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Diphenylene iodonium as an inhibitor of the NADPH oxidase complex of bovine neutrophils: Factors controlling the inhibitory potency of diphenylene iodonium in a cell‐free system of oxidase activation
Abstract
Diphenylene iodonium (Ph 2 I), a lipophilic reagent, is an efficient inhibitor of the production of O 2‐ by the activated NADPH oxidase of bovine neutrophils. In a cell‐free system of NADPH oxidase activation consisting of neutrophil membranes and cytosol from resting cells, supplemented with guanosine 5′‐[γ‐thio]triphosphate, MgCl 2 and arachidonic acid, or in membranes isolated from neutrophils activated by 4β‐phorbol 12‐myristate 13‐acetate, addition of a reducing agent, e.g. NADPH or sodium dithionite, markedly enhanced inhibition of the NADPH oxidase by Ph 2 I. The membrane fraction was found to contain the Ph 2 I‐sensitive component(s). In the presence of a concentration of Ph 2 I sufficient to fully inhibit O 2‐ production (around 10 nmol/mg membrane protein), addition of catalytic amounts of the redox mediator dichloroindophenol (Cl 2 Ind) resulted in a by‐pass of the electron flow to cytochrome c, the rate of which was about half of that determined in non‐inhibited oxidase. A marked increase in the efficiency of this by‐pass was achieved by addition of sodium deoxycholate. The Cl 2‐Ind‐mediated cytochrome c reduction was negligible in membranes isolated from resting neutrophils. At a higher concentration of Ph 2 I (100 nmol/mg membrane protein), the Cl 2 Ind‐mediated cytochrome c reductase activity was only half inhibited, which indicated that, in the NADPH oxidase complex, there are at least two Ph 2 I sensitive components differing by their sensitivity to the inhibitor. At low concentrations of Ph 2 I (≤ 10 nmol/mg protein), the spectrum of reduced cytochrome b558 in isolated neutrophil membranes was modified, suggesting that the component sensitive to low concentrations of Ph 2 I is the heme binding component of cytochrome b558. Higher concentrations of Ph 2 I were found to inhibit the isolated NADPH dehydrogenase component of the oxidase complex. A number of membrane and cytosolic proteins were labeled by [125 I]Ph 2 I. However, the radiolabeling of a membrane‐bound 24‐kDa protein, which might be the small subunit of cytochrome b558, responded more specifically to the conditions of activation and reduction which are required for inhibition of O 2‐ production by Ph 2 I. The O 2‐‐generating form of xanthine oxidase was also inhibited by Ph 2 I. Inhibition of xanthine oxidase, a non‐heme iron flavoprotein, by Ph 2 I had a number of features in common with that of the neutrophil NADPH oxidase, namely the requirement of reducing conditions for inhibition of O 2‐ production by Ph 2 I and the induction of a by‐pass of electron flow to cytochrome c by Cl 2 Ind in the inhibited enzyme, suggesting some similarity in the molecular organization of the two enzymes.
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Diphenylene iodonium (DPI) is a nonspecific inhibitor of all NOX isoforms.
“Diphenylene iodonium (DPI) (FIGURE 10) is a nonspecific inhibitor of all NOX isoforms (18, 197, 246).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [246]
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The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
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“nitric oxide synthase (835), xanthine oxidase (225), mito-”
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Metadata
- Authors
- DOUSSIÈRE, J., & VIGNAIS, P. V.
- Affiliations
- CEA Grenoble (FR)
- Corresponding author
- DOUSSIÈRE, Jacques
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1992-08
- Volume
- 208
- Issue
- 1
- Pages
- 61-71
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1538527390
- Cited by
- 153
- References
- 32
- Citations by year
- 2025: 4 · 2023: 5 · 2022: 1 · 2021: 3 · 2020: 2 · 2018: 7 · 2017: 4 · 2016: 1 · 2015: 3 · 2014: 4 · 2013: 7 · 2012: 5
- FWCI
- 1.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- 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
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- diphenyleneiodonium, NADPH oxidase, neutrophils, superoxide production, cytochrome b558, cytochrome c reduction, NADPH dehydrogenase, oxidase activation, redox mediators
- MeSH terms
- Animals, Cattle, Cell Membrane, Cell-Free System, Cytochrome c Group, Deoxycholic Acid, Electron Transport, Kinetics, Mersalyl, NADH, NADPH Oxidoreductases, Neutrophils, Onium Compounds, Oxidation-Reduction, 2,6-Dichloroindophenol, NADPH Oxidases
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