Cited by 216Genomics, phytochemicals, and oxidative stressHeme Oxygenase-1 and Carbon MonoxideImmune Response and Inflammation

The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.

Lipopolysaccharide-Induced Expression of NAD(P)H:Quinone Oxidoreductase 1 and Heme Oxygenase-1 Protects against Excessive Inflammatory Responses in Human Monocytes

Open access

Rushworth, Stuart A., MacEwan, David J., O’Connell, Maria A.·2008·The Journal of Immunology

DOI 10.4049/jimmunol.181.10.6730PMC PMC2923058

Open this paper in CoChat — free account Open PDF

Abstract

Monocytes play a central role in the immunopathological effects of sepsis. This role is mediated by production of the cytokines TNF-α and IL-1β. The transcription factor NF-E2-related factor 2 (Nrf2) regulates innate immune responses in various experimental disease models. Presently, the role of Nrf2-regulated genes in LPS-treated human monocytes is not well defined. Herein we show that Nrf2 mediates a significant regulation of LPS-induced inflammatory responses. Analysis of Nrf2-regulated gene expression in human monocytes showed that LPS induced the expression of the phase II detoxification gene NAD(P)H:quinone oxidoreductase 1 (NQO1). Furthermore, NQO1 mRNA or protein expression in response to LPS was regulated by Nrf2. Silencing Nrf2 expression in human monocytes inhibited LPS-induced NQO1 expression; however, in contrast, it significantly increased TNF and IL-1β production. Silencing expression of NQO1 alone, or in combination with heme oxygenase-1 (HO-1) silencing, markedly increased LPS-induced TNF and IL-1β expression. Additionally, overexpression of NQO1 and/or HO-1 inhibited LPS-induced TNF and IL-1β expression. These results show for the first time that LPS induces NQO1 and HO-1 expression in human monocytes via Nrf2 to modulate their inflammatory responsiveness, thus providing novel potential therapeutic strategies for the treatment of sepsis.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.4049/jimmunol.181.10.6730

Cites

51 of 51 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Heat Shock Protein A12B Protects Vascular Endothelial Cells Against Sepsis-Induced Acute Lung Injury in Mice
Chen, Y., Wang, L., Kang, Q., Zhang, X., Yu, G., Wan, X., Wang, J., & Zhu, K. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000477308 · Cited by 10,730
The epidemiology of sepsis in the United States from 1979 through 2000
Martin, G. S., Mannino, D. M., Eaton, S., & Moss, M. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa022139 · Cited by 5,841
Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g.
Bøyum, A. (1968) · PubMed · Cited by 5,263
An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999
Targeting the KEAP1-NRF2 system to prevent kidney disease progression
Nezu, M., Suzuki, N., & Yamamoto, M. (2017) · American Journal of Nephrology · doi:10.1159/000475890 · Cited by 3,447
The immunopathogenesis of sepsis
Cohen, J. (2002) · Nature · doi:10.1038/nature01326 · Cited by 2,742
The Glomerular Permeability Determined by Dextran Clearance Using Sephadex Gel Filtration
Mogensen, C. E. (1968) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365516809076979 · Cited by 2,654
The Prevalence of Nosocomial Infection in Intensive Care Units in Europe
Vincent, J. (1995) · JAMA · doi:10.1001/jama.274.8.639 · Cited by 2,592
LPS induction of gene expression in human monocytes
Guha, M., & Mackman, N. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(00)00149-2 · Cited by 2,333
Transcription Factor Nrf2 Coordinately Regulates a Group of Oxidative Stress-inducible Genes in Macrophages
Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., & Yamamoto, M. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16023 · Cited by 1,473

