The Quest for Selective Nox Inhibitors and Therapeutics: Challenges, Triumphs and Pitfalls

Cifuentes-Pagano, Eugenia; Meijles, Daniel N.; Pagano, Patrick J.

doi:10.1089/ars.2013.5620

Cited by 84Redox biology and oxidative stressNitric Oxide and Endothelin EffectsNeutrophil, Myeloperoxidase and Oxidative Mechanisms

The Quest for Selective Nox Inhibitors and Therapeutics: Challenges, Triumphs and Pitfalls

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Cifuentes-Pagano, Eugenia, Meijles, Daniel N., Pagano, Patrick J.·2014·Antioxidants & Redox Signaling

DOI 10.1089/ars.2013.5620PMC PMC4026400

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Abstract

Significance: Numerous studies in animal models and human subjects corroborate that elevated levels of reactive oxygen species (ROS) play a pivotal role in the progression of multiple diseases. As a major source of ROS in many organ systems, the NADPH oxidase (Nox) has become a prime target for therapeutic development. Recent Advances: In recent years, intense efforts have been dedicated to the development of pan- and isoform-specific Nox inhibitors as opposed to antioxidants that proved ineffective in clinical trials. Over the past decade, an array of compounds has been proposed in an attempt to fill this void. Critical Issues: Although many of these compounds have proven effective as Nox enzyme family inhibitors, isoform specificity has posed a formidable challenge to the scientific community. This review surveys the most prominent Nox inhibitors, and discusses potential isoform specificity, known mechanisms of action, and shortcomings. Some of these inhibitors hold substantial promise as targeted therapeutics. Future Directions: Increased insight into the mechanisms of action and regulation of this family of enzymes as well as atomic structures of key Nox subunits are expected to give way to a broader spectrum of more potent, efficacious, and specific molecules. These lead molecules will assuredly serve as a basis for drug development aimed at treating a wide array of diseases associated with increased Nox activity. Antioxid. Redox Signal. 20, 2741–2754.

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Most NOX inhibitors have shown poor specificity between isoforms, hampering progress in the field.
“Most of the inhibitors have shown poor specificity between isoforms, hampering the progress in the field (174).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [174]

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Adventitial delivery of dominant-negative p67phoxattenuates neointimal hyperplasia of the rat carotid artery
Weaver, M., Liu, J. J., Pimentel, D. R., Reddy, D. J., Harding, P., Peterson, E. L., & Pagano, P. J. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00690.2005 · Cited by 50 · see citing works
Self-citation
Isoform specific functions of Nox protein-derived reactive oxygen species in the vasculature
Schröder, K. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2010.01.002 · Cited by 48 · see citing works
Effects of antioxidant-rich foods on vascular reactivity: Review of the clinical evidence
Kay, C. D., Kris‐Etherton, P. M., & West, S. G. (2006) · Current Atherosclerosis Reports · doi:10.1007/s11883-006-0027-7 · Cited by 45 · see citing works
Nox4 as a potential therapeutic target for treatment of uremic toxicity associated to chronic kidney disease
Gorin, Y. C. (2013) · Kidney International · doi:10.1038/ki.2012.434 · Cited by 43 · see citing works
Effects of iodonium-class flavin dehydrogenase inhibitors on growth, reactive oxygen production, cell cycle progression, NADPH oxidase 1 levels, and gene expression in human colon cancer cells and xenografts
Doroshow, J. H., Gaur, S., Markel, S., Lu, J., van Balgooy, J. N. A., Synold, T. W., Xi, B., Wu, X., & Juhasz, A. N. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.002 · Cited by 43 · see citing works
Bridged tetrahydroisoquinolines as selective NADPH oxidase 2 (Nox2) inhibitors
Cifuentes-Pagano, E., Saha, J., Csányi, G., Ghouleh, I. A., Sahoo, S., Rodriguez, A. I., Wipf, P., Pagano, P. J., & Skoda, E. M. (2013) · MedChemComm · doi:10.1039/c3md00061c · Cited by 39 · see citing works
Self-citation
Strategies for identifying synthetic peptides to act as inhibitors of NADPH oxidases, or “All that you did and did not want to know about Nox inhibitory peptides”
Dahan, I. M., & Pick, E. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1007-4 · Cited by 36 · see citing works
A novel synthetic compound, 3-amino-3-(4-fluoro-phenyl)-1H-quinoline-2,4-dione, inhibits cisplatin-induced hearing loss by the suppression of reactive oxygen species: In vitro and in vivo study
Shin, Y. S., Song, S., Kang, S. U., Hwang, H. S., Choi, J. W., Lee, B. H., Jung, Y. S., & Kim, C. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.12.008 · Cited by 36 · see citing works
NOX enzymes in immuno-inflammatory pathologies
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Rac-Dependent Monocyte Chemoattractant Protein-1 Production Is Induced by Nutrient Deprivation
Lopes, N. H. M., Vasudevan, S. S., Gregg, D., Selvakumar, B., Pagano, P. J., Kovacic, H., & Goldschmidt‐Clermont, P. J. (2002) · Circulation Research · doi:10.1161/01.res.0000040421.54108.81 · Cited by 35 · see citing works
Self-citation
Role of gp91phox-containing NADPH oxidase in the deoxycorticosterone acetate-salt-induced hypertension
Fujii, A., Nakano, D., Katsuragi, M., Ohkita, M., Takaoka, M., Ohno, Y., & Matsumura, Y. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.09.039 · Cited by 32 · see citing works
High-fat Diet Increases and the Polyphenol, S17834, Decreases Acetylation of the Sirtuin-1–dependent Lysine-382 on p53 and Apoptotic Signaling in Atherosclerotic Lesion–prone Aortic Endothelium of Normal Mice
Xu, S., Jiang, B., Hou, X., Shi, C., Bachschmid, M. M., Zang, M., Verbeuren, T. J., & Cohen, R. A. (2011) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e3182239eb7 · Cited by 32 · see citing works
Potential role of the "NADPH oxidases" (NOX/DUOX) family in cystic fibrosis.
