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Nutrition and Metabolic Factors
Published in Michael H. Stone, Timothy J. Suchomel, W. Guy Hornsby, John P. Wagle, Aaron J. Cunanan, Strength and Conditioning in Sports, 2023
Michael H. Stone, Timothy J. Suchomel, W. Guy Hornsby, John P. Wagle, Aaron J. Cunanan
The biological value (BV) of a protein is a measure of the absorption and utilization of a protein. If the BV of a protein is higher, more nitrogen is absorbed, used, and retained, making proteins with higher BV those that can better promote greater levels of tissue remodeling and muscle gains. Protein synthesis (anabolism) in humans requires approximately 22 distinct amino acids, nine of which are classified as essential amino acids (EAA) in adults. Essential amino acids are defined as those that cannot be synthesized within the human body and must instead be consumed within an individual’s diet (Table 4.3). In contrast, nonessential amino acids can be synthesized from other substances, such as carbohydrate, assuming an adequate nitrogen source (such as other amino acids) has been made available. Regarding various food sources that supply EAA, some dietary proteins have been classified as either complete or incomplete proteins. Complete proteins are those that contain all the EAA needed for the synthesis of human tissue and have a high BV. Many of these proteins are typically found in animal sources and products such as red meat, dairy products, eggs, fish, and fowl. In contrast, incomplete proteins are those that contain very low amounts of one or more EAA. These proteins generally originate from plant sources and include nuts, grains, legumes, and seeds. However, it should be noted that the quantity of protein available in some plant sources (e.g., beans) is relatively high and may partially offset the lower BV that is typical of incomplete proteins.
Flaxseed, a Functional Food—Constituents and Their Health Benefits
Published in Robert Fried, Richard M. Carlton, Flaxseed, 2023
Robert Fried, Richard M. Carlton
Amino acids are classified into three groups: Essential amino acids cannot be made by the body, and so they must come from food. There are nine essential amino acids: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine.Nonessential amino acids can be produced by the body. These are alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, pro-line, serine and tyrosine.Conditional amino acids are usually not essential, except in times of illness and stress. These are arginine, cysteine, glutamine, tyrosine, glycine, ornithine, proline and serine. One does not need essential and nonessential amino acids at every meal, but getting a balance of them over the whole day is important. (3) Flax protein is not considered to be a complete protein due to the presence of the limiting amino acid lysine.
Nutritional requirements
Published in Judy More, Infant, Child and Adolescent Nutrition, 2021
Proteins are needed for building and maintaining all the cells in the body. During growth, vast numbers of new cells are created and extra protein is needed for this. Protein is made up of long chains of amino acids linked together. Some amino acids can be made by the human body (non-essential amino acids) but others cannot; these are called ‘essential amino acids’ and must be provided by food. All the essential amino acids needed are found in the protein in animal foods, such as milk, eggs, meat and fish. Proteins in plant-based foods contain some but not all of the essential amino acids. However, the combination of a starchy food, such as cereals and their flours, bread, pasta, potatoes or rice, together with pulses or nuts will provide all the essential amino acids together. Examples of this combination are baked beans on toast, rice and peas or a hummus or peanut butter sandwich.
Effects of preoperative intravenous glutamine administration on cardiac and renal functions in patients undergoing mitral valve replacement surgeries: A randomized double-blind controlled trial
Published in Egyptian Journal of Anaesthesia, 2023
Mohamed F. Mostafa, Hany Ahmad Ibrahim Elmorabaa, Mohammed Mahmoud Mostafa, Ramy Mostafa Abd El Gawad, Mohamed Ismail Seddik, Ragaa Herdan, Mostafa Hassanien Bakr, Emad Zarief Kamel
Conditional amino acids are usually not essential (except in times of illness and stress), which include arginine, cysteine, glutamine, tyrosine, glycine, ornithine proline and serine. In certain pathological conditions, such as burns, traumas, total parenteral nutrition, or in physiological status during pregnancy and weaning, a number of non-essential amino acids (arginine, glutamine, glutamate, glycine, proline, taurine, and cysteine) have been found to become compulsorily essential. This change in the need for specific amino acids can be due in part to their effects on the immune system [4]. Glutamine is a conditional essential amino acid, which has a well-known protective effects on gastrointestinal tract mucosa through the enhancement of heat shock protein production which in turn reduces the effects of inflammatory-induced cytokine cellular damage [5]. Glutamine deficiency impairs immunity and gastrointestinal endothelial dysfunction [6].
Therapeutic perspectives on the metabolism of lymphocytes in patients with rheumatoid arthritis and systemic lupus erythematosus
Published in Expert Review of Clinical Immunology, 2021
Amino acid metabolism plays an important role in immune cell activation, differentiation, and function. Amino acids are required not only for protein synthesis, but also for various cellular processes underlying inflammation, such as nucleic acid synthesis, regulation of mTORC1 signaling, and control of stress pathways [39,40]. Glutamine is a non-essential amino acid abundant in the circulatory system whose consumption is increased in activated T cells [28]. In glutaminolysis, glutamine is first hydrolyzed to glutamate and then to α-ketoglutarate which is an intermediate in the TCA cycle and a substrate for histone demethylases and DNA demethylases [41]. Glutamine deficiency [2,42] or inhibition of α-ketoglutarate [43] promotes Treg cell differentiation. Glutaminase, the first enzyme in the glutaminolytic pathway, is transcriptionally induced by ICER to promote Th17 cell differentiation. Inhibition of glutaminase suppresses Th17 cell differentiation, promotes Th1 cell differentiation, and has no effect on Treg cell differentiation [44].
Amino acids in post-stroke rehabilitation
Published in Nutritional Neuroscience, 2021
Dhanasekar Karukkupalayam Ramasamy, Trayambak Dutta, Vellaichamy Kannan, Venkatraman Chandramouleeswaran
Nutritional intervention in the form of amino acid supplementation can lead to improvement of muscle bulk and functional capacity during the early post-stroke rehabilitation period [14]. The availability of amino acids is regarded as a rate-limiting step in muscle protein synthesis [15]. Therefore, supplementation of amino acids can stimulate muscle protein synthesis and increase the anabolic activity [14]. Amino Acids restore skeletal muscle function and physical performance. Amino acids also contribute to physical independence and enhance the effectiveness of post-stroke rehabilitation. The availability of amino acids reduces muscle wasting after stroke. In this review, we have compiled the available data on the benefits of oral amino acids supplementation in post-stroke rehabilitation.