Show all 51 references

Sorted by citations

Transcriptional Regulation by Nrf2
Tonelli, C., Chio, I. I. C., & Tuveson, D. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7342 · Cited by 2,280
The Nrf2 regulatory network provides an interface between redox and intermediary metabolism
Hayes, J. D., & Dinkova‐Kostova, A. T. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.002 · Cited by 2,210
NRF2, a Transcription Factor for Stress Response and Beyond
He, F., Ru, X., & Wen, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134777 · Cited by 1,820
An Overview of Nrf2 Signaling Pathway and Its Role in Inflammation
Saha, S., Buttari, B., Panieri, E., Profumo, E., & Saso, L. (2020) · Molecules · doi:10.3390/molecules25225474 · Cited by 1,460
Role of Glutathione in Cancer Progression and Chemoresistance
Traverso, N., Ricciarelli, R., Nitti, M., Marengo, B., Furfaro, A. L., Pronzato, M. A., Marinari, U. M., & Domenicotti, C. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/972913 · Cited by 1,208
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130
Reactive Oxygen Species: Drivers of Physiological and Pathological Processes
Checa, J., & Aran, J. M. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s275595 · Cited by 1,060
NRF2 and NF-қB interplay in cerebrovascular and neurodegenerative disorders: Molecular mechanisms and possible therapeutic approaches
Sivandzade, F., Prasad, S., Bhalerao, A., & Cucullo, L. (2019) · Redox Biology · doi:10.1016/j.redox.2018.11.017 · Cited by 639
When NRF2 Talks, Who's Listening?
Wakabayashi, N., Slocum, S. L., Skoko, J. J., Shin, S., & Kensler, T. W. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3216 · Cited by 595
Nrf2 in cancers: A double‐edged sword
Wu, S., Lu, H., & Bai, Y. (2019) · Cancer Medicine · doi:10.1002/cam4.2101 · Cited by 479
Proteasomal Degradation Is Transcriptionally Controlled by TCF11 via an ERAD-Dependent Feedback Loop
Steffen, J., Seeger, M., Koch, A., & Krüger, E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.012 · Cited by 366
Dissecting the Crosstalk Between Nrf2 and NF-κB Response Pathways in Drug-Induced Toxicity
Gao, W., Guo, L., Yang, Y., Wang, Y., Xia, S., Gong, H., Zhang, B., & Yan, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809952 · Cited by 358
NRF2 as a regulator of cell metabolism and inflammation in cancer
He, F., Antonucci, L., & Karin, M. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa039 · Cited by 332
Doxorubicin and other anthracyclines in cancers: Activity, chemoresistance and its overcoming
Mattioli, R., Ilari, A., Colotti, B., Mosca, L., Fazi, F., & Colotti, G. (2023) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2023.101205 · Cited by 323
The high Nrf2 expression in human acute myeloid leukemia is driven by NF-κB and underlies its chemo-resistance
Rushworth, S. A., Zaitseva, L., Murray, M. Y., Shah, N. M., Bowles, K. M., & MacEwan, D. J. (2012) · Blood · doi:10.1182/blood-2012-04-422121 · Cited by 290
Self-citation
Transcriptional profiling reveals developmental relationship and distinct biological functions of CD16+ and CD16- monocyte subsets
Ancuța, P., Liu, K., Misra, V., Wacleche, V. S., Gosselin, A., Zhou, X., & Gabuzda, D. H. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-403 · Cited by 284
Thirty years of NRF2: advances and therapeutic challenges.
Zhang, D. D. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01145-0 · Cited by 282
A review on heme oxygenase-1 induction: is it a necessary evil
Waza, A. A., Hamid, Z., Ali, S., Bhat, S. A., & Bhat, M. A. (2018) · Inflammation Research · doi:10.1007/s00011-018-1151-x · Cited by 243
Nrf2: A Potential Target for New Therapeutics in Liver Disease
Bataille, A. M., & Manautou, J. E. (2012) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2012.110 · Cited by 230
Nrf2 regulates ferroportin 1-mediated iron efflux and counteracts lipopolysaccharide-induced ferroportin 1 mRNA suppression in macrophages
Harada, N., Kanayama, M., Maruyama, A., Yoshida, A., Tazumi, K., Hosoya, T., Mimura, J., Toki, T., Maher, J. M., Yamamoto, M. P., et al. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.02.001 · Cited by 236
Molecular and cellular paradigms of multidrug resistance in cancer
