then to HMB within your muscle tissue. Your body produces about 0.3 to 1 gm of HMB every day, depending on your total daily protein — more specifically, leucine — intake. Researchers speculate that HMB exerts some sort of signal preventing protein catabolism. The rise in the concentration of HMB within the muscle may act as a signal that protein is abundant and there is no need to further break down protein within the muscle to meet the needs of the body.

In human studies, HMB has shown promise as an anti-catabolic when used at the initiation of an unaccustomed resistance exercise program.



Phosphatidylserine (PS), which is now derived mainly from soy, may blunt the exercise-induced secretion of adrenocorticotropic hormone (ACTH), which is the hormone that triggers the secretion of the most catabolic hormone in the body — cortisol.

A number of studies have been conducted using either chronic or acute administration of PS in exercising human models. In every case, researchers found that PS administration reduced ACTH response during exercise. Further, a study in Biology of Sport found that the other indices of catabolism, such as soreness, chronic fatigue and even depression, were attenuated in the PS groups in comparison to the controls. Dosages for the oral administration were in the vicinity of 800 mg per day for 10 days, though perhaps the best strategy with PS is to follow a loading and maintenance routine similar to that of creatine.