Cited by 705Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

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NADPH oxidase

Babior, Bernard M·2004·Current Opinion in Immunology

DOI 10.1016/j.coi.2003.12.001

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Abstract

NADPH oxidase is an enzyme that catalyzes the production of superoxide from oxygen and NADPH. It is a complex enzyme consisting of two membrane-bound components and three components in the cytosol, plus rac 1 or rac 2. Activation of the oxidase involves the phosphorylation of one of the cytosolic components. Recent crystallography data indicate that the tail of this cytosolic component lies in a groove between two Src homology 3 domains and, when phosphorylated, the tail leaves the groove and is replaced by the tail of one of the membrane-bound components. Chronic granulomatous disease is an inherited immune deficiency caused by the absence of one of the components of the oxidase. The most important recent advances in the field have been the crystallographic analysis of the oxidase and the use of antifungal agents in the prophylaxis of chronic granulomatous disease.

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“It consists of several subunits, while the p22 phox protein, encoded by the polymorphic CYBA gene, is an essential subunit for proper expression, stabilization, and function of the enzyme (Babior, 2004; Bedard and Krause, 2007).”
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“of cell-free systems to activate this enzyme, which, in turn, led to the identification of its 5 subunits and associated regulatory G proteins (16).”
Background
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“…by phagocytic cells, neutrophils, eosinophils, and macrophages which is a substantial event for the initiation of phagocytosis and eventual destruction of foreign particles (Droge 2002) by the generation of superoxide anions and hydrogen peroxide by induction of NADPH oxidase (Babior 2004).”
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Authors: Babior, B. M.
Affiliations: Scripps Research Institute (US)
Corresponding author: Babior, Bernard M
Venue: Current Opinion in Immunology
Publisher: Elsevier BV
Published: 2004-02
Volume: 16
Issue: 1
Pages: 42-47
ISSN: 0952-7915 (ISSN-L)
DOI: 10.1016/j.coi.2003.12.001
OpenAlex: W4242182607
Cited by: 705
References: 63
Citations by year: 2026: 7 · 2025: 8 · 2024: 25 · 2023: 20 · 2022: 28 · 2021: 24 · 2020: 34 · 2019: 22 · 2018: 21 · 2017: 26 · 2016: 29 · 2015: 29 · 2014: 53 · 2013: 40 · 2012: 42
FWCI: 2.15
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Current Opinion in Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ai044434-05)
National Institute of Allergy and Infectious Diseases (AI44434, R01AI028479, AI-24227, AI28479)
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 (medical) › Nitric Oxide and Endothelin Effects
Keywords: NADPH oxidase, superoxide production, Rac1, Rac2, Src homology 3 domain, chronic granulomatous disease, antifungal prophylaxis, crystal structure
MeSH terms: Granulomatous Disease, Chronic, Humans, Models, Molecular, Crystallography, X-Ray, src Homology Domains, NADPH Oxidases, Protein Subunits

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