Vaidya, F. U., Chhipa, A. S., Mishra, V., Gupta, V. K., Rawat, S. G., Kumar, A., & Pathak, C. (2020) · Cancer Reports · doi:10.1002/cnr2.1291 · Cited by 215
NADPH Oxidase-Dependent Reactive Oxygen Species Mediate Amplified TLR4 Signaling and Sepsis-Induced Mortality in Nrf2-Deficient Mice
Kong, X., Thimmulappa, R. K., Kombairaju, P., & Biswal, S. S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902315 · Cited by 195
Potential Applications of NRF2 Inhibitors in Cancer Therapy
Panieri, E., & Saso, L. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8592348 · Cited by 189
Nrf2-Keap1 Signaling as a Potential Target for Chemoprevention of Inflammation-Associated Carcinogenesis
Kundu, J. K., & Surh, Y. (2010) · Pharmaceutical Research · doi:10.1007/s11095-010-0096-8 · Cited by 171
Effect of Redox Modulating NRF2 Activators on Chronic Kidney Disease
Choi, B.-H., Kang, K.-S., & Kwak, M. (2014) · Molecules · doi:10.3390/molecules190812727 · Cited by 164
Nobiletin and Derivatives: Functional Compounds from Citrus Fruit Peel for Colon Cancer Chemoprevention
Goh, J. X. H., Tan, L. T., Goh, J. K., Chan, K., Pusparajah, P., Lee, L., & Goh, B. H. (2019) · Cancers · doi:10.3390/cancers11060867 · Cited by 152
Nrf2 has a protective role against neuronal and capillary degeneration in retinal ischemia–reperfusion injury
Wei, Y., Gong, J., Yoshida, T., Eberhart, C. G., Xu, Z., Kombairaju, P., Sporn, M. B., Handa, J. T., & Duh, E. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.026 · Cited by 143
Anti-Inflammatory Mechanism of Compound K in Activated Microglia and Its Neuroprotective Effect on Experimental Stroke in Mice
Park, J., Shin, J. A., Jung, J.-S., Hyun, J., Le, T. K. V., Kim, D., Park, E., & Kim, H.-S. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.189035 · Cited by 142
Redox Control of Leukemia: From Molecular Mechanisms to Therapeutic Opportunities
Irwin, M. E., Valle, N. R.-D., & Chandra, J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4258 · Cited by 146
Ethanol-induced HO-1 and NQO1 Are Differentially Regulated by HIF-1α and Nrf2 to Attenuate Inflammatory Cytokine Expression
Yeligar, S. M., Machida, K., & Kalra, V. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.138636 · Cited by 140
Prolonged Neutrophil Dysfunction after Plasmodium falciparum Malaria Is Related to Hemolysis and Heme Oxygenase-1 Induction
Cunnington, A. J., Njie, M., Correa, S., Takem, E. N., Riley, E. M., & Walther, M. R. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201028 · Cited by 126
Anti-inflammatory Effect of a Cell-Penetrating Peptide Targeting the Nrf2/Keap1 Interaction
Steel, R., Cowan, J., Payerne, E., O'Connell, M. A., & Searcey, M. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300041g · Cited by 113
Self-citation
Effect of long-term human exposure to environmental heavy metals on the expression of detoxification and DNA repair genes
Al-Bakheet, S. A., Attafi, I. M., Maayah, Z. H., Abd‐Allah, A. R. A., Asiri, Y. A., & Korashy, H. M. (2013) · Environmental Pollution · doi:10.1016/j.envpol.2013.06.014 · Cited by 99
S100A9-RAGE Axis Accelerates Formation of Macrophage-Mediated Extracellular Vesicle Microcalcification in Diabetes Mellitus
Kawakami, R., Katsuki, S., Travers, R. J., Romero, D., BECKER-GREENE, D. R., Passos, L. S. A., Higashi, H., Blaser, M. C., Sukhova, G. K., Buttigieg, J. A., et al. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.314087 · Cited by 105
Dysregulation of NRF2 in Cancer: from Molecular Mechanisms to Therapeutic Opportunities
Jung, B.-J., Yoo, H.-S., Shin, S., Park, Y., & Jeon, S. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.195 · Cited by 104
Ligustrazin increases lung cell autophagy and ameliorates paraquat-induced pulmonary fibrosis by inhibiting PI3K/Akt/mTOR and hedgehog signalling via increasing miR-193a expression
Liu, M.-W., Su, M.-X., Tang, D.-Y., Hao, L., Xun, X.-H., & Huang, Y.-Q. (2019) · BMC Pulmonary Medicine · doi:10.1186/s12890-019-0799-5 · Cited by 94
Structure–Activity and Structure–Property Relationship and Exploratory in Vivo Evaluation of the Nanomolar Keap1–Nrf2 Protein–Protein Interaction Inhibitor
Jiang, Z., Xu, L., Lu, M., Chen, Z., Yuan, Z., Xu, X., Guo, X., Zhang, X., Sun, H.-P., & You, Q. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00185 · Cited by 94
