All About Muscle Anabolism Stimulation

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Anabolism and Catabolism may sound like superheroes from the favorite television show of a kid but these complex functions are described by doctors, health coaches, dietitians, and bodybuilders as ways to create diet and workout plans to influence metabolism and overall health.

In human beings, aging is usually associated with sarcopenia or the loss of lean muscle mass. The intake of food, especially the ingestion of amino acids or protein, is known to be a powerful stimulus to improve net muscle protein anabolism. However, this may get affected in growing men.

What Is Anabolism?

Anabolism can be defined as the mechanism that takes into account smaller units such as cells, amino acids, or nutrients and bind them together with a purpose of creating bigger structures. For instance, the human body adds structures and tissues around a wound when the body is trying to heal a cut.

How Do Hormones Affect Anabolism?

Acting as messengers, hormones communicate what functions to perform to your body. Hormones trigger catabolism (a mechanism breaking down muscle and fat for energy) and anabolism. While catabolic hormones (such as adrenaline, cytokines, cortisol, and glucagon) usually get activated under stress, anabolic hormones (estrogen, insulin, testosterone, and human growth hormone) are responsible for tissue growth and repair.

Can I Control My Metabolism?

Metabolism is directly affected by a lot of factors, including but not limited to age, genetics, and gender. However, you can positively influence hormones playing crucial roles in catabolism and anabolism by following certain healthy habits:

• Avoiding processed foods
• Identifying healthy ways to relieve stress
• Consuming high-quality fats, carbohydrates, and proteins
• Having a sound sleep of at least 7 hours every night
• Limiting the intake of nicotine and alcohol
• Avoiding substance use/abuse
• Consuming 10-14 glasses of water every day to stay hydrated
• Engaging in regular exercise and workouts

How Does Food Affect Anabolism?

Anabolism functions properly only when the body is deriving sufficient nutrients from foods such as fruits, lean meats, and vegetables. In fact, the human body requires high-quality building blocks to grow, repair, and heal.

Anabolic exercises include weight-bearing exercises such as pushups, squats, and weightlifting. Very little oxygen and little energy use are required to perform these activities though it may appear that the performance of these activities consume a lot of energy and oxygen. Anabolic exercises result in tiny tears in muscle fibers and the body expends more energy later to repair, heal, and strengthen the tissue. On the other hand, catabolic exercises such as swimming, cycling, and running demand more energy and oxygen use and lead to burning of fat and glucose during the activities.

How Muscle Anabolism Stimulation Gets Triggered?

According to a study, muscle anabolism stimulation is triggered by resistance exercise and leucine supplementation. A different study determined that the intake of free amino acids after a bout of resistance exercise stimulates net muscle protein synthesis. The study concluded that arterial amino acid concentrations were elevated by the ingestion of protein when volunteers consumed whey protein supplements and casein. It was also disclosed that the ingestion of both casein and whey protein stimulated a significantly larger uptake of net phenylalanine after resistance exercise, compared with the placebo. In short, it was revealed that the acute ingestion of both whey protein and casein after exercise leads to similar improvements in muscle protein net balance. This, in turn, resulted in net muscle protein synthesis irrespective of different patterns of blood amino acid responses.

According to a double-blind, randomized trial, myofibrillar protein synthesis in young men is enhanced by leucine supplementation of a low-protein mixed macronutrient beverage just like with a high-protein dose. A different study disclosed that integrative myofibrillar protein synthesis in free-living older men consuming lower- and higher-protein diets is enhanced by leucine supplementation. This study concluded that integrated myofibrillar protein synthesis (MyoPS) in free-living older men in rested and resistance exercise (REX) is equally effective in older men consuming daily protein intakes greater than or equal to the recommended daily allowance (RDA), thanks to Leucine co-ingestion with daily meals.

Other studies in the past have also revealed that leucine supplementation is critical for exercise-induced muscle hypertrophy. Moreover, the increased availability of amino acids from the ingestion of protein and amino acids leads to positive net muscle protein balance and increased muscle protein synthesis following exercise. In recent times, the impact of leucine on muscle protein anabolism or muscle anabolism stimulation following exercise begun to be investigated.

Studies in the past have also demonstrated that the absence of an enhanced anabolic response to leucine despite any likely increase in translation signaling is primarily because of the impact of high leucine levels on blood amino acids. It is important to note here that increased leucine levels reduce the availability of other amino acids in humans and other subjects. The extra leucine impacts the other branched-chain amino acids to a great extent, primarily because of the increased oxidation of branched-chain keto acid dehydrogenase activity and, therefore, increased oxidation.

A different study observing whether resistance exercise training (RET) improves muscle sensitivity to essential amino acids (EAAs) and if muscle protein anabolism is resistant in healthy older adults disclosed RET increased lean mass by 2%, muscle strength by 16%, basal MPS by 36%, and muscle cross-sectional area by 27% in healthy older adults. After the ingestion of EAAs pre- and post-training, muscle protein synthesis (MPS) and mTORC1 signaling (i.e., phosphorylation status of protein kinase B, 4E binding protein 1, 70-kDa S6 protein kinase, and ribosomal protein S6) increased.

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