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N-acetyl-l-cysteine averts ferroptosis by fostering glutathione peroxidase 4.
Cell Chem. Bio. 32, 767-775.e5 (2025)
Verlagsversion
DOI
PMC
N-acetyl-l-cysteine (NAC) is a medication and a widely used antioxidant in cell death research. Despite its somewhat obscure mechanism of action, its role in inhibiting ferroptosis is gaining increasing recognition. In this study, we demonstrate that NAC treatment rapidly replenishes the intracellular cysteine pool, reinforcing its function as a prodrug for cysteine. Interestingly, its enantiomer, N-acetyl-d-cysteine (d-NAC), which cannot be converted into cysteine, also exhibits a strong anti-ferroptotic effect. We further clarify that NAC, d-NAC, and cysteine all act as direct reducing substrates for GPX4, counteracting lipid peroxidation. Consequently, only GPX4-rather than system xc-, glutathione biosynthesis, or ferroptosis suppressor protein 1-is necessary for NAC and d-NAC to prevent ferroptosis. Additionally, we identify a broad range of reducing substrates for GPX4 in vitro, including β-mercaptoethanol. These findings provide new insights into the mechanisms underlying the protective effects of NAC and other potential GPX4-reducing substrates against ferroptosis.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Fsp1 ; Gpx4 ; Gsh ; Nac ; Cysteine ; D-nac ; Ferroptosis ; System X(c)(−) ; Xct ; β-me
ISSN (print) / ISBN
2451-9448
e-ISSN
2451-9456
Zeitschrift
Cell Chemical Biology
Quellenangaben
Band: 32,
Heft: 5,
Seiten: 767-775.e5
Verlag
Cell Press
Verlagsort
Cambridge, Massachusetts
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Metabolism and Cell Death (MCD)