Pongnimitprasert, N., Benna, J. E., Foglietti, M. J., Gougerot‐Pocidalo, M., Bernard, M., & Braut‐Boucher, F. (2008) · PubMed · doi:10.1684/abc.2008.0285 · Cited by 27 · see citing works
Towards specific NADPH oxidase inhibition by small synthetic peptides
Benna, J. E., Dang, P. M., & Périanin, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1008-3 · Cited by 24 · see citing works
Divergent Effects of p47 phox Phosphorylation at S303-4 or S379 on Tumor Necrosis Factor-α Signaling via TRAF4 and MAPK in Endothelial Cells
Teng, L., Fan, L. M., Meijles, D. N., & Li, J. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.112.247775 · Cited by 23 · see citing works
Self-citation
Inhibition of NADPH oxidase activation by peptides mapping within the dehydrogenase region of Nox2-A “peptide walking” study
Dahan, I. M., Molshanski-Mor, S., & Pick, E. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1011507 · Cited by 22 · see citing works
Strategies Aimed at Nox4 Oxidase Inhibition Employing Peptides from Nox4 B‐Loop and C‐Terminus and p22 <sup> <i>phox</i> </sup> N‐Terminus: An Elusive Target
Csányi, G., & Pagano, P. J. (2013) · International Journal of Hypertension · doi:10.1155/2013/842827 · Cited by 20 · see citing works
Self-citation
Nifedipine, a Calcium-Channel Blocker, Attenuated Glucose Intolerance and White Adipose Tissue Dysfunction in Type 2 Diabetic KK-Ay Mice
Iwai, M., Kanno, H., Inaba, S., Senba, I., Sone, H., Nakaoka, H., & Horiuchi, M. (2010) · American Journal of Hypertension · doi:10.1038/ajh.2010.198 · Cited by 19 · see citing works
Characterisation of Nox4 Inhibitors from Edible Plants
Kofler, P., Pircher, H., von Grafenstein, S., Diener, T., Höll, M., Liedl, K. R., Siems, K., & Jansen‐Dürr, P. (2013) · Planta Medica · doi:10.1055/s-0032-1328129 · Cited by 18 · see citing works
Inhibitory effects of a dihydropyridine calcium channel blocker on renal injury in aldosterone-infused rats
Fan, Y., Kohno, M., Nakano, D., Hitomi, H., Nagai, Y., Fujisawa, Y., Lu, X.-M., Fu, H., Du, J., Ohmori, K., et al. (2009) · Journal of Hypertension · doi:10.1097/hjh.0b013e32832dda6f · Cited by 18 · see citing works
Role of platelets in NOX2 activation mediated by TNFα in heart failure
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A Model of Interaction between Nicotinamide Adenine Dinucleotide Phosphate (NADPH) Oxidase and Apocynin Analogues by Docking Method
Jiang, J., Kang, H., Song, X., Huang, S., Li, S., & Xu, J. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14010807 · Cited by 12 · see citing works

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Oxidative stress in obstructive sleep apnea and intermittent hypoxia – Revisited – The bad ugly and good: Implications to the heart and brain
Lavie, L. (2014) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2014.07.003 · Cited by 692 · see citing works
Strategies to increase nitric oxide signalling in cardiovascular disease
Lundberg, J. O., Gladwin, M. T., & Weitzberg, E. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4623 · Cited by 576 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Oxidative stress in cancer and fibrosis: Opportunity for therapeutic intervention with antioxidant compounds, enzymes, and nanoparticles
Morry, J., Ngamcherdtrakul, W., & Yantasee, W. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.011 · Cited by 333 · see citing works
“Some issues with specificity, potency, and toxicity of these inhibitors have limited the use of these compounds in clinical studies [148].”