High basal nuclear levels of Nrf2 in acute myeloid leukemia reduces sensitivity to proteasome inhibitors
Rushworth, S. A., Bowles, K. M., & MacEwan, D. J. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3018 · Cited by 92
Self-citation
Marburgvirus Hijacks Nrf2-Dependent Pathway by Targeting Nrf2-Negative Regulator Keap1
Page, A., Volchkova, V. A., Reid, S. P., Mateo, M., Bagnaud-Baule, A., Nemirov, K., Shurtleff, A. C., Lawrence, P., Reynard, O., Ottmann, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.027 · Cited by 91
Novel roles of reactive oxygen species in the pathogenesis of acute myeloid leukemia
Zhou, F., Shen, Q., & Claret, F. X. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0113006 · Cited by 93
Cigarette smoke particle-phase extract induces HO-1 expression in human tracheal smooth muscle cells: Role of the c-Src/NADPH oxidase/MAPK/Nrf2 signaling pathway
Cheng, S.-E., Lee, I.-T., Lin, C.-C., Kou, Y. R., & Yang, C.-M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.026 · Cited by 86
Nobiletin and its colonic metabolites suppress colitis-associated colon carcinogenesis by down-regulating iNOS, inducing antioxidative enzymes and arresting cell cycle progression
Wu, X., Song, M., Gao, Z., Sun, Y., Wang, M., Li, F., Zheng, J., & Xiao, H. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.12.020 · Cited by 84
Inhibition of thioredoxin 1 leads to apoptosis in drug-resistant multiple myeloma
Raninga, P. V., Trapani, G. D., Vučković, S., Bhatia, M., & Tonissen, K. F. (2015) · Oncotarget · doi:10.18632/oncotarget.3795 · Cited by 83
Impaired antioxidant KEAP1-NRF2 system in amyotrophic lateral sclerosis: NRF2 activation as a potential therapeutic strategy
Bono, S., Feligioni, M., & Corbo, M. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00479-8 · Cited by 86
Targeting Cancer Stem Cell Redox Metabolism to Enhance Therapy Responses
Luo, M., & Wicha, M. S. (2018) · Seminars in Radiation Oncology · doi:10.1016/j.semradonc.2018.10.003 · Cited by 81
Cerebrovascular and Neurological Disorders: Protective Role of NRF2
Sivandzade, F., Bhalerao, A., & Cucullo, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143433 · Cited by 79
Nrf2 is a critical modulator of the innate immune response in a model of uveitis
Nagai, N., Thimmulappa, R. K., Cano, M., Fujihara, M., Izumi‐Nagai, K., Kong, X., Sporn, M. B., Kensler, T. W., Biswal, S. S., & Handa, J. T. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.04.033 · Cited by 79
Expression of heme oxygenase‐1 in human leukemic cells and its regulation by transcriptional repressor Bach1
Miyazaki, T., Kirino, Y., Takeno, M., Samukawa, S., Hama, M., Tanaka, M., Yamaji, S., Ueda, A., Tomita, N., Fujita, H., et al. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01550.x · Cited by 79
TNF Mediates the Sustained Activation of Nrf2 in Human Monocytes
Rushworth, S. A., Shah, S., & MacEwan, D. J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1004117 · Cited by 80
Self-citation
Protection of acute myeloid leukaemia cells from apoptosis induced by front-line chemotherapeutics is mediated by haem oxygenase-1
Heasman, S.-A., Zaitseva, L., Bowles, K. M., Rushworth, S. A., & MacEwan, D. J. (2011) · Oncotarget · doi:10.18632/oncotarget.321 · Cited by 77
Self-citation
Nrf2 activation supports cell survival during hypoxia and hypoxia/reoxygenation in cardiomyoblasts; the roles of reactive oxygen and nitrogen species
Kolamunne, R. T., Dias, I. H. K., Vernallis, A. B., Grant, M. M., & Griffiths, H. R. (2013) · Redox Biology · doi:10.1016/j.redox.2013.08.002 · Cited by 76
Redox Control of the Ubiquitin-Proteasome System: From Molecular Mechanisms to Functional Significance
Kriegenburg, F., Poulsen, E. G., Koch, A., Krüger, E., & Hartmann‐Petersen, R. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3590 · Cited by 77
Oxidative Stress Responses and NRF2 in Human Leukaemia
Abdul-Aziz, A. M., MacEwan, D. J., Bowles, K. M., & Rushworth, S. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/454659 · Cited by 73
Self-citation
Pistachio hull polysaccharide protects Nile tilapia against LPS-induced excessive inflammatory responses and oxidative stress, possibly via TLR2 and Nrf2 signaling pathways
