Detection of superoxide anion and hydrogen peroxide production by cellular NADPH oxidases

Nauseef, William M.

doi:10.1016/j.bbagen.2013.04.040

Cited by 180Redox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative MechanismsNitric Oxide and Endothelin Effects

Detection of superoxide anion and hydrogen peroxide production by cellular NADPH oxidases

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Nauseef, William M.·2014·Biochimica et Biophysica Acta (BBA) - General Subjects

DOI 10.1016/j.bbagen.2013.04.040PMC PMC3770773

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Abstract

Background The recent recognition that isoforms of the cellular NADPH-dependent oxidases, collectively known as the NOX protein family, participate in a wide range of physiologic and pathophysiologic processes in both the animal and plant kingdoms has stimulated interest in the identification, localization, and quantitation of their products in biological settings. Although several tools for measuring oxidants released extracellularly are available, the specificity and selectivity of the methods for reliable analysis of intracellular oxidants have not matched the enthusiasm for studying NOX proteins.Scope of review Focusing exclusively on superoxide anion and hydrogen peroxide produced by NOX proteins, this review describes the ideal probe for analysis of O2(-) and H2O2 generated extracellularly and intracellularly by NOX proteins. An overview of the components, organization, and topology of NOX proteins provides a rationale for applying specific probes for use and a context in which to interpret results and thereby construct plausible models linking NOX-derived oxidants to biological responses. The merits and shortcomings of methods currently in use to assess NOX activity are highlighted, and those assays that provide quantitation of superoxide or H2O2 are contrasted with those intended to examine spatial and temporal aspects of NOX activity.Major conclusions Although interest in measuring the extracellular and intracellular products of the NOX protein family is great, robust analytical probes are limited.General significance The widespread involvement of NOX proteins in many biological processes requires rigorous approaches to the detection, localization, and quantitation of the oxidants produced. This article is part of a Special Issue entitled Current methods to study reactive oxygen species - pros and cons and biophysics of membrane proteins. Guest Editor: Christine Winterbourn.

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WST-1, a cell-impermeable sulphonated tetrazolium salt, has very low background absorbance and is efficiently reduced by superoxide to a stable water-soluble formazan with high molar absorptivity.
“To overcome this limitation, the cell-impermeable sulphonated tetrazolium salt, WST-1, which exhibits a very low background absorbance and is efficiently reduced by superoxide to a stable, water-soluble formazan with high molar absorptivity, is used [154,155], Figure 61.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [154]