Oxidative Stress and Human Hypertension: Vascular Mechanisms, Biomarkers, and Novel Therapies
Montezano, A. C. I., Dulak-Lis, M. G., Tsiropoulou, S., Harvey, A., Briones, A. M., & Touyz, R. M. (2015) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2015.02.008 · Cited by 324 · see citing works
Teaching the basics of reactive oxygen species and their relevance to cancer biology: Mitochondrial reactive oxygen species detection, redox signaling, and targeted therapies
Kalyanaraman, B., Cheng, G., Hardy, M., Ouari, O., Bennett, B., & Zielonka, J. (2017) · Redox Biology · doi:10.1016/j.redox.2017.12.012 · Cited by 222 · see citing works
Redox Control of Skeletal Muscle Regeneration
Moal, E. L., Pialoux, V., Juban, G., Groussard, C., Zouhal, H., Chazaud, B., & Mounier, R. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6782 · Cited by 197 · see citing works
“(8 , 65)].”
Reduction-oxidation pathways involved in cancer development: a systematic review of literature reviews
Gao, X. Y., & Schöttker, B. (2017) · Oncotarget · doi:10.18632/oncotarget.17128 · Cited by 169 · see citing works
“However, most of them are not specific to NOX isoforms [91].”
Background
NADPH oxidases: key modulators in aging and age-related cardiovascular diseases?
Sahoo, S., Meijles, D. N., & Pagano, P. J. (2016) · Clinical Science · doi:10.1042/cs20150087 · Cited by 146 · see citing works
Self-citation
Lipotoxicity and β-Cell Failure in Type 2 Diabetes: Oxidative Stress Linked to NADPH Oxidase and ER Stress
Vilas‐Boas, E. A., de Almeida, D. C., Roma, L. P., Ortis, F., & Carpinelli, Â. R. (2021) · Cells · doi:10.3390/cells10123328 · Cited by 143 · see citing works
Nox/Duox Family of NADPH Oxidases: Lessons from Knockout Mouse Models
Sirokmány, G., Donkó, Á., & Geiszt, M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.01.006 · Cited by 132 · see citing works
Oxidative stress and antioxidants in the pathophysiology of malignant melanoma
Obrador, E., Liu-Smith, F., Dellinger, R. W., Salvador, R., Meyskens, F. L., & Estrela, J. M. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0327 · Cited by 119 · see citing works
NADPH Oxidase 2 Regulates NLRP3 Inflammasome Activation in the Brain after Traumatic Brain Injury
Ma, M. W., Wang, J., Dhandapani, K. M., & Brann, D. W. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6057609 · Cited by 116 · see citing works
“Although apocynin inhibits NOX2 assembly [51–53] and requires NOX2 to elicit protection after cerebral infarction [54], apocynin also may produce anti-inflammatory and antioxidant effects independent of NOX2 [55, 56].”
Background
Evidence for the free radical/oxidative stress theory of ageing from the CHANCES consortium: a meta-analysis of individual participant data
Schöttker, B., Brenner, H., Jansen, E. H. J. M., Gardiner, J., Peasey, A., Kubínová, R., Pająk, A., Topór-Mądry, R., Tamošiūnas, A., Saum, K.-U., et al. (2015) · BMC Medicine · doi:10.1186/s12916-015-0537-7 · Cited by 107 · see citing works
“However, more research is needed towards isoform-specific NOX-inhibitors but there is optimism that such drugs will be available in the near future [38].”
Background
The matricellular protein TSP1 promotes human and mouse endothelial cell senescence through CD47 and Nox1
Meijles, D. N., Sahoo, S., Ghouleh, I. A., Amaral, J. H., Bienes-Martínez, R., Knupp, H. E., Attaran, S., Sembrat, J., Nouraie, M. S., Rojas, M. M., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aaj1784 · Cited by 97 · see citing works
“Accordingly, interest in Nox inhibitor development has intensified and therefore represents an opportunity to interrogate, with therapeutic translation, the link between ROS and aging (15).”
BackgroundSelf-citation
Redox signaling, Nox5 and vascular remodeling in hypertension
Montezano, A. C., Tsiropoulou, S., Dulak-Lis, M., Harvey, A., Camargo, L. D. L., & Touyz, R. M. (2015) · Current Opinion in Nephrology and Hypertension · doi:10.1097/mnh.0000000000000153 · Cited by 93 · see citing works
H2O2 Metabolism in Normal Thyroid Cells and in Thyroid Tumorigenesis: Focus on NADPH Oxidases
Szántó, I., Pusztaszeri, M. P., & Mavromati, M. (2019) · Antioxidants · doi:10.3390/antiox8050126 · Cited by 89 · see citing works
Ultrasensitive ROS-Responsive Coassemblies of Tellurium-Containing Molecules and Phospholipids
Wang, L., Fan, F., Cao, W., & Xu, H. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b04419 · Cited by 89 · see citing works
Microvascular NADPH oxidase in health and disease
Li, Y., & Pagano, P. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.049 · Cited by 79 · see citing works
“Apocynin was initially believed to inhibit Noxs by specifically preventing p47phox translocation to the plasma membrane [220].”
