F1000Prime Recommended Article: Reevaluation of the protein requirement in young men with the indicator amino acid oxidation technique.

The indicator amino acid oxidation (IAAO) method is based on the concept that when 1 indispensable amino acid (IDAA) is deficient for protein synthesis, then all other IDAA, including the indicator amino acid, will be oxidized. With increasing intakes of the limiting amino acid, IAAO will decrease, reflecting increasing incorporation into protein. Once the requirement for the limiting amino acid is met, there will be no further change in the indicator oxidation. Originally, the IAAO method was designed to determine amino acid requirements in growing pigs. The minimally invasive IAAO method developed in humans has been systematically applied to determine IDAA requirements in adults. Due to its noninvasive nature, the IAAO method has also been used to determine requirements for amino acids in neonates and children, and in disease. The IAAO model has recently been applied to determine the metabolic availability (MA) of amino acids from dietary proteins and to determine total protein requirements. The IAAO method is robust, rapid, and reliable; it has been used to determine amino acid requirements in different species, across the life cycle, and in diseased populations. The recent application of IAAO to determine MA of amino acids and protein requirements is also very novel.

Protein forms an essential component of a healthy diet in humans to support both growth and maintenance. During pregnancy, an exceptional stage of li

Methionine is a nutritionally indispensable amino acid, and is unique among indispensable amino acids due to its sulfur atom. Methionine is involved in cysteine synthesis via the transsulfuration pathway, which is rate limiting for the key antioxidant molecule, glutathione. Methionine is also the primary methyl donor in the body through S-adenosylmethionine via the transmethylation pathway, which is involved in the synthesis of several key metabolites including creatine and phosphatidylcholine. Methionine can also be remethylated from homocysteine, in the presence of betaine via choline and/or folate. Thus methionine demands from a dietary perspective are regulated not only by the presence of cysteine in the body, but also by the demands in vivo for the various metabolites formed from it, and also by the presence of these compounds in foods. Indeed, methionine, cysteine, and the various methyl donors/acceptors vary in human foods, and thus regulate methionine availability, especially under conditions of growth and development. Much of our understanding of methionine nutrition and metabolism arises from experiments in animal models. This is because most animal feed formulations are plant-based and plant sources are relatively low in methionine and cysteine amounts. Thus, this brief review will touch on some broad aspects of human methionine nutrition, including requirements in different life stages, disease, and bioavailability, with some examples from the insights/lessons learned from experiments initially conducted in animals.