Cited by 407Genomics, phytochemicals, and oxidative stressHeme Oxygenase-1 and Carbon MonoxideInflammatory mediators and NSAID effects

The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.

Transcription Factor Nrf2 Regulates Inflammation by Mediating the Effect of 15-Deoxy-Δ12,14-Prostaglandin J2

Open access

Itoh, Ken, Mochizuki, Mie, Ishii, Yukio, Ishii, Tetsuro, Shibata, Takahiro, Kawamoto, Yoshiyuki, Kelly, Vincent, Sekizawa, Kiyohisa, Uchida, Koji, Yamamoto, Masayuki·2004·Molecular and Cellular Biology

DOI 10.1128/mcb.24.1.36-45.2004PMC PMC303336

Open this paper in CoChat — free account

Abstract

Activated macrophages express high levels of Nrf2, a transcription factor that positively regulates the gene expression of antioxidant and detoxication enzymes. In this study, we examined how Nrf2 contributes to the anti-inflammatory process. As a model system of acute inflammation, we administered carrageenan to induce pleurisy and found that in Nrf2-deficient mice, tissue invasion by neutrophils persisted during inflammation and the recruitment of macrophages was delayed. Using an antibody against 15-deoxy-Delta(12,14)-prostaglandin J(2) (15d-PGJ(2)), it was observed that macrophages from pleural lavage accumulate 15d-PGJ(2). We show that in mouse peritoneal macrophages 15d-PGJ(2) can activate Nrf2 by forming adducts with Keap1, resulting in an Nrf2-dependent induction of heme oxygenase 1 and peroxiredoxin I (PrxI) gene expression. Administration of the cyclooxygenase 2 inhibitor NS-398 to mice with carrageenan-induced pleurisy caused persistence of neutrophil recruitment and, in macrophages, attenuated the 15d-PGJ(2) accumulation and PrxI expression. Administration of 15d-PGJ(2) into the pleural space of NS-398-treated wild-type mice largely counteracted both the decrease in PrxI and persistence of neutrophil recruitment. In contrast, these changes did not occur in the Nrf2-deficient mice. These results demonstrate that Nrf2 regulates the inflammation process downstream of 15d-PGJ(2) by orchestrating the recruitment of inflammatory cells and regulating the gene expression within those cells.

Integrity signals

Registry

Crossref · 10.1128/mcb.24.1.36-45.2004

Cites

46 of 46 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Inhibition of Prostaglandin Synthesis as a Mechanism of Action for Aspirin-like Drugs
VANE, J. R. (1971) · Nature New Biology · doi:10.1038/newbio231232a0 · Cited by 8,605
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
Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Self-citation
The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation
Ricote, M., Li, A. C., Willson, T. M., Kelly, C. J., & Glass, C. K. (1998) · Nature · doi:10.1038/34178 · Cited by 3,525
PPAR-γ agonists inhibit production of monocyte inflammatory cytokines
Jiang, C., Ting, A. T., & Seed, B. (1998) · Nature · doi:10.1038/34184 · Cited by 2,899
Points of control in inflammation
Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738
Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153
Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
Self-citation
Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain.
Seibert, K., Zhang, Y., Leahy, K., Hauser, S. D., Masferrer, J. L., Perkins, W., Lee, L., & Isakson, P. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12013 · Cited by 1,551
Nonsteroid drug selectivities for cyclo-oxygenase-1 rather than cyclo-oxygenase-2 are associated with human gastrointestinal toxicity: A full in vitro analysis
Warner, T. D., Giuliano, F., Vojnovic, I., Bukasa, A., Mitchell, J. A., & Vane, J. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7563 · Cited by 1,521