Self-citation
Obligatory role for GPER in cardiovascular aging and disease
Meyer, M. R., Fredette, N. C., Daniel, C., Sharma, G., Amann, K., Arterburn, J. B., Barton, M., & Prossnitz, E. R. (2016) · Science Signaling · doi:10.1126/scisignal.aag0240 · Cited by 78 · see citing works
The role of CD71+ erythroid cells in the regulation of the immune response
Grzywa, T. M., Nowis, D., & Gołąb, J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107927 · Cited by 78 · see citing works
Phagocyte-like NADPH oxidase [Nox2] in cellular dysfunction in models of glucolipotoxicity and diabetes
Kowluru, A., & Kowluru, R. A. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.017 · Cited by 76 · see citing works
Lipopolysaccharide (LPS)-mediated Angiopoietin-2-dependent Autocrine Angiogenesis Is Regulated by NADPH Oxidase 2 (Nox2) in Human Pulmonary Microvascular Endothelial Cells
Menden, H. L., Welak, S. R., Cossette, S. M., Ramchandran, R., & Sampath, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600692 · Cited by 69 · see citing works
NOX-driven ROS formation in cell transformation of FLT3-ITD-positive AML
Jayavelu, A. K., Moloney, J. N., Böhmer, F., & Cotter, T. G. (2016) · Experimental Hematology · doi:10.1016/j.exphem.2016.08.008 · Cited by 69 · see citing works
Mitigation of NADPH Oxidase 2 Activity as a Strategy to Inhibit Peroxynitrite Formation
Zielonka, J., Zielonka, M., VerPlank, L., Cheng, G., Hardy, M., Ouari, O., Ayhan, M. M., Podsiadły, R., Sikora, A., Lambeth, J. D., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.702787 · Cited by 67 · see citing works
NADPH oxidases: Pathophysiology and therapeutic potential in age-associated pulmonary fibrosis
Kato, K., & Hecker, L. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101541 · Cited by 67 · see citing works
Mitochondrial signaling in the vascular endothelium: beyond reactive oxygen species
Kadlec, A. O., Beyer, A., Ait‐Aissa, K., & Gutterman, D. D. (2016) · Basic Research in Cardiology · doi:10.1007/s00395-016-0546-5 · Cited by 59 · see citing works
“Reports that mitochondrial ROS interact with other ROS-producing sites, such as the NADPH oxidase isoforms [19], underscore the complexity of ROS signaling and the importance of targeted antioxidants [13].”
Targeted Treatment of Metastatic Breast Cancer by PLK1 siRNA Delivered by an Antioxidant Nanoparticle Platform
Morry, J., Ngamcherdtrakul, W., Gu, S., Reda, M. M., Castro, D. J., Sangvanich, T., Gray, J. W., & Yantasee, W. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0644 · Cited by 62 · see citing works
“Nevertheless, these agents are not used in clinics for such purposes due to the inability to achieve sufficient cellular NAC levels based on the current prescribed dose (18) and the challenge of getting specificity to particular NOX isoforms (19).”
Background
Subpicomolar diphenyleneiodonium inhibits microglial NADPH oxidase with high specificity and shows great potential as a therapeutic agent for neurodegenerative diseases
Wang, Q., Chu, C., Oyarzabal, E. A., Jiang, L., Chen, S., Wilson, B. C., Li, Q., & Hong, J. (2014) · Glia · doi:10.1002/glia.22724 · Cited by 57 · see citing works
NADPH oxidase-derived reactive oxygen species contribute to impaired cutaneous microvascular function in chronic kidney disease
DuPont, J. J., Ramick, M. G., Farquhar, W. B., Townsend, R. R., & Edwards, D. G. (2014) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00058.2014 · Cited by 56 · see citing works
Nox Inhibitors & Therapies: Rational Design of Peptidic and Small Molecule Inhibitors
Cifuentes-Pagano, E., Meijles, D. N., & Pagano, P. J. (2015) · Current Pharmaceutical Design · doi:10.2174/1381612821666151029112013 · Cited by 55 · see citing works
Self-citation
The Impact of the Renin-Angiotensin-Aldosterone System on Inflammation, Coagulation, and Atherothrombotic Complications, and to Aggravated COVID-19
Ekholm, M., & Kahan, T. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.640185 · Cited by 56 · see citing works
Targeting the Redox Landscape in Cancer Therapy
Narayanan, D., Ma, S., & Özcelik, D. (2020) · Cancers · doi:10.3390/cancers12071706 · Cited by 54 · see citing works
“Recent in vivo studies reported that the inhibition of NOXs hinders tumor growth, indicating the pharmaceutical relevance of NOXs; however, current NOX inhibitors lack selectivity among NOX isoforms [161,162].”
