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Cited by 314Redox biology and oxidative stressSulfur Compounds in BiologyGlutathione Transferases and Polymorphisms

S-Glutathionylation: From Molecular Mechanisms to Health Outcomes

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Xiong, Ying, Uys, Joachim D., Tew, Kenneth D., Townsend, Danyelle M.·2011·Antioxidants & Redox Signaling
DOI 10.1089/ars.2010.3540PMC PMC3110090
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Abstract

Redox homeostasis governs a number of critical cellular processes. In turn, imbalances in pathways that control oxidative and reductive conditions have been linked to a number of human disease pathologies, particularly those associated with aging. Reduced glutathione is the most prevalent biological thiol and plays a crucial role in maintaining a reduced intracellular environment. Exposure to reactive oxygen or nitrogen species is causatively linked to the disease pathologies associated with redox imbalance. In particular, reactive oxygen species can differentially oxidize certain cysteine residues in target proteins and the reversible process of S-glutathionylation may mitigate or mediate the damage. This post-translational modification adds a tripeptide and a net negative charge that can lead to distinct structural and functional changes in the target protein. Because it is reversible, S-glutathionylation has the potential to act as a biological switch and to be integral in a number of critical oxidative signaling events. The present review provides a comprehensive account of how the S-glutathionylation cycle influences protein structure/function and cellular regulatory events, and how these may impact on human diseases. By understanding the components of this cycle, there should be opportunities to intervene in stress- and aging-related pathologies, perhaps through prevention and diagnostic and therapeutic platforms. Antioxid. Redox Signal. 15, 233–270.

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  • The overoxidation product cysteine sulfonic acid is irreparably damaged and the affected protein has to be degraded by the proteasome.

    “The overoxidation product cysteine sulfonic acid is irreparably damaged and the affected protein has to be degraded by the proteasome [19].”

    From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [19]

    Section III, “Enzymes That Catalyze the S-Glutathionylation Cycle” (page not available), says oxidation to sulfonic acid is generally irreparable and leads to proteasomal degradation of the protein. The citing sentence omits “generally” and makes degradation categorical (“has to”), overstating the review’s qualification. (LLM, conf=0.88)

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200 of 304 shown

Authors
Xiong, Y., Uys, J. D., Tew, K. D., & Townsend, D. M.
Affiliations
Medical University of South Carolina (US)
ORCID
Venue
Antioxidants & Redox Signaling
Publisher
SAGE Publications
Published
2011-07
Volume
15
Issue
1
Pages
233-270
ISSN
  • 1523-0864 (ISSN-L)
  • 1557-7716
DOI
10.1089/ars.2010.3540
PMC
PMC3110090
OpenAlex
W2031027059
Cited by
314
References
319
Citations by year
2026: 13 · 2025: 18 · 2024: 35 · 2023: 27 · 2022: 31 · 2021: 24 · 2020: 27 · 2019: 16 · 2018: 17 · 2017: 11 · 2016: 15 · 2015: 10 · 2014: 16 · 2013: 28 · 2012: 15
FWCI
2.00
Type
journal article
Language
en
Open access
Licence
journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)
Locations
  • Antioxidants and Redox Signaling (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords
S-glutathionylation, redox homeostasis, reduced glutathione, cysteine oxidation, reactive oxygen species, reactive nitrogen species, post-translational modification, protein structure-function relationship, redox signaling, aging, disease pathology, redox imbalance
MeSH terms
Animals, Glutathione, Humans, Nervous System Diseases, Protein Processing, Post-Translational, Signal Transduction, Reactive Oxygen Species

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