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A non-essential, non-polar, non-optical, glucogenic amino acid. Glycine, an inhibitory neurotransmitter in the CNS, triggers chloride ion influx via ionotropic receptors, thereby creating an inhibitory post-synaptic potential. In contrast, this agent also acts as a co-agonist, along with glutamate, facilitating an excitatory potential at the glutaminergic N-methyl-D-aspartic acid (NMDA) receptors. Glycine is an important component and precursor for many macromolecules in the cells.
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A semi-essential amino acid (children should obtain it from food) needed in humans for growth and tissue repair, Histidine is important for maintenance of myelin sheaths that protect nerve cells and is metabolized to the neurotransmitter histamine. Histamines play many roles in immunity, gastric secretion, and sexual functions. Histidine is also required for blood cell manufacture and protects tissues against damage caused by radiation and heavy metals. (NCI04)
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An amino acid derivative and homolog of cysteine containing an additional methylene bridge. Homocysteine is a product of methionine metabolism and elevated plasma levels are associated with cardiovascular disease, Alzheimer disease and several metabolic diseases.
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A nonessential amino acid derivative formed during post-translational protein modification through hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase which requires vitamin C as a co-factor. Hydroxyproline is a major component of the protein collagen and plays a key role in the stability of the collagen triple helix. It can be used as an indicator to determine the amount of collagen. Increased hydroxyproline levels in the urine and/or serum are normally associated with degradation of connective tissue. Vitamin C deficiency decreases the conversion of proline to hydroxyproline, which leads to reduced collagen stability.
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The most abundant immunoglobulin G (IgG) subclass in the circulation of healthy individuals. The IgG1 core hinge sequence contains 15 amino acids and two interchain disulfide bonds. This subtype has high affinity for binding both Fc receptors and complement component C1q. IgG1 is the predominant antibody subclass that responds to antigens derived from both soluble and membrane proteins. Reduced levels of circulating IgG1 can indicate the presence of a variety of primary and secondary antibody deficiencies, which can result in hypogammaglobulinemia.
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The second most abundant immunoglobulin G (IgG) subclass in the circulation of healthy individuals. The IgG2 core hinge sequence contains 12 amino acids and up to four interchain disulfide bonds. This subtype has low affinity for binding both Fc receptors and complement component C1q. The production of this IgG2 is stimulated by exposure to bacterial capsular polysaccharides and other antigenic glycans.
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Along with the immunoglobulin G4 subclass (IgG4), the IgG3 subtype makes up a minor part of circulating antibodies in healthy individuals. The core hinge sequence contains approximately four times the number of amino acids as the other subclasses; allotypes of IgG3 can have up to 62 hinge residues and up to four interchain disulfide bonds. The increased hinge size for IgG3 increases the separation between the Fc (constant fragment) tail and Fab (antigen binding fragment) arms of antibodies of this subclass. This enhances the relative flexibility of the molecule, which may modulate antigen-binding capacity and immune complex formation, and may increase the affinity for binding to both Fc receptors and complement component C1q.
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Along with the immunoglobulin G3 subclass (IgG3), the IgG4 subtype makes up a minor part of circulating antibodies in healthy individuals. The IgG4 core hinge sequence contains 12 amino acids and two interchain disulfide bonds.This subtype has moderate affinity for binding Fc receptors and does not bind complement component C1q. The production of IgG4 can be stimulated following repeated or long-term exposure to antigen. Elevated levels are found in various diseases and infections and can be indicative of an fibroinflammatory syndrome known as IgG4-related disease.
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One of nine essential amino acids in humans (present in dietary proteins), Isoleucine has diverse physiological functions, such as assisting wound healing, detoxification of nitrogenous wastes, stimulating immune function, and promoting secretion of several hormones. Necessary for hemoglobin formation and regulating blood sugar and energy levels, isoleucine is concentrated in muscle tissues in humans. Isoleucine is found especially in meats, fish, cheese, eggs, and most seeds and nuts. (NCI04)
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The levorotatory isomer of the aromatic amino acid tyrosine. L-tyrosine is a naturally occurring tyrosine and is synthesized in vivo from L-phenylalanine. It is considered a non-essential amino acid; however, in patients with phenylketonuria who lack phenylalanine hydroxylase and cannot convert phenylalanine into tyrosine, it is considered an essential nutrient. In vivo, tyrosine plays a role in protein synthesis and serves as a precursor for the synthesis of catecholamines, thyroxine, and melanin.
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One of nine essential amino acids in humans (provided by food), Leucine is important for protein synthesis and many metabolic functions. Leucine contributes to regulation of blood-sugar levels; growth and repair of muscle and bone tissue; growth hormone production; and wound healing. Leucine also prevents breakdown of muscle proteins after trauma or severe stress and may be beneficial for individuals with phenylketonuria. Leucine is available in many foods and deficiency is rare. (NCI04)
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One of nine essential amino acids in humans required for growth and tissue repair, Lysine is supplied by many foods, especially red meats, fish, and dairy products. Lysine seems to be active against herpes simplex viruses and present in many forms of diet supplements. The mechanism underlying this effect is based on the viral need for amino acid arginine; lysine competes with arginine for absorption and entry into cells. Lysine inhibits HSV growth by knocking out arginine. (NCI04)