NADPH oxidase-generated reactive oxygen species in mature follicles are essential for Drosophila ovulation
Li, W., Young, J. F., & Sun, J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800115115 · Cited by 51 · see citing works
“Consistent with this conclusion, pretreatment of mature follicles with diphenyleneio-donium (DPI) or VAS2870, potent NOX enzymatic inhibitors (27), was sufficient to inhibit OA-induced follicle rupture in a dose-dependent manner ( SI Appendix , Fig.”
NADPH oxidase 2 inhibitors CPP11G and CPP11H attenuate endothelial cell inflammation & vessel dysfunction and restore mouse hind-limb flow
Li, Y., Cifuentes-Pagano, E., DeVallance, E., de Jesus, D. S., Sahoo, S., Meijles, D. N., Koes, D. R., Camacho, C. J., Ross, M., Croix, C. M. S., et al. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101143 · Cited by 50 · see citing works
Self-citation
Understanding the biology of reactive oxygen species and their link to cancer: NADPH oxidases as novel pharmacological targets
Harrison, I. P., & Selemidis, S. (2014) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12238 · Cited by 43 · see citing works
Lung epithelial NOX/DUOX and respiratory virus infections
Grandvaux, N., Mariani, M. K., & Fink, K. (2014) · Clinical Science · doi:10.1042/cs20140321 · Cited by 39 · see citing works
Apocynin and Tempol ameliorate dietary sodium-induced declines in cutaneous microvascular function in salt-resistant humans
Ramick, M. G., Brian, M. S., Matthews, E. L., Patik, J. C., Seals, D. R., Lennon, S. L., Farquhar, W. B., & Edwards, D. G. (2019) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00786.2018 · Cited by 38 · see citing works
“Thus a limitation of using apocynin is that it does not provide information on isoform specificity (8).”
Background
Nicotinamide Adenine Dinucleotide Phosphate Oxidase 2 Regulates LPS-Induced Inflammation and Alveolar Remodeling in the Developing Lung
Menden, H. L., Xia, S., Mabry, S. M., Navarro, A., Nyp, M. F., & Sampath, V. (2016) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2016-0006oc · Cited by 36 · see citing works
“Although the use of gp91phox ds-tat in an animal model of sepsis is new, these data are consistent with other reports that indicate NOX2-mediated injury in hypertension, diabetes, and inflammasome activation is inhibited with gp91phox ds-tat (31, 54, 55).”
BackgroundMethodResultInfluential
Different procedures of diphenyleneiodonium chloride addition affect neutrophil extracellular trap formation
Ostafin, M., Pruchniak, M. P., Ciepiela, O., Reznick, A. Z., & Demkow, U. A. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.05.003 · Cited by 35 · see citing works
Reaction of low-molecular-mass organoselenium compounds (and their sulphur analogues) with inflammation-associated oxidants
Carroll, L., Davies, M. J., & Pattison, D. I. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1018247 · Cited by 35 · see citing works
Les NADPH oxydases, Nox
Nguyen, M. V. C., Lardy, B., Paclet, M., Rousset, F., Berthier, S., Baillet, A. C., Grange, L., Gaudin, P., & Morel, F. (2015) · médecine/sciences · doi:10.1051/medsci/20153101012 · Cited by 30 · see citing works
Rac-dependent feedforward autoactivation of NOX2 leads to oxidative burst
Hoang, H. M., Johnson, H. E., & Heo, J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100982 · Cited by 29 · see citing works
Recent Developments in the Probes and Assays for Measurement of the Activity of NADPH Oxidases
Zielonka, J., Hardy, M., Michalski, R., Sikora, A., Zielonka, M., Cheng, G., Ouari, O., Podsiadły, R., & Kalyanaraman, B. (2017) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-017-0813-6 · Cited by 29 · see citing works
Sildenafil Protects Endothelial Cells From Radiation-Induced Oxidative Stress
Wortel, R. C., Mizrachi, A., Li, H., Markovsky, E., Enyedi, B., Jacobi, J. M., Brodsky, O., Cao, J., Lippert, A. R., Incrocci, L., et al. (2019) · The Journal of Sexual Medicine · doi:10.1016/j.jsxm.2019.08.015 · Cited by 25 · see citing works
NADPH oxidase: its potential role in promotion of pulmonary arterial hypertension
Peng, J.-J., Liu, B., Xu, J., Peng, J., & Luo, X. (2017) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-017-1359-2 · Cited by 24 · see citing works
“…inhibitors, including triazolopyrimidine derivatives (such as VAS2870 and VAS3947), pyrazolopyridine derivatives (such as GK-136901 and GKT137831), and peptidebased inhibitors (such as NOX2ds-tat and NOXA1ds) (Cifuentes-Pagano et al. 2012; Cifuentes-Pagano et al. 2014; Ranayhossaini et al. 2013).”
BackgroundInfluential
The Cross‐Talk between Polyphenols and the Target Enzymes Related to Oxidative Stress‐Induced Thyroid Cancer
Heydarzadeh, S., Kia, S. K., Zarkesh, M., Pakizehkar, S., Hosseinzadeh, S., & Hedayati, M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2724324 · Cited by 22 · see citing works
“NOX enzymes are recognized as valuable pharmacological targets in a variety of disease treatment [77 – 79].”