Flagged first, then by citations

Show all 46 references

Research works printed but not linked: 1

Narumiya S., 1987, J. Pharmacol. Exp. Ther., 242, 306

Sorted by citations

Items 101–200 of 406

Active defense under oxidative stress. The antioxidant responsive element
Lyakhovich, V. V., Андреевич, В. В., Зенков, Н. К., & Брониславовна, М. Е. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906090033 · Cited by 123
Flavonoids Activation of the Transcription Factor Nrf2 as a Hypothesis Approach for the Prevention and Modulation of SARS-CoV-2 Infection Severity
Mendonca, P., & Soliman, K. F. A. (2020) · Antioxidants · doi:10.3390/antiox9080659 · Cited by 126
Nrf Transcription Factors in Keratinocytes Are Essential for Skin Tumor Prevention but Not for Wound Healing
Keller, U. A. D., Huber, M., Beyer, T. A., Kümin, A., Siemes, C., Braun, S., Bugnon, P., Mitropoulos, V., Johnson, D. A., Johnson, J. A., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3773-3784.2006 · Cited by 122
“We showed that Nrf2 knockout mice have a prolonged inflammatory response after skin injury (3), most likely reflecting the important role of Nrf2 in macrophages ( 24 ).”
Background
Transcriptional network dynamics in macrophage activation
Nilsson, R., Bajić, V. B., Suzuki, H., di Bernardo, D., Björkegren, J., Katayama, S., Reid, J. F., Sweet, M. J., Gariboldi, M., Carninci, P., et al. (2006) · Genomics · doi:10.1016/j.ygeno.2006.03.022 · Cited by 123
“This prediction was recently independently validated by the groups of Ishii and Iizuka [35,36] using NRF-2 knockout mice.”
Method
Coordinate regulation of enzyme markers for inflammation and for protection against oxidants and electrophiles
Liu, H., Dinkova‐Kostova, A. T., & Talalay, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808346105 · Cited by 121
Nrf2 signaling and inflammation are key events in physical plasma-spurred wound healing
Schmidt, A., von Woedtke, T., Vollmar, B., Hasse, S., & Bekeschus, S. (2019) · Theranostics · doi:10.7150/thno.29754 · Cited by 120
Green Tea Polyphenol (-)-Epigallocatechin-3-Gallate (EGCG): A Time for a New Player in the Treatment of Respiratory Diseases?
Mokrá, D., Adamčáková, J., & Mokrý, J. (2022) · Antioxidants · doi:10.3390/antiox11081566 · Cited by 133
Role of 15-DeoxyΔ12,14 Prostaglandin J2 and Nrf2 Pathways in Protection against Acute Lung Injury
Mochizuki, M., Ishii, Y., Itoh, K., Iizuka, T., Morishima, Y., Kimura, T., Kiwamoto, T., Matsuno, Y., Hegab, A. E., Nomura, A., et al. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200406-755oc · Cited by 116
Self-citation
Characterization of lung inflammation and its impact on macrophage function in aging
Canan, C., Gokhale, N. S., Carruthers, B., Lafuse, W. P., Schlesinger, L., Torrelles, J., & Turner, J. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.4a0214-093rr · Cited by 106
Redox-Dependent Anti-Inflammatory Signaling Actions of Unsaturated Fatty Acids
Delmastro-Greenwood, M. M., Freeman, B. Α., & Wendell, S. G. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170341 · Cited by 117
Nrf2 Knockout Attenuates the Anti-Inflammatory Effects of Phenethyl Isothiocyanate and Curcumin
Boyanapalli, S. S. S., Paredes‐Gonzalez, X., Fuentes, F., Zhang, C., Guo, Y., Pung, D., Saw, C. L. L., & Kong, A. T. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500234h · Cited by 113
Nrf2 Neh5 domain is differentially utilized in the transactivation of cytoprotective genes
Zhang, J., Hosoya, T., Maruyama, A., Nishikawa, K., Maher, J. M., Ohta, T., Motohashi, H., Fukamizu, A., Shibahara, S., Itoh, K., et al. (2007) · Biochemical Journal · doi:10.1042/bj20061611 · Cited by 111
Self-citation
Transcriptional regulation via cysteine thiol modification: A novel molecular strategy for chemoprevention and cytoprotection
Na, H., & Surh, Y. (2006) · Molecular Carcinogenesis · doi:10.1002/mc.20225 · Cited by 111
“Sulforaphane Keap1-Cys151 [45] Keap1-Cys273 [43] Keap1-Cys278 [43] Keap1-Kelch domain [56] NF-kB [63] 6-Methylsulfinylhexyl isothiocyanate Keap1-Cys [64] Diallyltrisulfide Keap1-Cys [68] Tubulin-Cys12b [67] Tubulin-Cys354b [67] Zerumbone Keap1-Cys [76] Curcumin NF-kB-p50-Cys [77] Keap1-Cys [80] TrxR-Cys496 [79] Caffei…”
Background
Clinical review: Oxygen as a signaling molecule
Bartz, R. R., & Piantadosi, C. A. (2010) · Critical Care · doi:10.1186/cc9185 · Cited by 116
Amelioration of inflammation and tissue damage in sickle cell model mice by Nrf2 activation
Keleku-Lukwete, N., Suzuki, M., Otsuki, A., Tsuchida, K., Katayama, S., Hayashi, M., Naganuma, E., Moriguchi, T., Tanabe, O., Engel, J. D., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509158112 · Cited by 108
Self-citation
The KEAP1-NRF2 System and Neurodegenerative Diseases
Uruno, A., & Yamamoto, M. P. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0234 · Cited by 113
Self-citation
Accumulation of 15-deoxy-Δ12,14-prostaglandin J2 adduct formation with Keap1 over time: effects on potency for intracellular antioxidant defence induction
Oh, J. Y., Giles, N. M., Landar, A. L., & Darley-Usmar, V. M. (2008) · Biochemical Journal · doi:10.1042/bj20071189 · Cited by 106
