Glutathione is a tripeptide composed of glutamate, cysteine, and glycine (?-Glu-Cys-Gly). It is the most abundant endogenous antioxidant in mammalian cells, present in millimolar concentrations intracellularly. Glutathione exists in two forms: reduced (GSH), which is the active antioxidant form, and oxidized (GSSG), which is recycled back to GSH by glutathione reductase using NADPH.
Researchers have studied glutathione extensively for its central role in cellular redox homeostasis. Research has examined how GSH neutralizes reactive oxygen species (ROS) and reactive nitrogen species (RNS) directly and serves as a cofactor for glutathione peroxidase enzymes. Studies have explored its role in xenobiotic detoxification, where conjugation with glutathione S-transferases facilitates the removal of electrophilic compounds from cells.
Research has also examined glutathione’s involvement in protein function regulation through glutathionylation – reversible modification of cysteine residues – and its role in maintaining protein folding fidelity. Studies have investigated changes in glutathione status in models of oxidative stress-related conditions affecting the nervous system, immune cells, and hepatic tissue. Preclinical research has explored intravenous and other delivery approaches in animal models to overcome its limited oral bioavailability.
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