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TRP Channels as Sensors and Signal Integrators of Redox Status Changes
Proteins are capable of sensing the redox status of cells. Cysteine residues, which react with oxidants, reductants, and electrophiles, have been increasingly recognized as the mediators of this redox sensitivity. Cation channels encoded by the transient receptor potential (trp) gene superfamily are...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Research Foundation
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3192318/ https://www.ncbi.nlm.nih.gov/pubmed/22016736 http://dx.doi.org/10.3389/fphar.2011.00058 |
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author | Takahashi, Nobuaki Mori, Yasuo |
author_facet | Takahashi, Nobuaki Mori, Yasuo |
author_sort | Takahashi, Nobuaki |
collection | PubMed |
description | Proteins are capable of sensing the redox status of cells. Cysteine residues, which react with oxidants, reductants, and electrophiles, have been increasingly recognized as the mediators of this redox sensitivity. Cation channels encoded by the transient receptor potential (trp) gene superfamily are characterized by a wide variety of activation triggers that act from outside and inside the cell. Recent studies have revealed that a class of TRP channels is sensitive to changes in redox status and is notably susceptible to modifications of cysteine residues, such as oxidation, electrophilic reaction, and S-nitrosylation of sulfhydryls. In this review, we focus on TRP channels, which directly sense redox status, and discuss the biological significance of cysteine modifications and the consequences of this chemical reaction for physiological responses. |
format | Online Article Text |
id | pubmed-3192318 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Frontiers Research Foundation |
record_format | MEDLINE/PubMed |
spelling | pubmed-31923182011-10-20 TRP Channels as Sensors and Signal Integrators of Redox Status Changes Takahashi, Nobuaki Mori, Yasuo Front Pharmacol Pharmacology Proteins are capable of sensing the redox status of cells. Cysteine residues, which react with oxidants, reductants, and electrophiles, have been increasingly recognized as the mediators of this redox sensitivity. Cation channels encoded by the transient receptor potential (trp) gene superfamily are characterized by a wide variety of activation triggers that act from outside and inside the cell. Recent studies have revealed that a class of TRP channels is sensitive to changes in redox status and is notably susceptible to modifications of cysteine residues, such as oxidation, electrophilic reaction, and S-nitrosylation of sulfhydryls. In this review, we focus on TRP channels, which directly sense redox status, and discuss the biological significance of cysteine modifications and the consequences of this chemical reaction for physiological responses. Frontiers Research Foundation 2011-10-13 /pmc/articles/PMC3192318/ /pubmed/22016736 http://dx.doi.org/10.3389/fphar.2011.00058 Text en Copyright © 2011 Takahashi and Mori. http://www.frontiersin.org/licenseagreement This is an open-access article subject to a non-exclusive license between the authors and Frontiers Media SA, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and other Frontiers conditions are complied with. |
spellingShingle | Pharmacology Takahashi, Nobuaki Mori, Yasuo TRP Channels as Sensors and Signal Integrators of Redox Status Changes |
title | TRP Channels as Sensors and Signal Integrators of Redox Status Changes |
title_full | TRP Channels as Sensors and Signal Integrators of Redox Status Changes |
title_fullStr | TRP Channels as Sensors and Signal Integrators of Redox Status Changes |
title_full_unstemmed | TRP Channels as Sensors and Signal Integrators of Redox Status Changes |
title_short | TRP Channels as Sensors and Signal Integrators of Redox Status Changes |
title_sort | trp channels as sensors and signal integrators of redox status changes |
topic | Pharmacology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3192318/ https://www.ncbi.nlm.nih.gov/pubmed/22016736 http://dx.doi.org/10.3389/fphar.2011.00058 |
work_keys_str_mv | AT takahashinobuaki trpchannelsassensorsandsignalintegratorsofredoxstatuschanges AT moriyasuo trpchannelsassensorsandsignalintegratorsofredoxstatuschanges |