Functional Peptide-Loaded Gelatin Nanoparticles as Eyedrops for Cornea Neovascularization Treatment
Chu, Y.-C., Fang, H., Wu, Y., Tang, Y.-J., Hsieh, E.-H., She, Y., Chang, C.-Y., Lin, I., Chen, Y., Liu, G., et al. (2023) · International Journal of Nanomedicine · doi:10.2147/ijn.s398769 · Cited by 20 · see citing works
“It also effectively attenuated ischemia/reperfusion-induced myocardial injury by inhibiting ROS release.(45,46) Hachisuka et al reported that gp91ds-tat treatment reduced new blood vessel formation in a tissue-engineering chamber.”
Background
Suppression of NADPH oxidase attenuates hypoxia-induced dysfunctions of endothelial progenitor cells
Liu, B., Ren, K., Peng, J.-J., Li, T., Luo, X., Fan, C., Yang, J., & Peng, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.11.161 · Cited by 20 · see citing works
Beta-Cell-Specific Expression of Nicotinamide Adenine Dinucleotide Phosphate Oxidase 5 Aggravates High-Fat Diet-Induced Impairment of Islet Insulin Secretion in Mice
Bouzakri, K., Veyrat‐Durebex, C., Holterman, C. E., Arous, C., Barbieux, C., Bosco, D., Altirriba, J., Ahmed, M. A., Tournier, B. B., Gunton, J. E., et al. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7579 · Cited by 19 · see citing works
“In this respect, NOX enzymes are among the most promising molecules (17, 31).”
Resolving Contributions of Oxygen‐Consuming and ROS‐Generating Enzymes at the Synapse
Abdel‐Rahman, E. A., Mahmoud, A. M., Aaliya, A., Radwan, Y., Yasseen, B. A., AlOkda, A., Atwa, A., Elhanafy, E., Habashy, M., & Ali, S. S. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1089364 · Cited by 18 · see citing works
Hydrogen Peroxide Generation as an Underlying Response to High Extracellular Inorganic Phosphate (Pi) in Breast Cancer Cells
Lacerda‐Abreu, M. A., Russo-Abrahão, T., Rocco-Machado, N., Cosentino‐Gomes, D., Dick, C. F., Carvalho‐Kelly, L. F., Nascimento, M. T. C., Rocha-Vieira, T. C., & Meyer‐Fernandes, J. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810096 · Cited by 17 · see citing works
“The triazol pyrimidine derivative, VAS2870 (3-benzyl-7-(2-benzoxazolyl)thio-1,2,3-triazolo [4,5d]pyrimidine) is characterized as a NOX inhibitor, without antioxidant properties or attenuation of xanthine oxidase activity [37].”
Background
NOX2 in Alzheimer's and Parkinson's disease
Dustin, C. M., Shiva, S. S., Vazquez, A. L., Saeed, A., Pascoal, T. A., Cifuentes-Pagano, E., & Pagano, P. J. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103433 · Cited by 17 · see citing works
Self-citation
Dysfunction of endothelial progenitor cells in hyperlipidemic rats involves the increase of NADPH oxidase derived reactive oxygen species production
Li, T., Zhang, J.-J., Liu, B., Luo, X., Ma, Q., & Peng, J. (2016) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2016-0142 · Cited by 15 · see citing works
Targeting Oxidative Stress in Stroke
Bach, A. (2017) · Springer series in translational stroke research · doi:10.1007/978-3-319-45345-3_8 · Cited by 15 · see citing works
Peptide screen identifies a new NADPH oxidase inhibitor: impact on cell migration and invasion
Mousslim, M., Pagano, A., Andreotti, N., Garrouste, F. L., Thuault, S., Peyrot, V., Parat, F., Luis, J., Culcasi, M., Laurent, S., et al. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.10.011 · Cited by 14 · see citing works
High-Throughput Screening of NOX Inhibitors
Zielonka, J., Zielonka, M., Cheng, G., Hardy, M., & Kalyanaraman, B. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9424-3_25 · Cited by 14 · see citing works
Novel NADPH Oxidase-2 Inhibitors as Potential Anti-Inflammatory and Neuroprotective Agents
Juric, M., Rawat, V., Amaradhi, R., Zielonka, J., & Ganesh, T. (2023) · Antioxidants · doi:10.3390/antiox12091660 · Cited by 12 · see citing works
NADPH Oxidase: A Therapeutic Target for Hyperoxaluria-Induced Oxidative Stress – An Update
Joshi, S. N., & Khan, S. R. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0275 · Cited by 12 · see citing works
Ferroptosis in age-related vascular diseases: Molecular mechanisms and innovative therapeutic strategies
Dai, Y., Wei, X., Jiang, T., Wang, Q., Li, Y., Ruan, N., Luo, P., Huang, J., Yang, Y., Qi, Y., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116356 · Cited by 11 · see citing works
VAS3947 Induces UPR-Mediated Apoptosis through Cysteine Thiol Alkylation in AML Cell Lines