Neuroinflammation and J2 prostaglandins: linking impairment of the ubiquitin-proteasome pathway and mitochondria to neurodegeneration
Figueiredo‐Pereira, M. E., Rockwell, P., Schmidt‐Glenewinkel, T., & Serrano, P. A. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00104 · Cited by 105
“…of the MAPK and JNK pathways (Wilmer et al., 2001; Li et al., 2004a), stabilization of the transcription factor Nrf2 via its interaction with Keap1 (Itoh et al., 2004; Kaspar et al., 2009; Haskew-Layton et al., 2013), and inhibition of the NFκB pathway (Rossi et al., 2000; Straus et al., 2000).”
Background
Current Landscape of NRF2 Biomarkers in Clinical Trials
Yagishita, Y., Gatbonton-Schwager, T. N., McCallum, M. L., & Kensler, T. W. (2020) · Antioxidants · doi:10.3390/antiox9080716 · Cited by 114
Activation of the Nrf2/antioxidant response pathway increases IL-8 expression
Zhang, X., Chen, X., Song, H., Chen, H., & Rovin, B. H. (2005) · European Journal of Immunology · doi:10.1002/eji.200526116 · Cited by 103
The NRF2/Keap1 pathway as a therapeutic target in inflammatory bowel disease
Geertsema, S., Bourgonje, A. R., Fagundes, R. R., Gaćeša, R., Weersma, R. K., van Goor, H., Mann, G. E., Dijkstra, G. D. H., & Faber, K. N. (2023) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2023.07.008 · Cited by 101
Role of microglial redox balance in modulation of neuroinflammation
Innamorato, N. G., Lastres‐Becker, I., & Cuadrado, A. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32832a3225 · Cited by 100
Respiratory Syncytial Virus Infection: Mechanisms of Redox Control and Novel Therapeutic Opportunities
Garofalo, R. P., Kolli, D., & Casola, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4307 · Cited by 103
Nrf2 regulates the alternative first exons of CD36 in macrophages through specific antioxidant response elements
Maruyama, A., Tsukamoto, S., Nishikawa, K., Yoshida, A., Harada, N., Motojima, K., Ishii, T., Nakane, A., Yamamoto, M. P., & Itoh, K. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.06.004 · Cited by 99
Self-citation
Maggot Extracts Alleviate Inflammation and Oxidative Stress in Acute Experimental Colitis via the Activation of Nrf2
Wang, R., Luo, Y., Lu, Y., Wang, D., Wang, T., Pu, W., & Wang, Y. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/4703253 · Cited by 97
Development of Neh2-Luciferase Reporter and Its Application for High Throughput Screening and Real-Time Monitoring of Nrf2 Activators
Smirnova, N. A., Haskew-Layton, R. E., Basso, M., Hushpulian, D. M., Payappilly, J. B., Speer, R. E., Ahn, Y., Rakhman, I., Cole, P. A., Pinto, J. T., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.03.013 · Cited by 96
“Canonical activators of Nrf2 such as 15-deoxy-prostaglandin J2 (15d-PGJ2) (Itoh et al., 2004), sulforaphane (Myzak and Dashwood, 2006), and tert-butylhydroquinone (TBHQ) (Moehlenkamp and Johnson, 1999) disrupt the interaction in the Neh2lucKeap1-Cul3 complex, leading to a measurable increase in…”
Background
Role of Nrf2 and p62/ZIP in the neurite outgrowth by carnosic acid in PC12h cells
Kosaka, K., Mimura, J., Itoh, K., Satoh, T., Shimojo, Y., Kitajima, C., Maruyama, A., Yamamoto, M. P., & Shirasawa, T. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp149 · Cited by 95
Self-citation
Identification of Novel Protein Targets for Modification by 15-Deoxy-Δ12,14-Prostaglandin J2 in Mesangial Cells Reveals Multiple Interactions with the Cytoskeleton
Stamatakis, K., Sánchez-Gómez, F. J., & Pérez‐Sala, D. (2005) · Journal of the American Society of Nephrology · doi:10.1681/asn.2005030329 · Cited by 95
Roles Nrf2 Plays in Myeloid Cells and Related Disorders
Kobayashi, E. H., Suzuki, T., & Yamamoto, M. P. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/529219 · Cited by 99
“Accumulating lines of recent evidence suggest that Nrf2 is also required for the primary functions ofmyeloid cells, which include phagocytosis, inflammation regulation, and ROS generation for bactericidal activities.”
BackgroundSelf-citation
The Keap1-Nrf2 Cellular Defense Pathway: Mechanisms of Regulation and Role in Protection Against Drug-Induced Toxicity
Copple, I. M., Goldring, C. E., Kitteringham, N. R., & Park, B. K. (2009) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-00663-0_9 · Cited by 98
NRF2 signalling in cytoprotection and metabolism
Murakami, S., Kusano, Y., Okazaki, K., Akaike, T., & Motohashi, H. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16246 · Cited by 91
“NRF2 exerts a potent anti-inflammatory function by accelerating resolution of acute inflammation (Itoh et al., 2004; Mochizuki et al., 2005) as well as alleviating chronic inflammation (Suzuki et al., 2017).”
Deletion of the Selenocysteine tRNA Gene in Macrophages and Liver Results in Compensatory Gene Induction of Cytoprotective Enzymes by Nrf2
Suzuki, T., Kelly, V. P., Motohashi, H., Nakajima, O., Takahashi, S., Nishimura, S., & Yamamoto, M. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708352200 · Cited by 92
Self-citation
An Overview of the Advantages of KEAP1-NRF2 System Activation During Inflammatory Disease Treatment
Keleku-Lukwete, N., Suzuki, M., & Yamamoto, M. P. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7358 · Cited by 90
Self-citation
Active NF-E2-related Factor (Nrf2) Contributes to Keep Endothelial NO Synthase (eNOS) in the Coupled State
Heiß, E. H., Schachner, D., Werner, E. R., & Dirsch, V. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.009175 · Cited by 89
Phospholipid oxidation generates potent anti‐inflammatory lipid mediators that mimic structurally related pro‐resolving eicosanoids by activating Nrf2
Bretscher, P., Egger, J., Shamshiev, A. T., Trötzmüller, M., Köfeler, H. C., Carreira, E. M., Köpf, M., & Freigang, S. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404702 · Cited by 88
Astaxanthin Treatment Confers Protection against Oxidative Stress in U937 Cells Stimulated with Lipopolysaccharide Reducing O2− Production
Franceschelli, S., Pesce, M., Ferrone, A., Lutiis, M. A. D., Patruno, A., Grilli, A., Felaco, M., & Speranza, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088359 · Cited by 88
The crosstalk between Nrf2 and NF-κB pathways in coronary artery disease: Can it be regulated by SIRT6?
Casper, E. A. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122007 · Cited by 87
Nrf2 signaling and redox homeostasis in the aging heart: A potential target to prevent cardiovascular diseases?
Silva‐Palacios, A., Königsberg, M., & Zazueta, C. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.12.005 · Cited by 84
“Once in the nucleus, Nrf2 binds to the antioxidant response element/electrophiles response element (ARE/EpRE) (Itoh et al., 2004).”
Background
The regulation of inflammation by oxidized phospholipids
Freigang, S. (2016) · European Journal of Immunology · doi:10.1002/eji.201545676 · Cited by 86
15-Deoxy-Δ12,14-prostaglandin J2 rescues PC12 cells from H2O2-induced apoptosis through Nrf2-mediated upregulation of heme oxygenase-1: Potential roles of Akt and ERK1/2
Kim, J., Li, M., Jang, J.-H., Na, H., Song, N., Lee, C., Johnson, J. A., & Surh, Y. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.08.007 · Cited by 83
Oxidants and Redox Signaling in Acute Lung Injury
Sarma, J. V., & Ward, P. A. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100068 · Cited by 86
NF‐E2‐related factor 2 regulates the stress response to UVA‐1‐oxidized phospholipids in skin cells
Gruber, F., Mayer, H., Lengauer, B., Mlitz, V., Sanders, J. M., Kadl, A., Bilban, M., de Martin, R., Wagner, O., Kensler, T. W., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-133520 · Cited by 80
“Nitrated unsaturated fatty acids (70) and 15deoxy- 12,14-prostaglandin J2, which bears similarities to structures in oxidized PAPC, can directly modify KEAP1 and thereby activate NRF2 and induce downstream genes (71).”
BackgroundSelf-citation
Keap1 is localized in neuronal and glial cytoplasmic inclusions in various neurodegenerative diseases
Tanji, K., Maruyama, A., Odagiri, S., Mori, F., Itoh, K., Kakita, A., Takahashi, H., & Wakabayashi, K. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31827b5713 · Cited by 80
Self-citation
Anti-Atherogenic Effect of Laminar Shear Stress via Nrf2 Activation
Takabe, W., Warabi, E., & Noguchi, N. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3433 · Cited by 82
GPx2 Counteracts PGE 2 Production by Dampening COX-2 and mPGES-1 Expression in Human Colon Cancer Cells
Banning, A., Florian, S., Deubel, S., Thalmann, S., Schmehl, K., Jacobasch, G., & Brigelius‐Flohé, R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2047 · Cited by 80
Prostanoids and Resolution of Inflammation – Beyond the Lipid-Mediator Class Switch
Schmid, T., & Brüne, B. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.714042 · Cited by 79
Nrf2 as molecular target for polyphenols: A novel therapeutic strategy in diabetic retinopathy
Nabavi, S. F., Barber, A. J., Spagnuolo, C., Russo, G. L., Daglia, M., Nabavi, S. M., & Sobarzo‐Sánchez, E. (2016) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2015.1129530 · Cited by 82
Heme oxygenase-1: a novel therapeutic target for gastrointestinal diseases
Naito, Y., Takagi, T., Uchiyama, K., & Yoshikawa, T. (2011) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.10-61 · Cited by 77
Calorie Restriction with a High-Fat Diet Effectively Attenuated Inflammatory Response and Oxidative Stress-Related Markers in Obese Tissues of the High Diet Fed Rats
Park, S., Park, N.-Y., Valacchi, G., & Lim, Y. (2012) · Mediators of Inflammation · doi:10.1155/2012/984643 · Cited by 77
Protein Thiol Modification by 15-deoxy-Δ12,14-Prostaglandin J2 Addition in Mesangial Cells: Role in the Inhibition of Pro-inflammatory Genes
Sánchez-Gómez, F. J., Cernuda‐Morollón, E., Stamatakis, K., & Pérez‐Sala, D. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.002824 · Cited by 76
Chlorogenic acid isomers directly interact with Keap 1-Nrf2 signaling in Caco-2 cells
Liang, N., Dupuis, J. H., Yada, R. Y., & Kitts, D. D. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03516-9 · Cited by 76
The Neuroprotection of Oxymatrine in Cerebral Ischemia/Reperfusion Is Related to Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2)-Mediated Antioxidant Response: Role of Nrf2 and Hemeoxygenase-1 Expression
