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Globin-based redox signaling
In recent years, moderate levels of reactive oxygen species (ROS) have become recognized as signaling cues that participate at all levels of cellular organization. Globins, with their redox-active heme iron and ubiquitous presence, seem ideally suited to participate in ROS metabolism. Here we commen...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5022669/ https://www.ncbi.nlm.nih.gov/pubmed/27695650 http://dx.doi.org/10.1080/21624054.2016.1184390 |
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author | De Henau, Sasha Braeckman, Bart P. |
author_facet | De Henau, Sasha Braeckman, Bart P. |
author_sort | De Henau, Sasha |
collection | PubMed |
description | In recent years, moderate levels of reactive oxygen species (ROS) have become recognized as signaling cues that participate at all levels of cellular organization. Globins, with their redox-active heme iron and ubiquitous presence, seem ideally suited to participate in ROS metabolism. Here we comment on our recent findings that show the participation of a globin, GLB-12, in a redox signaling pathway in Caenorhabditis elegans. We found that GLB-12 produces superoxide, a type of ROS, after which this is converted to what appears to be a hydrogen peroxide gradient over the plasma membrane by the activity of intracellular and extracellular superoxide dismutases. In the first part, we discuss in more detail the different regulatory mechanisms that increase the effectiveness of this redox signal. In the second part, we comment on how specific structural and biochemical properties allow this globin to perform redox reactions. Interestingly, these properties are also observed in 2 other C. elegans globins that appear to be involved in redox biology. We therefore hypothesize that globins involved in redox signaling display similar structural and biochemical characteristics and propose that a subgroup of globins can be added to the group of proteins that play a vital role in redox signaling. |
format | Online Article Text |
id | pubmed-5022669 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-50226692016-09-30 Globin-based redox signaling De Henau, Sasha Braeckman, Bart P. Worm Commentary In recent years, moderate levels of reactive oxygen species (ROS) have become recognized as signaling cues that participate at all levels of cellular organization. Globins, with their redox-active heme iron and ubiquitous presence, seem ideally suited to participate in ROS metabolism. Here we comment on our recent findings that show the participation of a globin, GLB-12, in a redox signaling pathway in Caenorhabditis elegans. We found that GLB-12 produces superoxide, a type of ROS, after which this is converted to what appears to be a hydrogen peroxide gradient over the plasma membrane by the activity of intracellular and extracellular superoxide dismutases. In the first part, we discuss in more detail the different regulatory mechanisms that increase the effectiveness of this redox signal. In the second part, we comment on how specific structural and biochemical properties allow this globin to perform redox reactions. Interestingly, these properties are also observed in 2 other C. elegans globins that appear to be involved in redox biology. We therefore hypothesize that globins involved in redox signaling display similar structural and biochemical characteristics and propose that a subgroup of globins can be added to the group of proteins that play a vital role in redox signaling. Taylor & Francis 2016-04-29 /pmc/articles/PMC5022669/ /pubmed/27695650 http://dx.doi.org/10.1080/21624054.2016.1184390 Text en © 2016 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted. |
spellingShingle | Commentary De Henau, Sasha Braeckman, Bart P. Globin-based redox signaling |
title | Globin-based redox signaling |
title_full | Globin-based redox signaling |
title_fullStr | Globin-based redox signaling |
title_full_unstemmed | Globin-based redox signaling |
title_short | Globin-based redox signaling |
title_sort | globin-based redox signaling |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5022669/ https://www.ncbi.nlm.nih.gov/pubmed/27695650 http://dx.doi.org/10.1080/21624054.2016.1184390 |
work_keys_str_mv | AT dehenausasha globinbasedredoxsignaling AT braeckmanbartp globinbasedredoxsignaling |