Dor, M. E., Dakik, H., Polomski, M., Haudebourg, E., Brachet‐Botineau, M., Gouilleux, F., Prié, G., Zibara, K., & Mazurier, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155470 · Cited by 10 · see citing works
A leading role for NADPH oxidase in an in-vitro study of experimental autoimmune encephalomyelitis
Seo, J., Hasan, M., Rahaman, K. A., Kang, M., Jung, B.-H., & Kwon, O. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.02.009 · Cited by 10 · see citing works
New Progress in the Molecular Regulations and Therapeutic Applications in Cardiac Oxidative Damage Caused by Pressure Overload
Shi, X., Dorsey, A., & Qiu, H. (2022) · Antioxidants · doi:10.3390/antiox11050877 · Cited by 9 · see citing works
Chemical synthesis of a reported p47phox/p22phox inhibitor and characterization of its instability and irreproducible activity
Zang, J., Cambet, Y., Jaquet, V., & Bach, A. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1075328 · Cited by 9 · see citing works
“Apocynin has been frequently used in the literature as a NOX2 inhibitor, but several studies have demonstrated reproducibility issues and lack of selectivity to NOX isoforms due to direct antioxidant and off-target effects (Wind et al., 2010; Cifuentes-Pagano et al., 2014; Altenhofer et al., 2015; Hirano et al., 2015;…”
Background
Redox Regulation of the Microcirculation
Kadlec, A. O., & Gutterman, D. D. (2019) · Comprehensive physiology · doi:10.1002/cphy.c180039 · Cited by 10 · see citing works
Redox Regulation of Microvascular Physiology and Pathophysiology: Insights into Therapeutic Strategies and Limitations
Bulger, D. A., Zhang, Z., Hu, R., Dave, E. K., Mehta, P. K., Griendling, K. K., & Valdivia, A. (2025) · Antioxidants and Redox Signaling · doi:10.1177/15230864251372607 · Cited by 7 · see citing works
Nox2ds-Tat, A Peptide Inhibitor of NADPH Oxidase, Exerts Cardioprotective Effects by Attenuating Reactive Oxygen Species During Ischemia/Reperfusion Injury
Chen, Q., Devine, I., Walker, S., Pham, H., Ondrasik, R. M., Patel, H., Chau, W. L., Parker, C. W., Bartol, K. D., Riahi, S., et al. (2016) · American Journal of Biomedical Sciences · doi:10.5099/aj160300208 · Cited by 7 · see citing works
Opening NADPH oxidase inhibitors for in vivo translation
Hecht, N., Terveer, N., Schollmayer, C., Holzgrabe, U., & Meinel, L. (2017) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2017.03.001 · Cited by 7 · see citing works
Electrophilic Nitro-Fatty Acids: Nitric Oxide and Nitrite-Derived Metabolic and Inflammatory Signaling Mediators
Freeman, B. Α., Pekarová, M., Rubbo, H., & Trostchansky, A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00016-8 · Cited by 7 · see citing works
Diphenyleneiodonium Triggers Cell Death of Acute Myeloid Leukemia Cells by Blocking the Mitochondrial Respiratory Chain, and Synergizes with Cytarabine
Dakik, H., Dor, M. E., Bourgeais, J., Kouzi, F., Hérault, O., Gouilleux, F., Zibara, K., & Mazurier, F. (2022) · Cancers · doi:10.3390/cancers14102485 · Cited by 7 · see citing works
“While DPI is widely used to prove NOX activity [10], it is a non-specific inhibitor of flavoproteins that can impede the activity of nitric oxide synthases (NOS), xanthine oxidases (XOS), and complexes I and III of the mitochondrial respiratory chain (MRC) [11–13].”
Isoform-Selective Nox Inhibitors: Advances and Future Perspectives
Dustin, C. M., Cifuentes-Pagano, E., & Pagano, P. J. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_21 · Cited by 5 · see citing works
Self-citation
Sphingosine-1-phosphate activates ICl,swell in ventricular myocytes via mitochondrial reactive oxygen production
Raucci, F. J., Mauro, A. G., Lesnefsky, E. J., & Baumgarten, C. M. (2025) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2025.11.009 · Cited by 2 · see citing works
Redox signaling in chronic airway diseases: pathogenic mechanisms and therapeutic implications
Cazzola, M., Rogliani, P., Calzetta, L., van Haren, F. M. P., Page, C. P., & Matera, M. G. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1734890 · Cited by 2 · see citing works
Redox Regulation of the Microcirculation
Kadlec, A. O., & Gutterman, D. D. (2020) · Comprehensive physiology · doi:10.1002/j.2040-4603.2020.tb00102.x · Cited by 2 · see citing works
“Inhibitors of Nox may be used to identify the role of particular isoforms in vascular regulation [see review (75) for more detail].”