Mohammadi, G., Karimi, A. A., Hafezieh, M., Dawood, M. A. O., & Abo‐Al‐Ela, H. G. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.12.042 · Cited by 70
Gamma-oryzanol Prevents LPS-induced Brain Inflammation and Cognitive Impairment in Adult Mice
Mastinu, A., Bonini, S. A., Rungratanawanich, W., Aria, F., Marziano, M., Maccarinelli, G., Abate, G., Premoli, M., Memo, M., & Uberti, D. L. (2019) · Nutrients · doi:10.3390/nu11040728 · Cited by 72
Nonalcoholic steatohepatitis and mechanisms by which it is ameliorated by activation of the CNC-bZIP transcription factor Nrf2
Bathish, B., Robertson, H., Dillon, J. F., Dinkova‐Kostova, A. T., & Hayes, J. D. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.226 · Cited by 68
Mkp-1 cross-talks with Nrf2/Ho-1 pathway protecting against intestinal inflammation
Li, J., Wang, H., Zheng, Z.-H., Luo, L., Wang, P., Liu, K., Namani, A., Jiang, Z., Wang, X. J., & Tang, X. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.002 · Cited by 67
Anti-inflammatory effects of 4′-demethylnobiletin, a major metabolite of nobiletin
Wu, X., Song, M., Rakariyatham, K., Zheng, J., Guo, S., Tang, Z., Zhou, S., & Xiao, H. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.09.035 · Cited by 65
The Role of Nrf2 and Cytoprotection in Regulating Chemotherapy Resistance of Human Leukemia Cells
Rushworth, S. A., & MacEwan, D. J. (2011) · Cancers · doi:10.3390/cancers3021605 · Cited by 63
Self-citation
Flavolignans from Silymarin as Nrf2 Bioactivators and Their Therapeutic Applications
Vargas-Mendoza, N., Morales‐González, Á., Morales-Martínez, M., Soriano-Ursua, M. A., Delgado‐Olivares, L., Sandoval-Gallegos, E. M., Madrigal‐Bujaidar, E., Álvarez‐González, I., Madrigal‐Santillán, E., & Morales‐González, J. A. (2020) · Biomedicines · doi:10.3390/biomedicines8050122 · Cited by 66
Curcumin mitigates deoxynivalenol-induced intestinal epithelial barrier disruption by regulating Nrf2/p53 and NF-κB/MLCK signaling in mice
Cao, Z., Gao, J., Huang, W., Yan, J., Shan, A., & Gao, X. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113281 · Cited by 63
NF-κB–Inhibited Acute Myeloid Leukemia Cells Are Rescued from Apoptosis by Heme Oxygenase-1 Induction
Rushworth, S. A., Bowles, K. M., Raninga, P. V., & MacEwan, D. J. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3407 · Cited by 62
Self-citation
NQO1 Suppresses NF-κB–p300 Interaction to Regulate Inflammatory Mediators Associated with Prostate Tumorigenesis
Thapa, D., Meng, P., Bedolla, R. G., Reddick, R. L., Kumar, A. P., & Ghosh, R. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0562 · Cited by 62
Ginseng: a promising neuroprotective strategy in stroke
Rastogi, V., Santiago‐Moreno, J., & Doré, S. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00457 · Cited by 61
HIV-1 gp120 induces antioxidant response element-mediated expression in primary astrocytes: Role in HIV associated neurocognitive disorder
Reddy, P. V. B., Gandhi, N. H., Samikkannu, T., Saiyed, Z. M., Agudelo, M., Yndart, A., Khatavkar, P., & Nair, M. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.06.011 · Cited by 59
3-(2-Oxo-2-phenylethylidene)-2,3,6,7-tetrahydro-1H-pyrazino[2,1-a]isoquinolin-4(11bH)-one (compound 1), a novel potent Nrf2/ARE inducer, protects against DSS-induced colitis via inhibiting NLRP3 inflammasome
Wang, Y., Wang, H., Qian, C., Tang, J., Zhou, W., Liu, X., You, Q., & Hu, R. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.11.015 · Cited by 59
NQO1 inhibits the TLR-dependent production of selective cytokines by promoting IκB-ζ degradation
Kimura, A., Kitajima, M., Nishida, K., Serada, S., Fujimoto, M., Naka, T., Fujii‐Kuriyama, Y., Sakamato, S., Ito, T., Handa, H., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20172024 · Cited by 58
Auranofin, a Gold(I)-Containing Antirheumatic Compound, Activates Keap1/Nrf2 Signaling via Rac1/iNOS Signal and Mitogen-Activated Protein Kinase Activation
Kim, N., Oh, M., Park, H., & Kim, I. (2010) · Journal of Pharmacological Sciences · doi:10.1254/jphs.09330fp · Cited by 56
The role of Nrf2 in protection against Pb-induced oxidative stress and apoptosis in SH-SY5Y cells
Ye, F., Li, X., Li, L., Lyu, L., Yuan, J., & Chen, J. (2015) · Food and Chemical Toxicology · doi:10.1016/j.fct.2015.10.009 · Cited by 55
