Targeting NADPH-oxidase by reactive oxygen species reveals an initial sensitive step in the assembly process
Abstract
NADPH-oxidase (Nox) is a highly regulated dynamic complex comprising membrane and cytosolic proteins and is the major source of nonmitochondrial cellular reactive oxygen species (ROS). In phagocyte cells, in which ROS are produced in huge amounts, Nox is "naturally" assailed by the action of its own ROS. We have subjected each individual component of Nox or the whole complex at various times during the assembly process either to oxygen free radicals produced by radiolysis or to hydrogen peroxide. Membrane components presented the highest irradiation sensitivity. Irradiation of p67(phox) drastically decreased its interaction with arachidonic acid and destabilized the [p47(phox)-p67(phox)] complex. When the system was irradiated during its assembly process, we could identify an initial irradiation-sensitive phase followed by a resistant form when the complex was assembled.
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Superoxide and H2O2 added to NOX subunits decrease O2•− production, but only when added prior to subunit assembly.
“Superoxide and H2O2 added to NOX subunits have been shown to decrease O2•− production, but only when added prior to subunit assembly [172].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [172]
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- Authors
- Ostuni, M. A., Gelinotte, M., Bizouarn, T., Baciou, L., & Houée-Levin, C.
- Affiliations
- Université Paris-Sud (FR)
- Corresponding author
- Ostuni, Mariano A.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 49
- Issue
- 5
- Pages
- 900-907
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2044499022
- Cited by
- 32
- References
- 46
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 3 · 2014: 7 · 2013: 1 · 2012: 2
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- CHIST-ERA
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase, reactive oxygen species, oxidative stress, protein complex formation, p67phox, p47phox, arachidonic acid, hydrogen peroxide, oxygen free radicals, radiolysis, phagocytes
- MeSH terms
- Animals, Cattle, Drug Resistance, Enzyme Activation, Humans, Hydrogen Peroxide, Models, Chemical, Phosphoproteins, Reactive Oxygen Species, NADPH Oxidases, Protein Subunits, Protein Multimerization
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