Physiology, metabolism and redox mechanisms in chronic cardiac volume overload
Schnelle, M. (2016) · doi:10.53846/goediss-5960 · Cited by 2 · see citing works
Regional heterogeneity in vascular contractile dysfunction in diabetic mice
Sallam, N. A., & Laher, I. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05257-4 · Cited by 1 · see citing works
“S2) suggesting a non-specific, NADPH oxidase-independent, effect of apocynin [59, 60] that counteracted vasorelaxant factor(s) regulating the basal tone.”
Targeting traumatic brain injury via novel tetrahydrocarbazole derivatives: in silico design, synthesis, and in vitro evaluation of dual NADPH oxidase 2 and 4 inhibitors
Pathania, A. S., Badhai, K., Singh, N., Chopra, D. S., & Singh, D. (2026) · Future Medicinal Chemistry · doi:10.1080/17568919.2026.2669608 · Cited by 1 · see citing works
Redox distress in organ fibrosis: The role of noncoding RNAs
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Mechanisms of Action of Drugs for Treating Endothelial Dysfunction in Diabetes Mellitus
Nizami, H. L., & Banerjee, S. (2017) · Springer eBooks · doi:10.1007/978-3-319-60324-7_22 · Cited by 1 · see citing works
Legal Responses to Terrorism with Special Reference to the Position of Kuwait
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Papel da NADPH oxidase durante a insulite e a lipotoxicidade: estresse oxidativo, disfunção e morte de células beta pancreáticas.
Vilas‐Boas, E. A. (2020) · doi:10.11606/t.42.2020.tde-03012022-095722
“diferentes isoformas trouxeram resultados interessantes nos últimos anos (185-187).”
Background
NOX4-mediated oxidative stress in diabetic complications: Potential of natural products
Sharma, S. H. A. D., Mittal, A., & Choudhary, M. (2026) · Pharmacological Research - Natural Products · doi:10.1016/j.prenap.2026.100515 · Cited by 1 · see citing works
Novel derivatives of tetrahydrocarbazole as NADPH oxidase 2 and 4 inhibitors: in silico , synthesis, and in vitro evaluation
Pathania, A. S., Badhai, K., Singh, N., Chopra, D. S., & Singh, D. (2026) · Future Medicinal Chemistry · doi:10.1080/17568919.2026.2628561
Research progress in skin anti-aging drugs based on core pathological drivers
Wei, Y., Liang, C., Zhou, X., Yang, S., Yang, Y., Yang, Y., Troulis, M. J., Shen, C., Jin, Z., & Chen, Y. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103375

Isoform-Selective Nox Inhibitors: Advances and Future Perspectives
Dustin, C. M., Cifuentes-Pagano, E., & Pagano, P. J. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_21 · Cited by 5 · see citing works
Self-citation
The NADPH Oxidase Family and Its Inhibitors
Chocry, M., & Leloup, L. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7915 · Cited by 89 · see citing works
NADPH oxidase inhibitors: a decade of discovery from Nox2ds to HTS
Cifuentes-Pagano, E., Csányi, G., & Pagano, P. J. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1009-2 · Cited by 92 · see citing works
Self-citation
Evolution of nadph oxidase inhibitors: Selectivity and mechanisms for target engagement
Altenhöfer, S., Radermacher, K. A., Kleikers, P. W. M., Wingler, K., & Schmidt, H. H. H. W. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5814 · Cited by 521 · see citing works
Nox Inhibitors & Therapies: Rational Design of Peptidic and Small Molecule Inhibitors
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Self-citation

Authors: Cifuentes-Pagano, E., Meijles, D. N., & Pagano, P. J.
Affiliations: University of Pittsburgh (US)
ORCID: Cifuentes-Pagano, Eugenia
Meijles, Daniel N.
Pagano, Patrick J.
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2014-06
Volume: 20
Issue: 17
Pages: 2741-2754
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2013.5620
PMC: PMC4026400
OpenAlex: W2020068152
Cited by: 84
References: 179
Citations by year: 2026: 5 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 5 · 2020: 6 · 2019: 8 · 2018: 3 · 2017: 12 · 2016: 17 · 2015: 9 · 2014: 6
FWCI: 1.00
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)
Locations: Antioxidants and Redox Signaling (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: University of Pittsburgh
Hemophilia Center of Western Pennsylvania
National Institutes of Health (PO1-HL-103455)
National Heart, Lung, and Blood Institute (R01HL079207, P01HL103455, R01HL112914)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords: NADPH oxidase, NOX inhibitors, reactive oxygen species, isoform specificity, drug development, mechanism of action, targeted therapeutics
MeSH terms: Animals, Antioxidants, Cardiovascular Diseases, Disease Models, Animal, Enzyme Inhibitors, Humans, Reactive Oxygen Species, Oxidative Stress, NADPH Oxidases, Protein Isoforms

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