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Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease

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, interactio...

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Detalles Bibliográficos
Autores principales: Musaogullari, Aysenur, Chai, Yuh-Cherng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7663550/
https://www.ncbi.nlm.nih.gov/pubmed/33143095
http://dx.doi.org/10.3390/ijms21218113
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author Musaogullari, Aysenur
Chai, Yuh-Cherng
author_facet Musaogullari, Aysenur
Chai, Yuh-Cherng
author_sort Musaogullari, Aysenur
collection PubMed
description 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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spelling pubmed-76635502020-11-14 Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease Musaogullari, Aysenur Chai, Yuh-Cherng Int J Mol Sci Review 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. MDPI 2020-10-30 /pmc/articles/PMC7663550/ /pubmed/33143095 http://dx.doi.org/10.3390/ijms21218113 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Musaogullari, Aysenur
Chai, Yuh-Cherng
Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
title Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
title_full Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
title_fullStr Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
title_full_unstemmed Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
title_short Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
title_sort redox regulation by protein s-glutathionylation: from molecular mechanisms to implications in health and disease
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7663550/
https://www.ncbi.nlm.nih.gov/pubmed/33143095
http://dx.doi.org/10.3390/ijms21218113
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