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Quantitative and temporal characterization of the extracellular H2O2 pool generated by human neutrophils.
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Detection of intracellular superoxide formation in endothelial cells and intact tissues using dihydroethidium and an HPLC-based assay
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Dual Oxidase-2 Has an Intrinsic Ca2+-dependent H2O2-generating Activity
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Boronate Probes as Diagnostic Tools for Real Time Monitoring of Peroxynitrite and Hydroperoxides
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Activation of a NADPH Oxidase From Horse Polymorphonuclear Leukocytes in a Cell- Free System
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Lucigenin (Bis-N-methylacridinium) as a Mediator of Superoxide Anion Production
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Isoluminol-enhanced chemiluminescence: A sensitive method to study the release of superoxide anion from human neutrophils
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Nox4-Derived H2O2 Mediates Endoplasmic Reticulum Signaling through Local Ras Activation
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Nox4 involvement in TGF-beta and SMAD3-driven induction of the epithelial-to-mesenchymal transition and migration of breast epithelial cells
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Detection of hydrogen peroxide with Amplex Red: interference by NADH and reduced glutathione auto-oxidation
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Gp91 phox is the heme binding subunit of the superoxide-generating NADPH oxidase
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A design of fluorescent probes for superoxide based on a nonredox mechanism
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The NADPH Oxidase Nox3 Constitutively Produces Superoxide in a p22 -dependent Manner
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Activity and activation of the granulocyte superoxide-generating system
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Measurement of NAD(P)H oxidase-derived superoxide with the luminol analogue L-012
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Global Profiling of Reactive Oxygen and Nitrogen Species in Biological Systems
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Neutrophils from p40phox−/− mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing
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In vitro evaluation of opsonic and cellular granulocyte function by luminol-dependent chemiluminescence: utility in patients with severe neutropenia and cellular deficiency states
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Processing and Maturation of Flavocytochromeb 558 Include Incorporation of Heme as a Prerequisite for Heterodimer Assembly
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Self-citation
Superoxide Production by Digitonin-Stimulated Guinea Pig Granulocytes
Cohen, H. J., & Chovaniec, M. E. (1978) · Journal of Clinical Investigation · doi:10.1172/jci109008 · Cited by 173 · see citing works
Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation
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A sensitive and selective assay for chloramine production by myeloperoxidase
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Fluorescent probes for nitric oxide and hydrogen peroxide in cell signaling
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Chemiluminescent Detection of Oxidants in Vascular Tissue
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Nox enzymes from fungus to fly to fish and what they tell us about Nox function in mammals
Aguirre, J., & Lambeth, J. D. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.027 · Cited by 158 · see citing works
Cytochrome c Is a Potent Catalyst of Dichlorofluorescin Oxidation: Implications for the Role of Reactive Oxygen Species in Apoptosis
Burkitt, M. J., & Wardman, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4578 · Cited by 154 · see citing works
Detection of reactive oxygen species derived from the family of NOX NADPH oxidases
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Reactive oxygen species derived from Nox4 mediateBMP2gene transcription and osteoblast differentiation
Mandal, C. C., Ganapathy, S., Gorin, Y. C., Mahadev, K., Block, K. L., Abboud, H. E., Harris, S. E., Ghosh-Choudhury, G., & Ghosh‐Choudhury, N. (2010) · Biochemical Journal · doi:10.1042/bj20100357 · Cited by 146 · see citing works
Measurement of Respiratory Burst Products Generated by Professional Phagocytes
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The Nox Family of NADPH Oxidases: Friend or Foe of the Vascular System?
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Application of the Amplex red/horseradish peroxidase assay to measure hydrogen peroxide generation by recombinant microsomal enzymes
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Nox4 mediates TGF-β1-induced retinoblastoma protein phosphorylation, proliferation, and hypertrophy in human airway smooth muscle cells
Sturrock, A., Huecksteadt, T. P., Norman, K. G., Sanders, K. A., Murphy, T. M., Chitano, P., Wilson, K. M., Hoidal, J. R., & Kennedy, T. P. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00430.2006 · Cited by 132 · see citing works
Dual oxidases
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Nox4-derived reactive oxygen species mediate cardiomyocyte injury in early type 1 diabetes
Maalouf, R., Eid, A. A., Gorin, Y. C., Block, K. L., Escobar, G. P., Bailey, S. R., & Abboud, H. E. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00331.2011 · Cited by 129 · see citing works
PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation
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What really happens in the neutrophil phagosome?
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Adventitial fibroblast reactive oxygen species as autacrine and paracrine mediators of remodeling: Bellwether for vascular disease?
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Fluorescent Gold Nanoprobe Sensitive to Intracellular Reactive Oxygen Species
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NOX5: from basic biology to signaling and disease
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Chronic Granulomatous Disease (CGD) and Complete Myeloperoxidase Deficiency Both Yield Strongly Reduced Dihydrorhodamine 123 Test Signals but Can Be Easily Discerned in Routine Testing for CGD
Mauch, L., Lun, A., O’Gorman, M. R. G., Harris, J. S., Schulze, I., Zychlinsky, A., Fuchs, T. A., Oelschlägel, U., Brenner, S., Kutter, D., et al. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2006.083444 · Cited by 119 · see citing works
Caspase-1 Dependent IL-1β Secretion Is Critical for Host Defense in a Mouse Model of Chlamydia pneumoniae Lung Infection
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CCLXXX.—Studies of the boron–carbon linkage. Part I. The oxidation and nitration of phenylboric acid
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The association of FAD with the cytochrome b–245 of human neutrophils
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Heme-ligating Histidines in Flavocytochromeb 558
Biberstine-Kinkade, K. J., DeLeo, F. R., Epstein, R. I., Leroy, B. A., Nauseef, W. M., & Dinauer, M. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103327200 · Cited by 109 · see citing works
Self-citation
Mutational Analysis Reveals Distinct Features of the Nox4-p22 Complex
von Löhneysen, K., Noack, D., Jesaitis, A. J., Dinauer, M. C., & Knaus, U. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804200200 · Cited by 106 · see citing works