Redox Regulation of Lipopolysaccharide-mediated Sulfiredoxin Induction, Which Depends on Both AP-1 and Nrf2
Kim, H., Jung, Y., Shin, B. S., Kim, H., Song, H., Bae, S. H., Rhee, S. G., & Jeong, W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126839 · Cited by 56
Induction of Nrf2-mediated genes by Antrodia salmonea inhibits ROS generation and inflammatory effects in lipopolysaccharide-stimulated RAW264.7 macrophages
Yang, H., Lin, S.-W., Lee, C.-C., Lin, K., Liao, C.-H., Yang, T., Wang, H., Huang, H., Wu, C., & Hseu, Y. (2014) · Food & Function · doi:10.1039/c4fo00869c · Cited by 53
Pyrocatechol, a component of coffee, suppresses LPS-induced inflammatory responses by inhibiting NF-κB and activating Nrf2
Funakoshi‐Tago, M., Nonaka, Y., Tago, K., Takeda, M., Ishihara, Y., Sakai, A., Matsutaka, M., Kobata, K., & Tamura, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-59380-x · Cited by 53
HO-1hi patrolling monocytes protect against vaso-occlusion in sickle cell disease
Liu, Y., Jing, F., Yi, W., Mendelson, A., Shi, P., Walsh, R., Friedman, D. F., Minniti, C., Manwani, D., Chou, S. T., et al. (2018) · Blood · doi:10.1182/blood-2017-12-819870 · Cited by 51
A novel compound VSC 2 has anti‐inflammatory and antioxidant properties in microglia and in P arkinson's disease animal model
Lee, J. A., Kim, J. H., Woo, S. Y., Son, H. J., Han, S. H., Jang, B. K., Choi, J. W., Kim, D. J., Park, K. D., & Hwang, O. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12973 · Cited by 50
PBK/TOPK mediates promyelocyte proliferation via Nrf2-regulated cell cycle progression and apoptosis
LIU, Y., Liu, H., Huiqin, C., Song, B., ZHANG, W., & Zhang, W. (2015) · Oncology Reports · doi:10.3892/or.2015.4308 · Cited by 49
The functional role of sulforaphane in intestinal inflammation: a review
Wei, L., Zhang, J., Zheng, L., & Chen, Y. (2021) · Food & Function · doi:10.1039/d1fo03398k · Cited by 48
Schizandrin C exerts anti-neuroinflammatory effects by upregulating phase II detoxifying/antioxidant enzymes in microglia
Park, S. Y., Park, S. J., Park, T. G., Seetharaman, R., Lee, S.-J., & Choi, Y. W. (2013) · International Immunopharmacology · doi:10.1016/j.intimp.2013.06.032 · Cited by 48
Patrolling monocytes scavenge endothelial-adherent sickle RBCs: a novel mechanism of inhibition of vaso-occlusion in SCD
Liu, Y., Zhong, H., Bao, W., Mendelson, A., An, X., Shi, P. A., Chou, S. T., Manwani, D. G., & Yazdanbakhsh, K. (2019) · Blood · doi:10.1182/blood.2019000172 · Cited by 51
Adoptive Transfer of Heme Oxygenase-1 (HO-1)-Modified Macrophages Rescues the Nuclear Factor Erythroid 2-Related Factor (Nrf2) Antiinflammatory Phenotype in Liver Ischemia/Reperfusion Injury
Huang, J., Shen, X., Yue, S., Zhu, J., Gao, F., Zhai, Y., Busuttil, R. W., Ke, B., & Kupiec‐Weglinski, J. W. (2014) · Molecular Medicine · doi:10.2119/molmed.2014.00103 · Cited by 48
Phytoestrogens modulate hepcidin expression by Nrf2: Implications for dietary control of iron absorption
Bayele, H. K., Balesaria, S., & Srai, S. K. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.001 · Cited by 47
Histone Methyltransferase SET8 Epigenetically Reprograms Host Immune Responses to Assist Mycobacterial Survival
Singh, V., Prakhar, P., Rajmani, R. S., Mahadik, K., Borbora, S. M., & Balaji, K. N. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jix322 · Cited by 49
Isoliquiritigenin alleviates LPS/ D-GalN-induced acute liver failure by activating the PGC-1α/ Nrf2 pathway to reduce oxidative stress and inflammatory response
Wang, L., Wang, X., Kong, L., Wang, S., Huang, K., Wu, J., Wang, C., Sun, H., Liu, K., & Meng, Q. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108159 · Cited by 46
Radix puerariae extracts ameliorate paraquat-induced pulmonary fibrosis by attenuating follistatin-like 1 and nuclear factor erythroid 2p45-related factor-2 signalling pathways through downregulation of miRNA-21 expression
Liu, M., Liu, R., Wu, H., Li, Y., Su, M.-X., Dong, M.-N., Zhang, W., & Qian, C. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-016-0991-6 · Cited by 45
Nrf2 as a master regulator of tissue damage control and disease tolerance to infection
Soares, M. P., & Ribeiro, A. M. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150054 · Cited by 46
