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Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme

NADPH oxidase is a superoxide (O(2)(•−))-generating enzyme first identified in phagocytes, essential for their bactericidal activities. Later, in non-phagocytes, production of O(2)(•−) was also demonstrated in an NADPH-dependent manner. In the last decade, several non-phagocyte-type NADPH oxidases h...

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Detalles Bibliográficos
Autores principales: Katsuyama, Masato, Matsuno, Kuniharu, Yabe-Nishimura, Chihiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: the Society for Free Radical Research Japan 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3246189/
https://www.ncbi.nlm.nih.gov/pubmed/22247596
http://dx.doi.org/10.3164/jcbn.11-06SR
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author Katsuyama, Masato
Matsuno, Kuniharu
Yabe-Nishimura, Chihiro
author_facet Katsuyama, Masato
Matsuno, Kuniharu
Yabe-Nishimura, Chihiro
author_sort Katsuyama, Masato
collection PubMed
description NADPH oxidase is a superoxide (O(2)(•−))-generating enzyme first identified in phagocytes, essential for their bactericidal activities. Later, in non-phagocytes, production of O(2)(•−) was also demonstrated in an NADPH-dependent manner. In the last decade, several non-phagocyte-type NADPH oxidases have been identified. The catalytic subunit of these oxidases, NOX, constitutes the NOX family. There are five homologs in the family, NOX1 to NOX5, and two related enzymes, DUOX1 and DUOX2. Transgenic or gene-disrupted mice of the NOX family have also been established. NOX/DUOX proteins possess distinct features in the dependency on other components for their enzymatic activities, tissue distributions, and physiological functions. This review summarized the characteristics of the NOX family proteins, especially focused on their functions clarified through studies using gene-modified mice.
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spelling pubmed-32461892012-01-13 Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme Katsuyama, Masato Matsuno, Kuniharu Yabe-Nishimura, Chihiro J Clin Biochem Nutr Serial Review NADPH oxidase is a superoxide (O(2)(•−))-generating enzyme first identified in phagocytes, essential for their bactericidal activities. Later, in non-phagocytes, production of O(2)(•−) was also demonstrated in an NADPH-dependent manner. In the last decade, several non-phagocyte-type NADPH oxidases have been identified. The catalytic subunit of these oxidases, NOX, constitutes the NOX family. There are five homologs in the family, NOX1 to NOX5, and two related enzymes, DUOX1 and DUOX2. Transgenic or gene-disrupted mice of the NOX family have also been established. NOX/DUOX proteins possess distinct features in the dependency on other components for their enzymatic activities, tissue distributions, and physiological functions. This review summarized the characteristics of the NOX family proteins, especially focused on their functions clarified through studies using gene-modified mice. the Society for Free Radical Research Japan 2012-01 2011-06-17 /pmc/articles/PMC3246189/ /pubmed/22247596 http://dx.doi.org/10.3164/jcbn.11-06SR Text en Copyright © 2012 JCBN This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Serial Review
Katsuyama, Masato
Matsuno, Kuniharu
Yabe-Nishimura, Chihiro
Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
title Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
title_full Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
title_fullStr Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
title_full_unstemmed Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
title_short Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
title_sort physiological roles of nox/nadph oxidase, the superoxide-generating enzyme
topic Serial Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3246189/
https://www.ncbi.nlm.nih.gov/pubmed/22247596
http://dx.doi.org/10.3164/jcbn.11-06SR
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