Antioxidant in plants, animals, fungi, and some bacteria and archaea.- Glutathione
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Semiessential proteinogenic amino acid with the formula HOOC-CH-(NH2)-CH2-SH.
Its antioxidant properties are typically expressed in the tripeptide glutathione, which occurs in humans and other organisms.
Antioxidants are compounds that inhibit oxidation, a chemical reaction that can produce free radicals and chain reactions that may damage the cells of organisms.
To balance oxidative stress, plants and animals maintain complex systems of overlapping antioxidants, such as glutathione.
Imbalance between the systemic manifestation of reactive oxygen species and a biological system's ability to readily detoxify the reactive intermediates or to repair the resulting damage.
Chemically, oxidative stress is associated with increased production of oxidizing species or a significant decrease in the effectiveness of antioxidant defenses, such as glutathione.
Reactive oxygen species (ROS) are highly reactive chemicals formed from O2.
Glutathione peroxidase reduces hydrogen peroxide by transferring the energy of the reactive peroxides to a sulfur-containing tripeptide called glutathione.
Peptide derived from three amino acids joined by two or sometimes three peptide bonds.
In terms of scientific investigations, the dominant tripeptide is glutathione (γ- L -Glutamyl- L -cysteinylglycine), which serves many roles in many forms of life.
Leukotrienes are a family of eicosanoid inflammatory mediators produced in leukocytes by the oxidation of arachidonic acid (AA) and the essential fatty acid eicosapentaenoic acid (EPA) by the enzyme arachidonate 5-lipoxygenase.
LTF4, like LTD4, is a metabolite of LTC4, but, unlike LTD4, which lacks the glutamic residue of glutathione, LTF4 lacks the glycine residue of glutathione.
Glutamate receptor and ion channel found in neurons.
However, hypofunction of NMDA receptors (due to glutathione deficiency or other causes) may be involved in impairment of synaptic plasticity and could have other negative repercussions.
Glutathione S-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification.
Any organosulfur compound of the form R−SH, where R represents an alkyl or other organic substituent.
Thiyl intermediates also are produced by the oxidation of glutathione, an antioxidant in biology.
Metabolic breakdown of drugs by living organisms, usually through specialized enzymatic systems.
In subsequent phase II reactions, these activated xenobiotic metabolites are conjugated with charged species such as glutathione (GSH), sulfate, glycine, or glucuronic acid.