Cytochrome c-mediated oxidation of hydroethidine and mito-hydroethidine in mitochondria: Identification of homo- and heterodimers
Zielonka, J., Srinivasan, S., Hardy, M., Ouari, O., López, M., Vasquez-Vivar, J. M., Avadhani, N. G., & Kalyanaraman, B. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.013 · Cited by 105 · see citing works
Lucigenin as mediator of superoxide production: revisited
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What do we measure by a luminol-dependent chemiluminescence of phagocytes?
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Voltage-Gated Proton Channels Find Their Dream Job Managing the Respiratory Burst in Phagocytes
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Control of Hepatic Nuclear Superoxide Production by Glucose 6-Phosphate Dehydrogenase and NADPH Oxidase-4
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Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells
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Luminescence of imidazo[1,2-a]pyrazin-3(7H)-one compounds
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Applications of Electron Spin Resonance Spectrometry for Reactive Oxygen Species and Reactive Nitrogen Species Research
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Guinea pig gastric mucosal cells produce abundant superoxide anion through an NADPH oxidase-like system
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Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3
Nakano, Y., Bánfi, B., Jesaitis, A. J., Dinauer, M. C., Allen, L. H., & Nauseef, W. M. (2007) · Biochemical Journal · doi:10.1042/bj20060819 · Cited by 86 · see citing works
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Caenorhabditis elegans and Human Dual Oxidase 1 (DUOX1) “Peroxidase” Domains
Meitzler, J. L., & de Montellano, P. R. O. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.013581 · Cited by 86 · see citing works
Nox enzymes in immune cells
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Biosynthesis of Flavocytochrome b 558
Yu, L., DeLeo, F. R., Biberstine-Kinkade, K. J., Renee, J., Nauseef, W. M., & Dinauer, M. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4364 · Cited by 78 · see citing works
Self-citation
Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: Its usefulness in the assay of respiratory burst in neutrophils
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IFNβ/TNFα synergism induces a non-canonical STAT2/IRF9-dependent pathway triggering a novel DUOX2 NADPH Oxidase-mediated airway antiviral response
Fink, K., Martin, L., Mukawera, E., Chartier, S., Deken, X. D., Brochiero, E., Miot, F., & Grandvaux, N. (2013) · Cell Research · doi:10.1038/cr.2013.47 · Cited by 69 · see citing works
Spatial and Temporal Analysis of NADPH Oxidase-Generated Hydrogen Peroxide Signals by Novel Fluorescent Reporter Proteins
Enyedi, B., Zana, M., Donkó, Á., & Geiszt, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4594 · Cited by 68 · see citing works
Pulse radiolysis and steady-state analyses of the reaction between hydroethidine and superoxide and other oxidants
Zielonka, J., Sarna, T., Roberts, J. E., Wishart, J. F., & Kalyanaraman, B. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.09.031 · Cited by 59 · see citing works
A Significant Improvement of the Efficacy of Radical Oxidant Probes by the Kinetic Isotope Effect
Kundu, K., Knight, S. F., Lee, S., Taylor, W. R., & Murthy, N. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201002228 · Cited by 58 · see citing works
The fluorescence detection of superoxide radical using hydroethidine could be complicated by the presence of heme proteins
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Constitutive NADPH Oxidase 4 Activity Resides in the Composition of the B-loop and the Penultimate C Terminus
von Löhneysen, K., Noack, D., Hayes, P., Friedman, J. S., & Knaus, U. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.332494 · Cited by 53 · see citing works
Interference of non-specific peroxidases in the fluorescence detection of superoxide radical by hydroethidine oxidation: a new assay for H2O2
Patsoukis, N., Papapostolou, I., & Georgiou, C. D. (2005) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-004-2999-x · Cited by 51 · see citing works
IGF-I increases the expression of fibronectin by Nox4-dependent Akt phosphorylation in renal tubular epithelial cells
New, D. D., Block, K. L., Bhandhari, B., Gorin, Y. C., & Abboud, H. E. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00141.2011 · Cited by 50 · see citing works
Hydropropidine: A novel, cell-impermeant fluorogenic probe for detecting extracellular superoxide
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Inhibitory Action of NoxA1 on Dual Oxidase Activity in Airway Cells
Pacquelet, S., Lehmann, M. D., Luxen, S., Regazzoni, K., Frausto, M., Noack, D., & Knaus, U. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709108200 · Cited by 44 · see citing works
Assays using horseradish peroxidase and phenolic substrates require superoxide dismutase for accurate determination of hydrogen peroxide production by neutrophils
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Optical imaging of intracellular reactive oxygen species for the assessment of the cytotoxicity of nanoparticles
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Thermodynamic Basis for Redox Regulation of the Yap1 Signal Transduction Pathway
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Excretion of superoxide by phagocytes measured with cytochrome c entrapped in resealed erythrocyte ghosts.
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Physiological roles of voltage-gated proton channels in leukocytes
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The type of DUOX-dependent ROS production is dictated by defined sequences in DUOXA
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Cell-Free Assays
Molshanski-Mor, S., Mizrahi, A., Ugolev, Y., Dahan, I. M., Berdichevsky, Y., & Pick, E. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-467-4_25 · Cited by 33 · see citing works
On radical production by PMA-stimulated neutrophils as monitored by luminol-amplified chemiluminescence
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Myeloperoxidase interaction with peroxynitrite: chloride deficiency and heme depletion
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Thyroid hydrogen peroxide production is enhanced by the Th2 cytokines, IL-4 and IL-13, through increased expression of the dual oxidase 2and its maturation factorDUOXA2
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Membrane phospholipid metabolism during phagocytosis in human neutrophils
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Generation of hydrogen peroxide by human neutrophils
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Anionic lipid-induced conformational changes in human phagocyte flavocytochrome b precede assembly and activation of the NADPH oxidase complex
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Analysis of Electrophysiological Properties and Responses of Neutrophils
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Analysis of Electrophysiological Properties and Responses of Neutrophils
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Generation of hydrogen peroxide by human neutrophils: Effects of soluble stimuli and requirements for divalent cations
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Cytofluorometric assessment of phagosomal oxidation and the mode of inheritance in patients suffering from chronic granulomatous disease
Kohl, A., Roesler, J., Döcke, W. ‐., Valet, G., & Volk, H. (1991) · Inflammation Research · doi:10.1007/bf01983341 · Cited by 1 · see citing works

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Oxidative Stress
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520 · see citing works
Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress
Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148 · see citing works
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
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Authors: Nauseef, W. M.
Affiliations: University of Iowa (US)
Corresponding author: Nauseef, William M.
ORCID: Nauseef, William M.
Venue: Biochimica et Biophysica Acta (BBA) - General Subjects
Publisher: Elsevier BV
Published: 2014-02
Volume: 1840
Issue: 2
Pages: 757-767
ISSN: 0304-4165 (ISSN-L)
DOI: 10.1016/j.bbagen.2013.04.040
PMC: PMC3770773
OpenAlex: W2085864038
Cited by: 180
References: 171
Citations by year: 2026: 11 · 2025: 9 · 2024: 13 · 2023: 12 · 2022: 17 · 2021: 5 · 2020: 16 · 2019: 14 · 2018: 14 · 2017: 19 · 2016: 17 · 2015: 17 · 2014: 13 · 2013: 3
FWCI: 1.53
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Health (AI70958, AI044642)
Veterans Administration
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords: NADPH oxidase, superoxide, hydrogen peroxide, reactive oxygen species, fluorescent probes
MeSH terms: Animals, Humans, Hydrogen Peroxide, Superoxides, NADPH Oxidases

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Detection of superoxide anion and hydrogen peroxide production by cellular NADPH oxidases

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