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Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress
Molecular responses mediated by sensor proteins are important for biological defense against electrophilic stresses, such as xenobiotic electrophile exposure. NF-E2-related factor 2 (Nrf2) has an essential function as a master regulator of such cytoprotective molecular responses along with sensor pr...
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/PMC7013553/ https://www.ncbi.nlm.nih.gov/pubmed/31952233 http://dx.doi.org/10.3390/ijms21020545 |
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author | Unoki, Takamitsu Akiyama, Masahiro Kumagai, Yoshito |
author_facet | Unoki, Takamitsu Akiyama, Masahiro Kumagai, Yoshito |
author_sort | Unoki, Takamitsu |
collection | PubMed |
description | Molecular responses mediated by sensor proteins are important for biological defense against electrophilic stresses, such as xenobiotic electrophile exposure. NF-E2-related factor 2 (Nrf2) has an essential function as a master regulator of such cytoprotective molecular responses along with sensor protein Kelch-like ECH-associated protein 1. This review focuses on Nrf2 activation and its involvement with the protective defense systems under electrophilic stresses integrated with our recent findings that reactive sulfur species (RSS) mediate detoxification of electrophiles. The Nrf2 pathway does not function redundantly with the RSS-generating cystathionine γ-lyase pathway, and vice versa. |
format | Online Article Text |
id | pubmed-7013553 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70135532020-03-09 Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress Unoki, Takamitsu Akiyama, Masahiro Kumagai, Yoshito Int J Mol Sci Review Molecular responses mediated by sensor proteins are important for biological defense against electrophilic stresses, such as xenobiotic electrophile exposure. NF-E2-related factor 2 (Nrf2) has an essential function as a master regulator of such cytoprotective molecular responses along with sensor protein Kelch-like ECH-associated protein 1. This review focuses on Nrf2 activation and its involvement with the protective defense systems under electrophilic stresses integrated with our recent findings that reactive sulfur species (RSS) mediate detoxification of electrophiles. The Nrf2 pathway does not function redundantly with the RSS-generating cystathionine γ-lyase pathway, and vice versa. MDPI 2020-01-15 /pmc/articles/PMC7013553/ /pubmed/31952233 http://dx.doi.org/10.3390/ijms21020545 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 Unoki, Takamitsu Akiyama, Masahiro Kumagai, Yoshito Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress |
title | Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress |
title_full | Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress |
title_fullStr | Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress |
title_full_unstemmed | Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress |
title_short | Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress |
title_sort | nrf2 activation and its coordination with the protective defense systems in response to electrophilic stress |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7013553/ https://www.ncbi.nlm.nih.gov/pubmed/31952233 http://dx.doi.org/10.3390/ijms21020545 |
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