The molecular biology and therapeutic potential of Nrf2 in leukemia
Khodakarami, A., Adibfar, S., Karpisheh, V., Abolhasani, S., Jalali, P., Mohammadi, H., Navashenaq, J. G., Hojjat‐Farsangi, M., & Jadidi‐Niaragh, F. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02660-5 · Cited by 46
Inhibitory Effects of 4′-Demethylnobiletin, a Metabolite of Nobiletin, on 12-O-Tetradecanoylphorbol-13-acetate (TPA)-Induced Inflammation in Mouse Ears
Wu, X., Song, M., Rakariyatham, K., Zheng, J., Wang, M., Xu, F., Gao, Z., & Xiao, H. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b05156 · Cited by 44
CO/HO-1 Induces NQO-1 Expression via Nrf2 Activation
Kim, H. J., Zheng, M., Kim, S., Cho, J. J., Shin, C. H., Joe, Y., & Chung, H. (2011) · Immune Network · doi:10.4110/in.2011.11.6.376 · Cited by 46
Targeting macrophage polarization by Nrf2 agonists for treating various xenobiotics-induced toxic responses
Wang, Y., Zhang, X., Meng, F.-G., & Zeng, T. (2021) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2021.1894624 · Cited by 40
Escherichia coli and Staphylococcus aureus Differentially Regulate Nrf2 Pathway in Bovine Mammary Epithelial Cells: Relation to Distinct Innate Immune Response
Ying, Y.-T., Yang, J., Tan, X., Liu, R., Zhuang, Y., Xu, J.-X., & Ren, W. (2021) · Cells · doi:10.3390/cells10123426 · Cited by 40
The Tobacco Smoke Component, Acrolein, Suppresses Innate Macrophage Responses by Direct Alkylation of c-Jun N-Terminal Kinase
Hristova, M., Spiess, P. C., Kasahara, D. I., Randall, M. J., Deng, B., & van der Vliet, A. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0134oc · Cited by 40
Nuclear factor erythroid 2-related factor 2 is a critical target for the treatment of glucocorticoid-resistant lupus nephritis
Ebihara, S., TAJIMA, H., & Ono, M. (2016) · Arthritis Research & Therapy · doi:10.1186/s13075-016-1039-5 · Cited by 39
Corynoline Isolated from Corydalis bungeana Turcz. Exhibits Anti-Inflammatory Effects via Modulation of Nfr2 and MAPKs
Yang, C., Zhang, C., Wang, Z., Tang, Z., Kuang, H., & Kong, A. T. (2016) · Molecules · doi:10.3390/molecules21080975 · Cited by 39
Punicalagin from pomegranate ameliorates TNF-α/IFN-γ-induced inflammatory responses in HaCaT cells via regulation of SIRT1/STAT3 axis and Nrf2/HO-1 signaling pathway
Huang, W., Liou, C., Shen, S., Hu, S., Chao, J. C.-J., Huang, C., & Wu, S. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.111665 · Cited by 36
Transcription factor Nrf2 suppresses LPS-induced hyperactivation of BV-2 microglial cells
Koh, K., Kim, J., Jang, Y. J., Yoon, K., Cha, Y., Lee, H. J., & Kim, J. (2011) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2011.01.004 · Cited by 36
Sulfosuccinimidyl oleate sodium is neuroprotective and alleviates stroke-induced neuroinflammation
Dhungana, H., Huuskonen, M. T., Jaronen, M., Lemarchant, S., Ali, H., Keksa-Goldsteine, V., Goldsteins, G., Kanninen, K. M., Koıstınaho, J., & Malm, T. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-1010-7 · Cited by 35
Ethyl gallate attenuates acute lung injury through Nrf2 signaling
Mehla, K., Balwani, S., Agrawal, A., & Ghosh, B. (2013) · Biochimie · doi:10.1016/j.biochi.2013.08.030 · Cited by 34
Heme oxygenase-1 prevents liver fibrosis in rats by regulating the expression of PPARγ and NF-κB
Yang, H. (2012) · World Journal of Gastroenterology · doi:10.3748/wjg.v18.i14.1680 · Cited by 34
Tert-butylhydroquinone ameliorates doxorubicin-induced cardiotoxicity by activating Nrf2 and inducing the expression of its target genes.
Wang, L., Su, S., Wang, L., Zhang, G., Zhang, R., Niu, Y., Guo, Y., Li, C., Jiang, W., Liu, Y., et al. (2015) · Europe PMC (PubMed Central) · Cited by 34
High NRF2 expression controls endoplasmic reticulum stress induced apoptosis in multiple myeloma
Sun, Y., Aziz, A., Bowles, K. M., & Rushworth, S. A. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.10.005 · Cited by 34
Self-citation
Methylated pentavalent arsenic metabolites are bifunctional inducers, as they induce cytochrome P450 1A1 and NAD(P)H:quinone oxidoreductase through AhR- and Nrf2-dependent mechanisms
Anwar‐Mohamed, A., Elshenawy, O. H., Soshilov, A. A., Denison, M. S., Le, X. C., Klotz, L., & El‐Kadi, A. O. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.810 · Cited by 33

