Glutathione Redox Cycle, 2nd Edition

Dear Colleagues,

γ-L-glutamyl-L-cysteinyl-glycine, also defined as reduced glutathione (GSH), is involved in cell processes required for the maintenance and regulation of thiol redox status, while oxidized glutathione (GSSG) is formed either by the catalytic reaction of glutathione peroxidase or by GSH reactions with electrophilic compounds. Reduced glutathione (GSH) and its oxidized form (GSSG) are central to maintaining cellular redox homeostasis. Under physiological and stress conditions, this cycle regulates a wide range of cellular processes through thiol–disulfide exchange, enzymatic catalysis, and metabolite recycling.

Key pathways include the following:

• Biosynthesis and Metabolism: The synthesis of GSH via γ-glutamyl-cysteine synthase and glutathione synthase and its catabolism through enzymes such as γ-glutamyl transpeptidase.
• Redox Regulation: The interplay between glutathione peroxidase, glutathione reductase, and the thioredoxin/glutaredoxin system in managing oxidative stress and detoxification.
• Protein Modification: The formation of mixed disulfides (S-glutathionylation) and its role in signaling and stress adaptation.
• Detoxification: Catalysis by glutathione transferases in conjugating electrophilic compounds.

Building on the success of the first edition, this second edition aims to gather the latest research on the glutathione redox cycle. We encourage submissions—including original research and review articles—that explore not only the core biochemistry and metabolism but also emerging topics, such as its role in disease mechanisms, aging, environmental adaptation, and novel therapeutic targets. Authors are encouraged to discuss not only the limited biochemical and metabolic examples described above in their publications, but also all aspects concerning the glutathione redox cycle.

We welcome your contributions and look forward to advancing this dynamic field together.

Prof. Dr. Alessio Bocedi
Guest Editor

Manuscript Submission Information

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