There are 20 types of amino acids that make up muscle protein, but these are considered essential amino acids (EAA) and should be supplemented through a balanced diet. Skin proteins are in a state of constant renewal and protein synthesis. In other words, when the protein is degraded by the substitute, a constant amount of protein is lost.
You need enough energy to synthesize new muscle protein, all EAA, and 11 non-essential amino acids (NEAA) that your body can produce. Branched chain amino acids, leucine, valine and isoleucine are three of the nine EAAs. Leucine is not only the precursor of muscle protein synthesis, but also has the concept of surpassing BCAA's unique ability to stimulate muscle protein synthesis in the process of protein synthesis.
The pathway involves three 10-year-old intracellular signal regulators. The data supporting this hypothesis comes from a study of rat responses. It was reported in 1981 that the synthesis of rat muscle protein may determine the rate. Other studies support the view that branched-chain amino acids have a unique effect on muscle protein synthesis in rats, but some studies only study the response of oral branched-chain amino acids.
Studies by Kari Katsura (Garlic) and Grant (Grant) have shown that injecting a mixture of branched chain amino acids into rats may increase the effect of insulin on muscle protein synthesis. Measuring the effect of branched chain amino acids has not been completed. Injection of branched-chain amino acids into rats alone is short-lived, although it can induce an increase in muscle protein synthesis. Perhaps due to its high synthesis rate, it is limited to the availability of other EAAs. The study of rat muscle protein synthesis has limited relevance to human response. Compared with humans, skeletal muscle accounts for a much smaller proportion of the total weight of rats, and there are many ways to regulate muscle protein synthesis.
Therefore, in the original study of protein metabolism by Waterlow et al., they concluded from existing data that dietary amino acids do not stimulate the synthesis of muscle protein in rats. Recent studies disagree with this statement, but the limited stimulation of dietary amino acids on protein synthesis in rats is usually synthesized under conditions after absorption to enhance intracellular activity. This reflects the ability to use endogenous amino acids to increase excess protein. Due to the difference in expression, the synthesis of rat muscle protein is obviously limited by the transformation process, not the first process. On the other hand, as we will see later, this does not seem to exist in humans. Another important difference in studying the effects of amino acids on human and rat muscle protein synthesis is related to common methods. The "overflow dose" technique is often used in rat research. This process measures the amount of muscle protein your amino acid tracer consumes in a short period of time (usually 10 minutes). This method cannot distinguish between transient and continuous stimulation of protein synthesis.