View clinical trials related to Muscle Protein Synthesis.
Filter by:To measure the absorption kinetics and postprandial amino acid availability after ingestion of minced beef compared with hydrolyzed beef in young males. Moreover, the basal muscle protein synthesis and the postprandial muscle protein synthetic response to minced beef and hydrolyzed beef ingestion are measured in young males. The postprandial muscle protein synthetic response is measured and compared during the early postprandial period (0-3 hours) after ingestion of the two meat products.
This study investigates whether a protein-nutrition beverage can increase muscle protein synthesis to a similar magnitude as a control beverage.
Muscle mass is normally maintained through the regulated balance between the processes of protein synthesis (i.e. making new muscle proteins) and protein breakdown (breaking down old muscle proteins). Proteins are composed of amino acids and we know that amino acids increase muscle protein synthesis. However, not all amino acids are the same. Essential amino acids are ones that must be consumed through food, while non-essential amino acids can be made by our body. Interestingly, the essential amino acids are all that are required to increase the rate of muscle protein synthesis. In addition, the essential amino acid leucine appears to be particularly important in regulating protein synthesis. However, how leucine is able to increase protein synthesis is not entirely understood. Previously, it has been shown that 20-25 g of high-quality protein, such as that found in milk (whey), appears to be the amount of protein that maximizes the rate of muscle protein synthesis after performing a bout of resistance exercise. Thus, we aim to measure the synthesis of new muscle proteins after ingesting different amounts of protein and amino acids. We will measure muscle protein synthesis after consumption of the beverage a participant is randomized to in a leg that has done no exercise ( ie. a rested leg) and in the other leg that has done resistance exercise. Amino acids are 'strung-together' to make protein. The 'essential' amino acids must be consumed through food because our body cannot make them, thus they are consumed when you eat protein rich foods like milk or chicken. Leucine, isoleucine, and valine are simply 3 of the 8 essential amino acids that make up dietary protein. Unlike essential amino acids, 'non-essential' amino acids may be synthesized by the body, however they are also present in protein rich foods like chicken or milk. We aim to determine if it is the leucine content found in 25 g of whey protein that is primarily responsible for maximizing muscle protein synthesis at rest and following resistance exercise. We also wish to determine how muscle genes and metabolism respond to this protocol.
A diet rich in leafy green vegetables has been shown to reduce the risk of developing chronic metabolic disease. The health benefits from these particular vegetables may be attributed to their high nitrate content. Recent work suggests that dietary nitrate triggers endogenous nitric oxide release, thereby stimulating vasodilation and improving muscle perfusion in an insulin-independent manner. We hypothesize that in an insulin-resistant state, nitrate co-ingestion will increase muscle perfusion, thereby improving post-prandial delivery of nutrients to skeletal muscle tissue. Specifically, a more efficient delivery of food derived amino acids will stimulate post-prandial muscle protein synthesis and, as such, compensate for a blunted muscle protein synthetic response to food intake in the elderly. This proposal will investigate the efficacy of nitrate co-ingestion as a means to augment muscle protein synthesis in elderly, type 2 diabetes patients and may lead to a novel therapy in the clinical care of type 2 diabetes patients.
This study examines the muscle protein signalling response after resistance and endurance exercise. We hypothesize that the signalling response after endurance and resistance exercise will be partly similar.