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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7663550 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT musaogullariaysenur redoxregulationbyproteinsglutathionylationfrommolecularmechanismstoimplicationsinhealthanddisease AT chaiyuhcherng redoxregulationbyproteinsglutathionylationfrommolecularmechanismstoimplicationsinhealthanddisease |