Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
Department of Chemistry, John Carroll University, University Heights, OH 44118, USA
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Int. J. Mol. Sci. 2020, 21(21), 8113; https://doi.org/10.3390/ijms21218113
Received: 11 October 2020
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Revised: 26 October 2020
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Accepted: 27 October 2020
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Published: 30 October 2020
(This article belongs to the Special Issue S-Glutathionylation in Redox Protein Signaling and Health Outcomes)
S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases.
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Keywords:
S-glutathionylation; redox modification; protein post-translational modification; GSH/GSSG; oxidative stress
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MDPI and ACS Style
Musaogullari, A.; Chai, Y.-C. Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease. Int. J. Mol. Sci. 2020, 21, 8113. https://doi.org/10.3390/ijms21218113
AMA Style
Musaogullari A, Chai Y-C. Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease. International Journal of Molecular Sciences. 2020; 21(21):8113. https://doi.org/10.3390/ijms21218113
Chicago/Turabian StyleMusaogullari, Aysenur, and Yuh-Cherng Chai. 2020. "Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease" International Journal of Molecular Sciences 21, no. 21: 8113. https://doi.org/10.3390/ijms21218113
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