Authors: Rushworth, S. A., MacEwan, D. J., & O’Connell, M. A.
Affiliations: University of East Anglia (GB)
School of Chemical Sciences and Pharmacy, University of East Anglia , Norwich,
ORCID: Rushworth, Stuart A.
MacEwan, David J.
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 2008-11
Volume: 181
Issue: 10
Pages: 6730-6737
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.181.10.6730
PMC: PMC2923058
OpenAlex: W2105691693
Cited by: 215
References: 51
Citations by year: 2026: 7 · 2025: 6 · 2024: 12 · 2023: 8 · 2022: 14 · 2021: 12 · 2020: 18 · 2019: 11 · 2018: 8 · 2017: 14 · 2016: 8 · 2015: 16 · 2014: 17 · 2013: 13 · 2012: 11
FWCI: 5.49
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
UEA Digital Repository (University of East Anglia) (submittedVersion)
Funders: University of East Anglia
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: lipopolysaccharide, NAD(P)H:quinone oxidoreductase 1, heme oxygenase-1, Nrf2, human monocytes, sepsis, inflammation, TNF-α, IL-1β, innate immunity
MeSH terms: Cell Line, Gene Expression Regulation, Humans, Inflammation, Lipopolysaccharides, Monocytes, RNA, Messenger, Tumor Necrosis Factor-alpha, Gene Expression, NAD(P)H Dehydrogenase (Quinone), Reactive Oxygen Species, Sepsis, Reverse Transcriptase Polymerase Chain Reaction, Gene Silencing, NF-E2-Related Factor 2, Heme Oxygenase-1, Interleukin-1beta

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Lipopolysaccharide-Induced Expression of NAD(P)H:Quinone Oxidoreductase 1 and Heme Oxygenase-1 Protects against Excessive Inflammatory Responses in Human Monocytes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks