Pharmacological characterization of the seven human NOX isoforms and their inhibitors

NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O ) and/or hydrogen peroxide (H O ). As major oxidant generators, NOX are associated with oxidative damage in numerous diseases and represent promising drug targets for several pathologies. Var...

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Veröffentlicht in:	Redox biology Jg. 26; S. 101272
Hauptverfasser:	Augsburger, Fiona, Filippova, Aleksandra, Rasti, Delphine, Seredenina, Tamara, Lam, Magdalena, Maghzal, Ghassan, Mahiout, Zahia, Jansen-Dürr, Pidder, Knaus, Ulla G., Doroshow, James, Stocker, Roland, Krause, Karl-Heinz, Jaquet, Vincent
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Netherlands Elsevier 01.09.2019
Schlagworte:	Catalysis Cell Line Chromatography, Liquid Drug Discovery Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Humans Hydrogen Peroxide - metabolism Isoenzymes Leukocytes - drug effects Leukocytes - metabolism Metabolic Networks and Pathways - drug effects Models, Biological NADPH Oxidases - antagonists & inhibitors NADPH Oxidases - genetics NADPH Oxidases - metabolism Reactive Oxygen Species - metabolism Research Paper Structure-Activity Relationship Tandem Mass Spectrometry Reactive oxygen species Small molecule inhibitors NADPH oxidase NOX
ISSN:	2213-2317, 2213-2317
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Abstract	NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O ) and/or hydrogen peroxide (H O ). As major oxidant generators, NOX are associated with oxidative damage in numerous diseases and represent promising drug targets for several pathologies. Various small molecule NOX inhibitors are used in the literature, but their pharmacological characterization is often incomplete in terms of potency, specificity and mode of action. We used cell lines expressing high levels of human NOX isoforms (NOX1-5, DUOX1 and 2) to detect NOX-derived O or H O using a variety of specific probes. NOX inhibitory activity of diphenylene iodonium (DPI), apocynin, diapocynin, ebselen, GKT136901 and VAS2870 was tested on NOX isoforms in cellular and membrane assays. Additional assays were used to identify potential off target effects, such as antioxidant activity, interference with assays or acute cytotoxicity. Cells expressing active NOX isoforms formed O , except for DUOX1 and 2, and in all cases activation of NOX isoforms was associated with the detection of extracellular H O . Among all molecules tested, DPI elicited dose-dependent inhibition of all isoforms in all assays, however all other molecules tested displayed interesting pharmacological characteristics, but did not meet criteria for bona fide NOX inhibitors. Our findings indicate that experimental results obtained with widely used NOX inhibitors must be carefully interpreted and highlight the challenge of developing reliable pharmacological inhibitors of these key molecular targets.
AbstractList	Background: NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O2•-) and/or hydrogen peroxide (H2O2). As major oxidant generators, NOX are associated with oxidative damage in numerous diseases and represent promising drug targets for several pathologies. Various small molecule NOX inhibitors are used in the literature, but their pharmacological characterization is often incomplete in terms of potency, specificity and mode of action. Experimental approach: We used cell lines expressing high levels of human NOX isoforms (NOX1-5, DUOX1 and 2) to detect NOX-derived O2•- or H2O2 using a variety of specific probes. NOX inhibitory activity of diphenylene iodonium (DPI), apocynin, diapocynin, ebselen, GKT136901 and VAS2870 was tested on NOX isoforms in cellular and membrane assays. Additional assays were used to identify potential off target effects, such as antioxidant activity, interference with assays or acute cytotoxicity. Key results: Cells expressing active NOX isoforms formed O2•-, except for DUOX1 and 2, and in all cases activation of NOX isoforms was associated with the detection of extracellular H2O2. Among all molecules tested, DPI elicited dose-dependent inhibition of all isoforms in all assays, however all other molecules tested displayed interesting pharmacological characteristics, but did not meet criteria for bona fide NOX inhibitors. Conclusion: Our findings indicate that experimental results obtained with widely used NOX inhibitors must be carefully interpreted and highlight the challenge of developing reliable pharmacological inhibitors of these key molecular targets. Keywords: NADPH oxidase, NOX, Reactive oxygen species, Small molecule inhibitors Image 1 NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O ) and/or hydrogen peroxide (H O ). As major oxidant generators, NOX are associated with oxidative damage in numerous diseases and represent promising drug targets for several pathologies. Various small molecule NOX inhibitors are used in the literature, but their pharmacological characterization is often incomplete in terms of potency, specificity and mode of action. We used cell lines expressing high levels of human NOX isoforms (NOX1-5, DUOX1 and 2) to detect NOX-derived O or H O using a variety of specific probes. NOX inhibitory activity of diphenylene iodonium (DPI), apocynin, diapocynin, ebselen, GKT136901 and VAS2870 was tested on NOX isoforms in cellular and membrane assays. Additional assays were used to identify potential off target effects, such as antioxidant activity, interference with assays or acute cytotoxicity. Cells expressing active NOX isoforms formed O , except for DUOX1 and 2, and in all cases activation of NOX isoforms was associated with the detection of extracellular H O . Among all molecules tested, DPI elicited dose-dependent inhibition of all isoforms in all assays, however all other molecules tested displayed interesting pharmacological characteristics, but did not meet criteria for bona fide NOX inhibitors. Our findings indicate that experimental results obtained with widely used NOX inhibitors must be carefully interpreted and highlight the challenge of developing reliable pharmacological inhibitors of these key molecular targets. NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O2•-) and/or hydrogen peroxide (H2O2). As major oxidant generators, NOX are associated with oxidative damage in numerous diseases and represent promising drug targets for several pathologies. Various small molecule NOX inhibitors are used in the literature, but their pharmacological characterization is often incomplete in terms of potency, specificity and mode of action.BACKGROUNDNADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O2•-) and/or hydrogen peroxide (H2O2). As major oxidant generators, NOX are associated with oxidative damage in numerous diseases and represent promising drug targets for several pathologies. Various small molecule NOX inhibitors are used in the literature, but their pharmacological characterization is often incomplete in terms of potency, specificity and mode of action.We used cell lines expressing high levels of human NOX isoforms (NOX1-5, DUOX1 and 2) to detect NOX-derived O2•- or H2O2 using a variety of specific probes. NOX inhibitory activity of diphenylene iodonium (DPI), apocynin, diapocynin, ebselen, GKT136901 and VAS2870 was tested on NOX isoforms in cellular and membrane assays. Additional assays were used to identify potential off target effects, such as antioxidant activity, interference with assays or acute cytotoxicity.EXPERIMENTAL APPROACHWe used cell lines expressing high levels of human NOX isoforms (NOX1-5, DUOX1 and 2) to detect NOX-derived O2•- or H2O2 using a variety of specific probes. NOX inhibitory activity of diphenylene iodonium (DPI), apocynin, diapocynin, ebselen, GKT136901 and VAS2870 was tested on NOX isoforms in cellular and membrane assays. Additional assays were used to identify potential off target effects, such as antioxidant activity, interference with assays or acute cytotoxicity.Cells expressing active NOX isoforms formed O2•-, except for DUOX1 and 2, and in all cases activation of NOX isoforms was associated with the detection of extracellular H2O2. Among all molecules tested, DPI elicited dose-dependent inhibition of all isoforms in all assays, however all other molecules tested displayed interesting pharmacological characteristics, but did not meet criteria for bona fide NOX inhibitors.KEY RESULTSCells expressing active NOX isoforms formed O2•-, except for DUOX1 and 2, and in all cases activation of NOX isoforms was associated with the detection of extracellular H2O2. Among all molecules tested, DPI elicited dose-dependent inhibition of all isoforms in all assays, however all other molecules tested displayed interesting pharmacological characteristics, but did not meet criteria for bona fide NOX inhibitors.Our findings indicate that experimental results obtained with widely used NOX inhibitors must be carefully interpreted and highlight the challenge of developing reliable pharmacological inhibitors of these key molecular targets.CONCLUSIONOur findings indicate that experimental results obtained with widely used NOX inhibitors must be carefully interpreted and highlight the challenge of developing reliable pharmacological inhibitors of these key molecular targets.
ArticleNumber	101272
Author	Doroshow, James Lam, Magdalena Mahiout, Zahia Augsburger, Fiona Maghzal, Ghassan Jaquet, Vincent Knaus, Ulla G. Krause, Karl-Heinz Rasti, Delphine Jansen-Dürr, Pidder Stocker, Roland Seredenina, Tamara Filippova, Aleksandra
AuthorAffiliation	a Department of Pathology and Immunology, Centre Médical Universitaire, Geneva, Switzerland b Institute for Biomedical Aging Research (IBA), University of Innsbruck, Innsbruck, Austria c Conway Institute, University College Dublin, Dublin, Ireland d National Cancer Institute, Bethesda, MD, 20816, USA f St Vincent's Clinical School, University of New South Wales, NSW, Australia e Victor Chang Cardiac Research Institute, Vascular Biology Division, 405 Liverpool Street, Darlinghurst, NSW, 2010, Australia
AuthorAffiliation_xml	– name: d National Cancer Institute, Bethesda, MD, 20816, USA – name: f St Vincent's Clinical School, University of New South Wales, NSW, Australia – name: a Department of Pathology and Immunology, Centre Médical Universitaire, Geneva, Switzerland – name: c Conway Institute, University College Dublin, Dublin, Ireland – name: e Victor Chang Cardiac Research Institute, Vascular Biology Division, 405 Liverpool Street, Darlinghurst, NSW, 2010, Australia – name: b Institute for Biomedical Aging Research (IBA), University of Innsbruck, Innsbruck, Austria
Author_xml	– sequence: 1 givenname: Fiona surname: Augsburger fullname: Augsburger, Fiona – sequence: 2 givenname: Aleksandra surname: Filippova fullname: Filippova, Aleksandra – sequence: 3 givenname: Delphine surname: Rasti fullname: Rasti, Delphine – sequence: 4 givenname: Tamara surname: Seredenina fullname: Seredenina, Tamara – sequence: 5 givenname: Magdalena surname: Lam fullname: Lam, Magdalena – sequence: 6 givenname: Ghassan surname: Maghzal fullname: Maghzal, Ghassan – sequence: 7 givenname: Zahia surname: Mahiout fullname: Mahiout, Zahia – sequence: 8 givenname: Pidder surname: Jansen-Dürr fullname: Jansen-Dürr, Pidder – sequence: 9 givenname: Ulla G. surname: Knaus fullname: Knaus, Ulla G. – sequence: 10 givenname: James surname: Doroshow fullname: Doroshow, James – sequence: 11 givenname: Roland surname: Stocker fullname: Stocker, Roland – sequence: 12 givenname: Karl-Heinz surname: Krause fullname: Krause, Karl-Heinz – sequence: 13 givenname: Vincent surname: Jaquet fullname: Jaquet, Vincent
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/31330481$$D View this record in MEDLINE/PubMed
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Keywords	Reactive oxygen species Small molecule inhibitors NADPH oxidase NOX
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Snippet	NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O ) and/or hydrogen peroxide (H O ). As major... NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O2•-) and/or hydrogen peroxide (H2O2). As major... Image 1 Background: NADPH oxidases (NOX) are a family of flavoenzymes that catalyze the formation of superoxide anion radical (O2•-) and/or hydrogen peroxide (H2O2)....
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SubjectTerms	Catalysis Cell Line Chromatography, Liquid Drug Discovery Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Humans Hydrogen Peroxide - metabolism Isoenzymes Leukocytes - drug effects Leukocytes - metabolism Metabolic Networks and Pathways - drug effects Models, Biological NADPH Oxidases - antagonists & inhibitors NADPH Oxidases - genetics NADPH Oxidases - metabolism Reactive Oxygen Species - metabolism Research Paper Structure-Activity Relationship Tandem Mass Spectrometry
Title	Pharmacological characterization of the seven human NOX isoforms and their inhibitors
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