Li, M., Zhang, X., Cui, L., Yang, R., Wang, L., Liu, L., & Du, W. (2011) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.34.595 · Cited by 76
Amelioration of Oxidative Stress in Caco-2 Cells Treated with Pro-inflammatory Proteins by Chlorogenic Acid Isomers via Activation of the Nrf2–Keap1–ARE-Signaling Pathway
Liang, N., & Kitts, D. D. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03983 · Cited by 75
Induction of Adaptive Response and Enhancement of PC12 Cell Tolerance by 7-Hydroxycholesterol and 15-Deoxy-Δ12,14-Prostaglandin J2 through Up-regulation of Cellular Glutathione via Different Mechanisms
Chen, Z.-H., Yoshida, Y., Saito, Y., Sekine, A., Noguchi, N., & Niki, E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600260200 · Cited by 73
Part of the Series: From dietary antioxidants to regulators in cellular signaling and gene regulation
Brigelius‐Flohé, R., & Banning, A. (2006) · Free Radical Research · doi:10.1080/10715760600722643 · Cited by 73
Induction of Hepatic Glutathione S-Transferases in Male Mice by Prototypes of Various Classes of Microsomal Enzyme Inducers
Knight, T. R., Choudhuri, S., & Klaassen, C. D. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn179 · Cited by 72
“A number of well-known responsive elements, such as glucocorticoid response element, xenobiotic response element, and antioxidant responsive element or electrophile responsive element (ARE/EpRE), are thought to mediate transcriptional regulation of Gsts (van Bladeren, 2000).”
BackgroundInfluential
Interdependence of Anti-Inflammatory and Antioxidant Properties of Squalene–Implication for Cardiovascular Health
Ibrahim, N. ‘., & Mohamed, I. N. (2021) · Life · doi:10.3390/life11020103 · Cited by 84
p-Hydroxybenzyl Alcohol Prevents Brain Injury and Behavioral Impairment by Activating Nrf2, PDI, and Neurotrophic Factor Genes in a Rat Model of Brain Ischemia
Kam, K.-Y., Yu, S. J., Jeong, N. H., Hong, J. H., Jalin, A. M. A. A., Lee, S., Choi, Y. W., Lee, C. K., & Kang, S. G. (2011) · Molecules and Cells · doi:10.1007/s10059-011-0028-4 · Cited by 71
“Overexpression of Nrf2 upregulates ARE-mediated expression of reporter genes that are inducible by various antioxidants and chemopreventive agents (Jeong et al., 2005).”
BackgroundInfluential
Regulation of Toll-like Receptor-Mediated Sestrin2 Induction by AP-1, Nrf2, and the Ubiquitin-Proteasome System in Macrophages
Kim, M. G., Yang, J. H., Kim, K. M., Jang, C. H., Jung, J. Y., Cho, I. J., Shin, S. M., & Ki, S. H. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv012 · Cited by 70
Identification of genes and molecular pathways involved in the progression of premalignant oral epithelia
Banerjee, A. G., Bhattacharyya, I., & Vishwanatha, J. K. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0033 · Cited by 71
Unique cistrome defined as CsMBE is strictly required for Nrf2-sMaf heterodimer function in cytoprotection
Otsuki, A., Suzuki, M., Katsuoka, F., Tsuchida, K., Suda, H., Morita, M., Shimizu, R., & Yamamoto, M. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.005 · Cited by 70
Self-citation
Dietary natural products as epigenetic modifiers in aging-associated inflammation and disease
Evans, L. W., Stratton, M. S., & Ferguson, B. S. (2020) · Natural Product Reports · doi:10.1039/c9np00057g · Cited by 71
Natural products as non-covalent and covalent modulators of the KEAP1/NRF2 pathway exerting antioxidant effects
Culletta, G., Buttari, B., Arese, M., Brogi, S., Almerico, A. M., Saso, L., & Tutone, M. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116355 · Cited by 73
Interaction with CREB binding protein modulates the activities of Nrf2 and NF-κB in cystic fibrosis airway epithelial cells
Ziady, A. G., Sokolow, A. G., Shank, S. L., Corey, D. A., Myers, R., Plafker, S. M., & Kelley, T. J. (2012) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00156.2011 · Cited by 71
15d-PGJ2 stimulates HO-1 expression through p38 MAP kinase and Nrf-2 pathway in rat vascular smooth muscle cells
Lim, H., Lee, K., Lee, S., Park, J., Choi, H., Go, S. H., Kwak, H. J., & Park, H. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.04.019 · Cited by 68
Δ12-Prostaglandin J2as a Product and Ligand of Human Serum Albumin: Formation of an Unusual Covalent Adduct at His146
Yamaguchi, S., Aldini, G., Ito, S., Morishita, N., Shibata, T., Vistoli, G., Carini, M., & Uchida, K. (2009) · Journal of the American Chemical Society · doi:10.1021/ja908878n · Cited by 67
Self-citation
A Generalizable Platform for Interrogating Target- and Signal-Specific Consequences of Electrophilic Modifications in Redox-Dependent Cell Signaling
Lin, H., Haegele, J. A., Disare, M. T., Lin, Q., & Aye, Y. (2015) · Journal of the American Chemical Society · doi:10.1021/ja5132648 · Cited by 65
Environmental Electrophiles: Protein Adducts, Modulation of Redox Signaling, and Interaction with Persulfides/Polysulfides
Kumagai, Y., & Abiko, Y. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00326 · Cited by 68
Data mining and systematic pharmacology to reveal the mechanisms of traditional Chinese medicine in Mycoplasma pneumoniae pneumonia treatment
Sun, J. H., Sun, F., Yan, B., Li, J. Y., & Xin, D. L. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.109900 · Cited by 65
An overview of the mechanisms and novel roles of Nrf2 in cardiovascular diseases
Jiang, S., Yang, Y., Li, T. X., Ma, Z., Hu, W., Deng, C., Fan, C., Lv, J., Sun, Y., & Yi, W. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2016.1250887 · Cited by 66
Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma
Mahaffey, C. M., Zhang, H., Rinna, A., Holland, W. S., Mack, P. C., & Forman, H. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.023 · Cited by 64
Hepatic Ischemia-Reperfusion Induces Renal Heme Oxygenase-1 via NF-E2-Related Factor 2 in Rats and Mice
Tanaka, Y., Maher, J. M., Chen, C., & Klaassen, C. D. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.029033 · Cited by 64
“The second is that inflammation increases the production of cyclopentenone prostaglandins, including 15-d-PGJ2 in kidneys, which binds to Keap1 in a manner that allows for Nrf2 release (Itoh et al., 2004).”
Background
Induction of the permeability transition and cytochrome c release by 15-deoxy-Δ12,14-prostaglandin J2 in mitochondria
Landar, A. L., Shiva, S., Levonen, A., Oh, J., Zaragoza, C., Johnson, M. S., & Darley-Usmar, V. M. (2006) · Biochemical Journal · doi:10.1042/bj20051259 · Cited by 63
Hypoxia and Heme Oxygenases: Oxygen Sensing and Regulation of Expression
Shibahara, S., Han, F., Li, B., & Takeda, K. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1784 · Cited by 62
Activation of Nrf2 signaling pathway by natural and synthetic chalcones: a therapeutic road map for oxidative stress
Egbujor, M. C., Saha, S., Buttari, B., Profumo, E., & Saso, L. (2021) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2021.1901578 · Cited by 63
“damage [43], redox signaling, protection against triptolideinduced oxidative stress [44], metabolism of carbohydrates [45], lipids and iron [46], and inflammation regulation [47].”
Dihydroquercetin (DHQ) ameliorated concanavalin A-induced mouse experimental fulminant hepatitis and enhanced HO-1 expression through MAPK/Nrf2 antioxidant pathway in RAW cells
Zhao, M., Chen, J., Zhu, P., Fujino, M., Takahara, T., Toyama, S., Tomita, A., Zhao, L., Yang, Z., Hei, M., et al. (2015) · International Immunopharmacology · doi:10.1016/j.intimp.2015.04.032 · Cited by 62
Keap1‐Nrf2 system regulates cell fate determination of hematopoietic stem cells
Murakami, S., Shimizu, R., Roméo, P., Yamamoto, M. P., & Motohashi, H. (2014) · Genes to Cells · doi:10.1111/gtc.12126 · Cited by 65
“In addition to the changes in the characteristics of macrophages by Nrf2 deletion, the macrophage influx into inflammatory sites is delayed in Nrf2 / mice, leading to the persistence of neutrophils (Itoh et al. 2004).”
BackgroundSelf-citation
Mechanistic insight into carnosol-mediated pharmacological effects: Recent trends and advancements
Kashyap, D., Kumar, G., Sharma, A. K., Sak, K., Tuli, H. S., & Mukherjee, T. K. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.11.013 · Cited by 63
Ochratoxin A-Induced Hepatotoxicity through Phase I and Phase II Reactions Regulated by AhR in Liver Cells
Shin, H. S., Lee, H. J., Pyo, M. C., Ryu, D., & Lee, K. (2019) · Toxins · doi:10.3390/toxins11070377 · Cited by 62
“The main regulator of the antioxidant defense system is NF-E2-related factor 2 (Nrf2) [19], which controls the expression of various antioxidant enzymes, such as heme oxygenase-1 (HO-1) [20], glutamate-cysteine ligase (GCL) [21], and NAD(P)H quinone dehydrogenase 1 (NQO1) [22].”
Background
Nrf2 regulates NGF mRNA induction by carnosic acid in T98G glioblastoma cells and normal human astrocytes
Mimura, J., Kosaka, K., Maruyama, A., Satoh, T., Harada, N., Yoshida, H., Satoh, K., Yamamoto, M. P., & Itoh, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr065 · Cited by 60
Self-citation
A possible protective role of Nrf2 in preeclampsia
Kweider, N., Huppertz, B., Kadyrov, M., Rath, W. H., Pufe, T., & Wruck, C. J. (2014) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2014.04.002 · Cited by 58
Protective effects of pyrroloquinoline quinone against oxidative stress-induced cellular senescence and inflammation in human renal tubular epithelial cells via Keap1/Nrf2 signaling pathway
Wang, Z., Han, N., Zhao, K., Li, Y., Chi, Y., & Wang, B. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.04.040 · Cited by 57
Stress-Induced Peroxiredoxins
Ishii, T., & Yanagawa, T. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-6051-9_18 · Cited by 57
Self-citation
Gene expression profiling for analysis acquired oxaliplatin resistant factors in human gastric carcinoma TSGH-S3 cells: The role of IL-6 signaling and Nrf2/AKR1C axis identification
Chen, C., Chu, C., Liu, K., Huang, C. F., Chang, J., Pan, W., Chen, H.-H., Cheng, Y.-H., Lee, K., Chen, M., et al. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.07.025 · Cited by 56
“To verify whether activation of the Nrf2 pathway in S3 cells reflected transactivation of other antioxidant response element (ARE)driven genes [30,35], mRNA levels of glutathione reductase (GR), thioredoxin reductase (TR), reduced glutathione biosynthetic enzymes glutamate cysteine ligase (g-glutamyl cysteine syntheta…”
Background
Adaptive HNE-Nrf2-HO-1 pathway against oxidative stress is associated with acute gastric mucosal lesions
Ueda, K., Ueyama, T., Yoshida, K., Kimura, H. M., Ito, T., Shimizu, Y., Oka, M., Tsuruo, Y., & Ichinose, M. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00204.2007 · Cited by 56
Involvement of the Nrf2/HO‐1/CO axis and therapeutic intervention with the CO‐releasing molecule CORM‐A1, in a murine model of autoimmune hepatitis
Mangano, K., Cavalli, E., Mammana, S., Basile, M. S., Caltabiano, R., Pesce, A., Puleo, S., Atanasov, A. G., Magro, G. G., Nicoletti, F., et al. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26223 · Cited by 55
“…pathway as an endogenous regulator of immunoinflammatory responses has been described in several experimental settings including LPS or carrageenan-induced lung injury (Itoh et al., 2004; Thimmulappa et al., 2006) and rodent retina after ischemia–reperfusion-induced damage (He et al., 2014).”
Background
Electrophilic Chemicals but not UV Irradiation or Reactive Oxygen Species Activate Nrf2 in Keratinocytes In Vitro and In Vivo
Durchdewald, M., Beyer, T. A., Johnson, D. A., Johnson, J. A., Werner, S., & Keller, U. A. D. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700585 · Cited by 53
3H-1,2-Dithiole-3-thione as a novel therapeutic agent for the treatment of ischemic stroke through Nrf2 defense pathway
Kuo, P., Yu, I.-C. I., Scofield, B. A., Brown, D. A., Curfman, E. T., Paraiso, H. C., Chang, F., & Yen, J.-H. J. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2017.01.018 · Cited by 52
Prostanoids with Cyclopentenone Structure as Tools for the Characterization of Electrophilic Lipid–Protein Interactomes
Stamatakis, K., & Pérez‐Sala, D. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1378.096 · Cited by 52
Inhibition of Activator Protein 1 Activation, Vascular Endothelial Growth Factor, and Cyclooxygenase-2 Expression by 15-Deoxy-Δ12,14-Prostaglandin J2 in Colon Carcinoma Cells: Evidence for a Redox-Sensitive Peroxisome Proliferator-Activated Receptor-γ-Independent Mechanism
Grau, R., Iñiguez, M. A., & Fresno, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0849 · Cited by 53
Sequestosome1/p62: A regulator of redox-sensitive voltage-activated potassium channels, arterial remodeling, inflammation, and neurite outgrowth
Ishii, T., Warabi, E., Siow, R. C. M., & Mann, G. E. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.019 · Cited by 52
Self-citation
4-Octyl Itaconate Regulates Immune Balance by Activating Nrf2 and Negatively Regulating PD-L1 in a Mouse Model of Sepsis
Zhang, P., Wang, Y., Yang, W., Yin, Y., Li, C., Ma, X., Shi, L., Li, R., & Tao, K. (2022) · International Journal of Biological Sciences · doi:10.2139/ssrn.4045961 · Cited by 52
Redox‐regulation of activator protein 1 family members in blood cancer cell lines exposed to cold physical plasma‐treated medium
Schmidt, A., Rödder, K., Hasse, S., Masur, K., Toups, L., Lillig, C. H., von Woedtke, T., Wende, K., & Bekeschus, S. (2016) · Plasma Processes and Polymers · doi:10.1002/ppap.201600090 · Cited by 50
Nutrigenomics: Concepts and Applications to Pharmacogenomics and Clinical Medicine
Kaput, J., Perlina, A., Hatipoğlu, B., Bartholomew, A. M., & Nikolsky, Y. (2007) · Pharmacogenomics · doi:10.2217/14622416.8.4.369 · Cited by 50
Close teamwork between Nrf2 and peroxiredoxins 1 and 6 for the regulation of prostaglandin D2 and E2 production in macrophages in acute inflammation
Ishii, T. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.034 · Cited by 52
Self-citation
Regulation of Signal Transduction by Glutathione Transferases
Pajaud, J., Kumar, S., Rauch, C., Morel, F., & Aninat, C. (2012) · International Journal of Hepatology · doi:10.1155/2012/137676 · Cited by 50
“15d-PGJ2 can also stimulate Nrf2-mediated induction of gene expression through the antioxidant response element [39, 40].”
Background
HDAC3 inhibition in diabetic mice may activate Nrf2 preventing diabetes-induced liver damage and FGF21 synthesis and secretion leading to aortic protection
Zhang, J., Xu, Z., Gu, J., Jiang, S., Liu, Q., Zheng, Y., Freedman, J. H., Sun, J., & Cai, L. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00465.2017 · Cited by 50
Nrf2 represses the onset of type 1 diabetes in non-obese diabetic mice
Yagishita, Y., Uruno, A., Chartoumpekis, D. V., Kensler, T. W., & Yamamoto, M. P. (2019) · Journal of Endocrinology · doi:10.1530/joe-18-0355 · Cited by 49
Self-citation
Therapeutics potentiating microglial p21-Nrf2 axis can rescue neurodegeneration caused by neuroinflammation
Nakano-Kobayashi, A., Fukumoto, A., Morizane, A., Nguyen, D. T., Le, T. M., Hashida, K., Hosoya, T., Takahashi, R., Takahashi, J. B., Hori, O., et al. (2020) · Science Advances · doi:10.1126/sciadv.abc1428 · Cited by 50
15-Deoxy-Δ12,14-Prostaglandin J2 Protects against Nitrosative PC12 Cell Death through Up-regulation of Intracellular Glutathione Synthesis
Lim, S.-Y., Jang, J.-H., Na, H., Lu, S. C.-L., Rahman, I., & Surh, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406555200 · Cited by 50

