A subset of N-substituted phenothiazines inhibits NADPH oxidases
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NADPH oxidases (NOXs) constitute a family of enzymes generating reactive oxygen species (ROS) and are increasingly recognized as interesting drug targets. Here we investigated the effects of 10 phenothiazine compounds on NOX activity using an extensive panel of assays to measure production of ROS (Amplex red, WST-1, MCLA) and oxygen consumption. Striking differences between highly similar phenothiazines were observed. Two phenothiazines without N-substitution, including ML171, did not inhibit NOX enzymes, but showed assay interference. Introduction of an aliphatic amine chain on the N atom of the phenothiazine B ring (promazine) conferred inhibitory activity toward NOX2, NOX4, and NOX5 but not NOX1 and NOX3. Addition of an electron-attracting substituent in position 2 of the C ring extended the inhibitory activity to NOX1 and NOX3, with thioridazine being the most potent inhibitor. In contrast, the presence of a methylsulfoxide group at the same position (mesoridazine) entirely abolished NOX-inhibitory activity. A cell-free NOX2 assay suggested that inhibition by N-substituted phenothiazines was not due to competition with NADPH. A functional implication of NOX-inhibitory activity of thioridazine was demonstrated by its ability to block redox-dependent myofibroblast differentiation. Our results demonstrate that NOX-inhibitory activity is not a common feature of all antipsychotic phenothiazines and that substitution on the B-ring nitrogen is crucial for the activity, whereas that on the second position of the C ring modulates it. Our findings contribute to a better understanding of NOX pharmacology and might pave the path to discovery of more potent and selective NOX inhibitors.
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NOX2 is the main NOX isoform in neutrophils and macrophages where it mediates the oxidative burst.
“NOX2 is the main NOX isoform in neutrophils and macrophages where it mediates the oxidative burst (198, 845).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [845]
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Zhang, L., Yang, X.-L., Yi, R., Wu, S., Li, Q., Hu, G., & Chen, Z. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14610 · Cited by 1 · see citing works
Methods to Measure Reactive Oxygen Species Production by NADPH Oxidases
Zielonka, J., & Juric, M. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_20
Xu, B., Luo, J., Pang, S., Tu, C., Hu, J., Zhao, J., Zhang, T., Guo, P., Zheng, W., Wang, Y., et al. (2026) · Bioactive Materials · doi:10.1016/j.bioactmat.2026.07.039
BindingDB Entry 50020295: NADPH Oxidases: From Molecular Mechanisms to Current Inhibitors.
BindingDB (2024) · UC San Diego · doi:10.7270/q2jm2g3p
- Authors
- Seredenina, T., Chiriano, G., Filippova, A., Nayernia, Z., Mahiout, Z., Fioraso-Cartier, L., Plastre, O., Scapozza, L., Krause, K.-H., & Jaquet, V.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Jaquet, Vincent
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2015-09
- Volume
- 86
- Pages
- 239-249
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W208812206
- Cited by
- 45
- References
- 47
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 6 · 2022: 2 · 2021: 1 · 2020: 6 · 2019: 6 · 2018: 3 · 2017: 5 · 2016: 6 · 2015: 1
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- Swiss innovation promotion agency CTI (KTI-9958.1 PFLS-LS)
- European Community׳s Framework program (Health-F2-2011-278611)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Phenothiazines and Benzothiazines Synthesis and Activities
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- NADPH oxidase, phenothiazines, thioridazine, mesoridazine, promazine, NOX2, NOX4, NADPH oxidase 5, reactive oxygen species, antipsychotic drugs, structure-activity relationship, myofibroblast differentiation, NOX inhibitors
- MeSH terms
- Animals, Cell Differentiation, Cricetulus, Drug Evaluation, Preclinical, Enzyme Inhibitors, Cricetinae, Humans, Oxidation-Reduction, Oxygen Consumption, Phenothiazines, Structure-Activity Relationship, CHO Cells, Reactive Oxygen Species, Oxidative Stress, NADPH Oxidases, Inhibitory Concentration 50, HEK293 Cells, Myofibroblasts
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