Glutathione: A Research Overview

Chemical identity

Background

Glutathione is γ-L-glutamyl-L-cysteinylglycine. Its first bond joins the side-chain (γ) carboxyl group of glutamate to cysteine, unlike the α-peptide bonds in proteins. The thiol group (-SH) of the cysteine residue is its reactive centre.

Cells make it in two ATP-dependent steps. Glutamate–cysteine ligase forms γ-glutamylcysteine, the rate-limiting step, and glutathione synthetase then adds glycine.

Glutathione exists in a reduced form (GSH) and an oxidized form (GSSG), a disulfide of two glutathione molecules. The enzyme glutathione reductase converts GSSG back to GSH using NADPH, and the ratio of the two forms is widely used as a measure of cellular redox state.

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What the published literature reports

1. Review

   Introductory review describing glutathione as the most abundant low-molecular-weight thiol made in cells, with an overview of its roles, how it is measured, and how it is synthesised.

   Forman HJ, Zhang H, Rinna A, Mol Aspects Med, 2009 · PubMed
2. Review

   Review of how cells synthesise glutathione, covering the two enzymatic steps and how they are regulated.

   Lu SC, Biochim Biophys Acta, 2013 · PubMed
3. Review

   Review article on the roles of glutathione in the cell.

   Pompella A et al., Biochem Pharmacol, 2003 · PubMed

How to read this literature

The work cited above spans review. Findings from cell culture or animal models, and review articles that summarise them, do not establish how a compound behaves in other systems. Each citation links to the original record so you can read it directly.

Summaries describe what each cited paper reports in its own model system. They are not claims about the effects of this product.