Authors: Itoh, K., Mochizuki, M., Ishii, Y., Ishii, T., Shibata, T., Kawamoto, Y., Kelly, V., Sekizawa, K., Uchida, K., & Yamamoto, M.
Affiliations: Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA) (JP)
Institute of Clinical Medicines
University of Tsukuba (JP)
Nagoya University (JP)
Institute of Social Medicines, University of Tsukuba, Tsukuba 305-8577
Corresponding author: Yamamoto, Masayuki
ORCID: Itoh, Ken
Ishii, Yukio
Shibata, Takahiro
Kawamoto, Yoshiyuki
Kelly, Vincent
Yamamoto, Masayuki
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2004-01-01
Volume: 24
Issue: 1
Pages: 36-45
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.24.1.36-45.2004
PMC: PMC303336
OpenAlex: W2113971187
Cited by: 407
References: 46
Citations by year: 2026: 4 · 2025: 8 · 2024: 9 · 2023: 13 · 2022: 13 · 2021: 21 · 2020: 20 · 2019: 20 · 2018: 21 · 2017: 21 · 2016: 24 · 2015: 23 · 2014: 14 · 2013: 21 · 2012: 11
FWCI: 6.55
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
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
Health Sciences › Medicine › Pharmacology (medical) › Inflammatory mediators and NSAID effects
Keywords: Nrf2, 15-deoxy-Δ12,14-prostaglandin J2, anti-inflammatory signaling, macrophages, neutrophil recruitment, carrageenan-induced pleurisy, Keap1, heme oxygenase-1, peroxiredoxin 1, cyclooxygenase-2, NS-398, acute inflammation, Nrf2-deficient mice
MeSH terms: Animals, DNA-Binding Proteins, Inflammation, Isoenzymes, Macrophages, Peritoneum, Pleurisy, Prostaglandin-Endoperoxide Synthases, Prostaglandin D2, Trans-Activators, Hepatocytes, NF-E2-Related Factor 2, Mice, Cyclooxygenase 2

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

Transcription Factor Nrf2 Regulates Inflammation by Mediating the Effect of 15-Deoxy-Δ12,14-Prostaglandin J2

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks