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

Show all 46 references

Research works printed but not linked: 1

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

Sorted by citations

Items 201–300 of 406

Modification of cysteine residues by cyclopentenone prostaglandins: Interplay with redox regulation of protein function
Oeste, C. L., & Pérez‐Sala, D. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21383 · Cited by 48
“Activation of Nrf2 by cyPG appears to play an important role in cyPG effects, since it has been reported that Nrf2 is required for the antiinflammatory actions of 15d-PGJ2 in some experimental systems (Itoh et al., 2004; Lin et al., 2012).”
Background
The cap’n’collar transcription factor Nrf2 mediates both intrinsic resistance to environmental stressors and an adaptive response elicited by chemopreventive agents that determines susceptibility to electrophilic xenobiotics
Higgins, L. G., & Hayes, J. D. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.09.025 · Cited by 49
Curcumin Alleviates IUGR Jejunum Damage by Increasing Antioxidant Capacity through Nrf2/Keap1 Pathway in Growing Pigs
Yan, E., Zhang, J., Han, H., Wu, J., Gan, Z., Wei, C., Zhang, L., Wang, C., & Wang, T. Z. (2019) · Animals · doi:10.3390/ani10010041 · Cited by 49
Sulforaphane reduces intracellular survival of Staphylococcus aureus in macrophages through inhibition of JNK and p38 MAPK‑induced inflammation
Deramaudt, T. B., Ali, M., Vinit, S., & Bonay, M. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4563 · Cited by 50
Loss of Nrf2 in bone marrow-derived macrophages impairs antigen-driven CD8+ T cell function by limiting GSH and Cys availability
Sha, L. K., Sha, W., Kuchler, L., Daiber, A., Giegerich, A. K., Weigert, A., Knape, T., Snodgrass, R. G., Schröder, K., Brandes, R. P., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.004 · Cited by 48
Bardoxolone methyl analog attenuates proteinuria‐induced tubular damage by modulating mitochondrial function
Nagasu, H., Sogawa, Y., Kidokoro, K., Itano, S., Yamamoto, T., Satoh, M., Sasaki, T., Suzuki, T., Yamamoto, M. P., Wigley, W. C., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900217r · Cited by 48
Self-citation
Nrf2 transcriptional derepression from Keap1 by dietary polyphenols
Bayele, H. K., Debnam, E. S., & Srai, S. K. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.11.103 · Cited by 47
Effects of substance P on osteoblastic differentiation and heme oxygenase‐1 in human periodontal ligament cells
Kook, Y., Lee, S., Son, D., Kim, Y., Kang, K., Cho, J., Kim, S., Kim, Y. S., Lee, H., Lee, S., et al. (2009) · Cell Biology International · doi:10.1016/j.cellbi.2008.12.007 · Cited by 46
“Regarding the transcription of HO-1, Nrf-2 is a relatively well-known transcription factor, and has been implicated in oxidative stress-induced HO-1 expression (Itoh et al., 2004; Martin et al., 2004).”
Background
Oncogenic Activation of Nrf2, Though as a Master Antioxidant Transcription Factor, Liberated by Specific Knockout of the Full-Length Nrf1α that Acts as a Dominant Tumor Repressor
Qiu, L., Wang, M., Hu, S., Ru, X., Ren, Y., Zhang, Z., Yu, S., & Zhang, Y. (2018) · Cancers · doi:10.3390/cancers10120520 · Cited by 46
“Intriguingly, the abundance of COX2, as a well-known direct target of Nrf2, was not decreased, but rather marginally increased by ectopic expression of Nrf1 that had been restored into Nrf1α−/− cells (Figure 2F), in which the repressed expression of COX1 was also not rescued, albeit both genes encompass the ARE sites…”
BackgroundInfluential
Prostaglandin J2: a potential target for halting inflammation‐induced neurodegeneration
Figueiredo‐Pereira, M. E., Corwin, C., & Babich, J. W. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12987 · Cited by 42
Halobenzoquinone-Induced Alteration of Gene Expression Associated with Oxidative Stress Signaling Pathways
Li, J., Moe, B., Liu, Y., & Li, X. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.7b06428 · Cited by 45
Impacts of high fat diet on ocular outcomes in rodent models of visual disease
Clarkson-Townsend, D. A., Douglass, A., Singh, A., Allen, R. S., Uwaifo, I. N., & Pardue, M. T. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108440 · Cited by 47
Nrf2 deficiency causes lipid oxidation, inflammation, and matrix-protease expression in DHA-supplemented and UVA-irradiated skin fibroblasts
Gruber, F., Ornelas, C. M., Karner, S., Narzt, M.-S., Nagelreiter, I. M., Gschwandtner, M., Bochkov, V., & Tschachler, E. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.006 · Cited by 44
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
“Accordingly, it has been demonstrated that downregulation of Nrf2 in mice is associated with persistent inflammation [127, 133, 134].”
Background
Nrf2 Deficiency Unmasks the Significance of Nitric Oxide Synthase Activity for Cardioprotection
Erkens, R., Suvorava, T., Sutton, T. R., Fernandez, B. O., Mikus-Lelinska, M., Barbarino, F., Flögel, U., Kelm, M., Feelisch, M., & Cortese-Krott, M. M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8309698 · Cited by 43
Can Nrf2 Modulate the Development of Intestinal Fibrosis and Cancer in Inflammatory Bowel Disease?
Pompili, S., Sferra, R., Gaudio, E., Viscido, A., Frieri, G., Vetuschi, A., & Latella, G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20164061 · Cited by 44
Multifaceted Roles of the KEAP1–NRF2 System in Cancer and Inflammatory Disease Milieu
Panda, H., Wen, H., Suzuki, M., & Yamamoto, M. P. (2022) · Antioxidants · doi:10.3390/antiox11030538 · Cited by 46
Self-citation
Differential effect of covalent protein modification and glutathione depletion on the transcriptional response of Nrf2 and NF-κB
Chia, A. J. L., Goldring, C. E., Kitteringham, N. R., Wong, S. Q., Morgan, P., & Park, B. K. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.04.004 · Cited by 43
Nrf2 Activation and Its Coordination with the Protective Defense Systems in Response to Electrophilic Stress
Unoki, T., Akiyama, M., & Kumagai, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020545 · Cited by 43
Anti-Inflammatory Prostanoids: Focus on the Interactions between Electrophile Signaling and Resolution of Inflammation
Díez-Dacal, B., & Pérez‐Sala, D. (2010) · The Scientific World JOURNAL · doi:10.1100/tsw.2010.69 · Cited by 43
3H-1,2-dithiole-3-thione as a novel therapeutic agent for the treatment of experimental autoimmune encephalomyelitis.
Kuo, P.-C., Brown, D. A., Scofield, B., Yu, I.-C., Chang, F.-L. F., Wang, P., & Yen, J. (2016) · Brain, behavior, and immunity · doi:10.1016/j.bbi.2016.03.015 · Cited by 43
Emerging evidence for crosstalk between Nrf2 and mitochondria in physiological homeostasis and in heart disease
Tsushima, M., Liu, J., Hirao, W., Yamazaki, H., Tomita, H., & Itoh, K. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01188-z · Cited by 42
Self-citation
Oxidized Phospholipids in Healthy and Diseased Lung Endothelium
Karki, P., & Birukov, K. G. (2020) · Cells · doi:10.3390/cells9040981 · Cited by 43
The novel Nrf2 inducer TFM-735 ameliorates experimental autoimmune encephalomyelitis in mice
Higashi, C., Kawaji, A., Tsuda, N., Hayashi, M., Saito, R., Yagishita, Y., Suzuki, T., Uruno, A., Nakamura, M., Nakao, K., et al. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.02.044 · Cited by 44
“Previous reports have demonstrated that Nrf2 exerts immuno-modulatory effects (Itoh et al., 2004; Kobayashi et al., 2016; Thimmulappa et al., 2007), and several Nrf2 inducers exhibit immuno-modulatory activity in EAE mice.”
BackgroundSelf-citation
17-β estradiol exerts anti-inflammatory effects through activation of Nrf2 in mouse embryonic fibroblasts
Song, C., Kim, N., Kim, D.-H., Lee, H.-N., & Surh, Y. (2019) · PLoS ONE · doi:10.1371/journal.pone.0221650 · Cited by 41
Carcinogenesis and transcriptional regulation through Maf recognition elements
Motohashi, H., & Yamamoto, M. P. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00358.x · Cited by 41
Self-citation
Nrf2 in TIME: The Emerging Role of Nuclear Factor Erythroid 2-Related Factor 2 in the Tumor Immune Microenvironment
Feng, J., Read, O. J., & Dinkova‐Kostova, A. T. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.2183 · Cited by 42
Neuroprotective Effects of Melatonin on Experimental Allergic Encephalomyelitis Mice Via Anti-Oxidative Stress Activity
Long, T., Yang, Y., Peng, L., & Li, Z. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-017-1022-x · Cited by 40
“flammation in a model of acute pleurisy (Itoh et al. 2004) and the mouse model of sickle cell disease (Keleku-Lukwete et al.”
Background
A novel chalcone derivative as Nrf2 activator attenuates learning and memory impairment in a scopolamine-induced mouse model
Kim, H. J., Jang, B. K., Park, J., Choi, J., Park, S. J., Byeon, S. R., Pae, A. N., Lee, Y. S., Cheong, E., & Park, K. D. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111777 · Cited by 40
Redox ticklers and beyond: Naphthoquinone repository in the spotlight against inflammation and associated maladies
Kapoor, N., Kandwal, P., Sharma, G., & Gambhir, L. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105968 · Cited by 40
The antioxidant and anti-inflammatory activities of tocopherols are independent of Nrf2 in mice
Li, G., Lee, M., Liu, A. B., Yang, Z., Lin, Y., Shih, W. J., & Yang, C. S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.005 · Cited by 40
Lipid peroxidation and redox-sensitive signaling pathways
Uchida, K. (2007) · Current Atherosclerosis Reports · doi:10.1007/s11883-007-0022-7 · Cited by 40
Self-citation
The Phenolic Components of Gastrodia elata improve Prognosis in Rats after Cerebral Ischemia/Reperfusion by Enhancing the Endogenous Antioxidant Mechanisms
Shi, A., Xiang, J., He, F., Zhu, Y.-P., Zhu, G., Lin, Y.-H., & Zhou, N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7642158 · Cited by 39
Tea polyphenols protect bovine mammary epithelial cells from hydrogen peroxide-induced oxidative damage in vitro by activating NFE2L2/HMOX1 pathways
Ma, Y., Zhao, L., Coleman, D. N., Gao, M., & Loor, J. J. (2018) · Journal of Dairy Science · doi:10.3168/jds.2018-15047 · Cited by 39
Renal protection by 3H-1,2-dithiole-3-thione against cisplatin through the Nrf2-antioxidant pathway
Park, H.-M., Cho, J., Lee, H., Shim, G.-S., & Kwak, M. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.06.021 · Cited by 39
A Nitric Oxide Storage and Transport System That Protects Activated Macrophages from Endogenous Nitric Oxide Cytotoxicity
Lok, H. C., Sahni, S., Jansson, P. J., Kovacevic, Z., Hawkins, C. L., & Richardson, D. R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.763714 · Cited by 36
“This increase in NRF2 levels is consistent with previous studies examining its expression after macrophage activation (66).”
Result
GPx2 Induction Is Mediated Through STAT Transcription Factors During Acute Colitis
Hiller, F., Besselt, K., Deubel, S., Brigelius‐Flohé, R., & Kipp, A. P. (2015) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000464 · Cited by 38
Identification of a novel series of anti-inflammatory and anti-oxidative phospholipid oxidation products containing the cyclopentenone moiety in vitro and in vivo: Implication in atherosclerosis
Lu, J., Guo, S., Xue, X., Chen, Q., Ge, J., Zhuo, Y., Zhong, H., Chen, B., Zhao, M., Han, W., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.751909 · Cited by 38
Delayed Nrf2-regulated antioxidant gene induction in response to silica nanoparticles
Zhang, H., Zhou, L., Yuen, J., Birkner, N. R., Leppert, V. J., O’Day, P. A., & Forman, H. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.002 · Cited by 37
“In addition, 15-deoxydelta-12,14-prostaglandin J2 (15d-PGJ2), a product of COX-2, is a well-established Nrf2 activator [71].”
Background
Deficiency of TDAG51 Protects Against Atherosclerosis by Modulating Apoptosis, Cholesterol Efflux, and Peroxiredoxin‐1 Expression
Hossain, G. S., Lynn, E. G., Maclean, K. N., Zhou, J., Dickhout, J. G., Lhoták, Š., Trigatti, B. L., Capone, J. P., Rho, J., Tang, D., et al. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000134 · Cited by 36
Arachidonic Acid Induces ARE/Nrf2-Dependent Heme Oxygenase-1 Transcription in Rat Brain Astrocytes
Lin, C., Yang, C.-C., Chen, Y., Hsiao, L., & Yang, C. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0590-7 · Cited by 36
Bixin protects against particle-induced long-term lung injury in an NRF2-dependent manner
Xue, L., Zhang, H., Zhang, J., Li, B., Zhang, Z., & Tao, S. (2018) · Toxicology Research · doi:10.1039/c7tx00304h · Cited by 35
Therapeutic advancement of simvastatin-loaded solid lipid nanoparticles (SV-SLNs) in treatment of hyperlipidemia and attenuating hepatotoxicity, myopathy and apoptosis: Comprehensive study
Abo-Zalam, H. B., El-Denshary, E. S., Abdelsalam, R. M., Khalil, I. A. H., Khattab, M. M., & Hamzawy, M. A. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111494 · Cited by 35
Anticancer Effects of 15d-Prostaglandin-J2 in Wild-Type and Doxorubicin-Resistant Ovarian Cancer Cells: Novel Actions on SIRT1 and HDAC
de Jong, E., Winkel, P., Poelstra, K., & Prakash, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025192 · Cited by 35
Proteomic studies on protein modification by cyclopentenone prostaglandins: Expanding our view on electrophile actions
Garzón, B., Oeste, C. L., Díez-Dacal, B., & Pérez‐Sala, D. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.03.028 · Cited by 35
Expression of TREM-1 is inhibited by PGD2 and PGJ2 in macrophages
Syed, M. A., Joo, M., Abbas, Z., Rodger, D., Christman, J. W., Mehta, D., & Sadikot, R. T. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.08.009 · Cited by 34
Tenuigenin inhibits LPS-induced inflammatory responses in microglia via activating the Nrf2-mediated HO-1 signaling pathway
Wang, X., Li, M., Cao, Y., Wang, J., Zhang, H., Zhou, X., Li, Q., & Wang, L. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.05.004 · Cited by 35
“Recently, Nrf2 has been reported to have anti-inflammatory effects (Itoh et al., 2004; Surh and Na, 2008).”
Background
Cyclopentenone Prostaglandins and Structurally Related Oxidized Lipid Species Instigate and Share Distinct Pro- and Anti-inflammatory Pathways
Muri, J., Feng, Q., Wolleb, H., Shamshiev, A. T., Ebner, C., Tortola, L., Brož, P., Carreira, E. M., & Köpf, M. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.019 · Cited by 34
Cyclopentenone Prostaglandin, 15-Deoxy-Δ12,14-PGJ2, Is Metabolized by HepG2 Cells via Conjugation with Glutathione
Brunoldi, E. M., Zanoni, G., Vidari, G., Sasi, S., Freeman, M. L., Milne, G. L., & Morrow, J. D. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700231a · Cited by 33
Nonenzymatic free radical-catalyzed generation of 15-deoxy-Δ12,14-prostaglandin J2-like compounds (deoxy-J2-isoprostanes) in vivo
Hardy, K. D., Cox, B. E., Milne, G. L., Yin, H., & Roberts, I. L. J. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m010264 · Cited by 33
Hepatic Gene Expression Profiling in Nrf2 Knockout Mice after Long-Term High-Fat Diet-Induced Obesity
Chartoumpekis, D. V., Ziros, P. G., Zaravinos, A., Iskrenova, R. P., Psyrogiannis, A. I., Kyriazopoulou, V. E., Sykiotis, G. P., & Habeos, I. G. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/340731 · Cited by 33
A gene co-association network regulating gut microbial communities in a Duroc pig population
Reverter, A., Ballester, M., Alexandre, P. A., Mármol‐Sánchez, E., Dalmau, A., Quintanilla, R., & Ramayo‐Caldas, Y. (2021) · Microbiome · doi:10.1186/s40168-020-00994-8 · Cited by 37
Cyclopentenone Prostaglandins: Biologically Active Lipid Mediators Targeting Inflammation
Lee, B. R., Paing, M. H., & Sharma-Walia, N. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.640374 · Cited by 34
4-Octyl-Itaconate and Dimethyl Fumarate Inhibit COX2 Expression and Prostaglandin Production in Macrophages
Diskin, C., Zotta, A., Corcoran, S. E., Tyrrell, V. J., Zasłona, Z., O’Donnell, V. B., & O'Neill, L. A. J. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100488 · Cited by 32
Disrupted Balance of the Oxidant–Antioxidant System in the Pathophysiology of Female Reproduction: Oxidative Stress and Adverse Pregnancy Outcomes
Joó, J. G., Sulyok, E., Bódis, J., & Kornya, L. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45100511 · Cited by 38
Detection of electrophile-sensitive proteins
Wall, S. B., Smith, M. R., Ricart, K. C., Zhou, F., Vayalil, P. K., Oh, J., & Landar, A. L. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.003 · Cited by 31
Whole-Body In Vivo Monitoring of Inflammatory Diseases Exploiting Human Interleukin 6-Luciferase Transgenic Mice
Hayashi, M., Takai, J., Yu, L., Motohashi, H., Moriguchi, T., & Yamamoto, M. P. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00506-15 · Cited by 31
“For instance, Nrf2-deficient mice showed persistent inflammation in a carrageenan-induced acute pleurisy model (17) and in elastase-induced pulmonary inflammation (18).”
BackgroundSelf-citation
Pharmacological blockade of the EP3 prostaglandin E2 receptor in the setting of type 2 diabetes enhances β-cell proliferation and identity and relieves oxidative damage
Bosma, K. J., Andrei, S. R., Katz, L. S., Smith, A. A., Dunn, J. C., RICCIARDI, V. F., Ramirez, M. A., Baumel-Alterzon, S., Pace, W. A., Carroll, D. T., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101347 · Cited by 29
15-Deoxy-Δ12,14-prostaglandin J2 as an electrophilic mediator
Shibata, T. (2015) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2015.1012149 · Cited by 30
Self-citation
Protective Effects of BML-111 on Cerulein-Induced Acute Pancreatitis-Associated Lung Injury via Activation of Nrf2/ARE Signaling Pathway
Wang, Y., Zhang, Y., Cheng, J.-S., Ni, Q., Li, P.-W., Han, W., & Zhang, Y. (2014) · Inflammation · doi:10.1007/s10753-014-9836-y · Cited by 30
The novel Nrf2-interacting factor KAP1 regulates susceptibility to oxidative stress by promoting the Nrf2-mediated cytoprotective response
Maruyama, A., Nishikawa, K., Kawatani, Y., Mimura, J., Hosoya, T., Harada, N., Yamamato, M., & Itoh, K. (2011) · Biochemical Journal · doi:10.1042/bj20101748 · Cited by 30
Self-citation
Heme oxygenase-1 protects human periodontal ligament cells against substance P-induced RANKL expression
Lee, H., Jeong, G., Pi, S., Lee, S.-I., Bae, W. ‐., Kim, S.-J., Lee, S.-K., & Kim, E.-C. (2010) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2009.01247.x · Cited by 30
Nrf2-mediated Induction of Cytoprotective Enzymes by 15-Deoxy-Δ12,14-Prostaglandin J2 Is Attenuated by Alkenal/one Oxidoreductase
Yu, X. Y., Egner, P. A., Wakabayashi, J., Wakabayashi, N., Yamamoto, M. P., & Kensler, T. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604620200 · Cited by 30
Self-citation
Induction of peroxiredoxin I gene expression by LPS involves the Src/PI3K/JNK signalling pathway
Bast, A., Fischer, K., Erttmann, S. F., & Walther, R. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.11.015 · Cited by 29
15d-PGJ2 alleviates ConA-induced acute liver injury in mice by up-regulating HO-1 and reducing hepatic cell autophagy
Chen, K., Li, J., Li, S., Feng, J., Wu, L., Liu, T., Zhang, R., Xu, S., Cheng, K., Zhou, Y., et al. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.03.012 · Cited by 29
Increased Risk of Nasopharyngeal Carcinoma with Increasing Levels of Diet-Associated Inflammation in an Italian Case–Control Study
Shivappa, N., Hébert, J. R., Zucchetto, A., Montella, M., Libra, M., Garavello, W., Rossi, M., Vecchia, C. L., & Serraino, D. (2016) · Nutrition and Cancer · doi:10.1080/01635581.2016.1216137 · Cited by 30
“(Nrf-2), which are regulators of inflammatory responses (50,51).”
Background
Targeting of Histone Acetyltransferase p300 by Cyclopentenone Prostaglandin Δ12-PGJ2 through Covalent Binding to Cys1438
Ravindra, K. C., Narayan, V., Lushington, G. H., Peterson, B. R., & Prabhu, K. S. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200383c · Cited by 29
15-Deoxy-Δ 12,14 -Prostaglandin J 2 Exerts Proresolving Effects Through Nuclear Factor E2-Related Factor 2-Induced Expression of CD36 and Heme Oxygenase-1
Kim, W., Lee, H., Jang, J., Kim, S. H., Lee, Y., Hahn, Y., Ngo, H., Choi, Y., Joe, Y., Chung, H., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6754 · Cited by 28
Andrographolide attenuates inflammatory response induced by LPS via activating Nrf2 signaling pathway in bovine endometrial epithelial cells
Fu, K., Chen, H., Wang, Z., & Cao, R. (2020) · Research in Veterinary Science · doi:10.1016/j.rvsc.2020.11.022 · Cited by 28
Rosiglitazone and 15-Deoxy-Δ 12,14 -Prostaglandin J 2 , PPAR γ Agonists, Differentially Regulate Cigarette Smoke-Mediated Pro-Inflammatory Cytokine Release in Monocytes/Macrophages
Caito, S. W., Yang, S., Kode, A., Edirisinghe, I., Rajendrasozhan, S., Phipps, R. P., & Rahman, I. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1889 · Cited by 28
Cyclopentenone-containing oxidized phospholipids and their isoprostanes as pro-resolving mediators of inflammation
Friedli, O., & Freigang, S. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.07.006 · Cited by 28
Saikosaponin A Inhibits LPS-Induced Endometritis in Mice Through Activating Nrf2 Signaling Pathway
Wang, J., Wang, W., & Pang, Y. (2018) · Inflammation · doi:10.1007/s10753-018-0796-5 · Cited by 28
Genetic ablation of Nrf2 exacerbates neurotoxic effects of acrylamide in mice
Ekuban, F. A., Zong, C., Takikawa, M., Morikawa, K., Sakurai, T., Ichihara, S., Itoh, K., Yamamoto, M. P., Ohsako, S., & Ichihara, G. (2021) · Toxicology · doi:10.1016/j.tox.2021.152785 · Cited by 28
Self-citation
Prostaglandin D2 induces heme oxygenase-1 in human retinal pigment epithelial cells
Kuesap, J., Li, B., Satarug, S., Takeda, K., Numata, I., Na‐Bangchang, K., & Shibahara, S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.148 · Cited by 27
Nrf2 downregulates zymosan-induced neutrophil activation and modulates migration
Helou, D. G., Braham, S., de Chaisemartin, L., Granger, V., Damien, M.-H., Pallardy, M. J., Kerdine‐Römer, S., & Chollet‐Martin, S. (2019) · PLoS ONE · doi:10.1371/journal.pone.0216465 · Cited by 26
Mechanisms underlying unidirectional laminar shear stress-mediated Nrf2 activation in endothelial cells: Amplification of low shear stress signaling by primary cilia
Ishii, T., Warabi, E., & Mann, G. E. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102103 · Cited by 28
Self-citation
Modulation of the expression of the π class of glutathione S-transferase by Andrographis paniculata extracts and andrographolide
Chang, K., Lii, C., Tsai, C.-W., Yang, A.-J., & Chen, H. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.11.002 · Cited by 26
Epigenome and transcriptome study of moringa isothiocyanate in mouse kidney mesangial cells induced by high glucose, a potential model for diabetic-induced nephropathy
Li, S. N., Li, W., Wu, R., Yin, R., Sargsyan, D., Raskin, I., & Kong, A. T. (2019) · The AAPS Journal · doi:10.1208/s12248-019-0393-z · Cited by 26
“Previous studies have found that Nrf2 regulates antioxidant response element to activate target genes and thus participate in the anti-oxidative stress/anti-inflammatory process (38,39).”
Background
MyD88 is a mediator for the activation of Nrf2
Kim, K. H., Lyu, J. H., Koo, S., Oh, S., Lee, H., Ahn, K., Sadikot, R. T., & Joo, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.11.051 · Cited by 26
Glutathione S Transferases: Biochemistry, Polymorphism and Role in Colorectal Carcinogenesis
Nissar, S., Aga, S. S., Rasool, R., Chowdri, N. A., & Rashid, F. (2017) · Journal of Carcinogenesis & Mutagenesis · doi:10.4172/2157-2518.1000287 · Cited by 26
Influence of iNOS and COX on peroxiredoxin gene expression in primary macrophages
Bast, A., Erttmann, S. F., Walther, R., & Steinmetz, I. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.015 · Cited by 25
The permissive role of mitochondria in the induction of haem oxygenase-1 in endothelial cells
Ricart, K. C., Bolisetty, S., Johnson, M. S., Perez, J. N., Agarwal, A., Murphy, M. P., & Landar, A. L. (2009) · Biochemical Journal · doi:10.1042/bj20081350 · Cited by 25
Chemical genomics of cancer chemopreventive dithiolethiones
Tran, Q. T., Xu, L., Phan, V., Goodwin, S. B., Rahman, M., Jin, V. X., Sutter, T. R., Roebuck, B. D., Kensler, T. W., George, E. O., et al. (2009) · Carcinogenesis · doi:10.1093/carcin/bgn292 · Cited by 24
Temporal changes in glutathione biosynthesis during the lipopolysaccharide-induced inflammatory response of THP-1 macrophages
Zhang, H., Liu, H., Zhou, L., Yuen, J., & Forman, H. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.010 · Cited by 24
Oxidative Stress and Antioxidant Therapy in Chronic Kidney and Cardiovascular Disease
David, M., & Glenda, C. (2013) · InTech eBooks · doi:10.5772/51923 · Cited by 25
Suppression of antioxidant Nrf-2 and downstream pathway in H9c2 cells by advanced glycation end products (AGEs) via ERK phosphorylation
Ko, S., Chang, S.-S., Lin, I.-H., & Chen, H. (2015) · Biochimie · doi:10.1016/j.biochi.2015.07.019 · Cited by 23
Roles of Nrf2 in drug and chemical toxicity
Clarke, J., Murray, J. B., Park, B. K., & Copple, I. M. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.004 · Cited by 23
Macrophage Migration Inhibitory Factor as an Emerging Drug Target to Regulate Antioxidant Response Element System
Yukitake, H., Takizawa, M., & Kimura, H. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8584930 · Cited by 23
“…ROS and a function of enzymatic/nonenzymatic antioxidant reaction system in living organisms, and disturbance of this homeostasis plays a critical role in pathophysiology of human diseases, such as cardiovascular diseases, inflammatory bowel diseases, septic shock, rheumatoid arthritis,…”
Background
Carbocisteine Reduces Virus-Induced Pulmonary Inflammation in Mice Exposed to Cigarette Smoke
Yageta, Y., Ishii, Y., Morishima, Y., Ano, S., Ohtsuka, S., Matsuyama, M., Takeuchi, K., Itoh, K., Yamamoto, M. P., & Hizawa, N. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0292oc · Cited by 23
Self-citation
Identification of 15d-PGJ2 as an antagonist of farnesoid X receptor: Molecular modeling with biological evaluation
Xu, X. Y., Lu, Y., Chen, L., Chen, J., Luo, X., & Shen, X. (2013) · Steroids · doi:10.1016/j.steroids.2013.04.018 · Cited by 22
17β-Estradiol strongly inhibits azoxymethane/dextran sulfate sodium-induced colorectal cancer development in Nrf2 knockout male mice
Song, C., Kim, N., Nam, R. H., Choi, S. I., Son, J. H., Yu, J. E., Shin, E. H., Lee, H., Kim, D.-H., & Surh, Y. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114279 · Cited by 23
4-Ethylguaiacol modulates neuroinflammation and Th1/Th17 differentiation to ameliorate disease severity in experimental autoimmune encephalomyelitis
Weng, W., Kuo, P., Brown, D. A., Scofield, B. A., Furnas, D., Paraiso, H. C., Wang, P., Yu, I.-C. I., & Yen, J.-H. J. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02143-w · Cited by 24
BTZO-15, an ARE-Activator, Ameliorates DSS- and TNBS-Induced Colitis in Rats
Yukitake, H., Kimura, H., Suzuki, H., Tajima, Y., Sato, Y., Imaeda, T., Kajino, M., & Takizawa, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023256 · Cited by 22
Anti-inflammatory effects of lindenenyl acetate via heme oxygenase-1 and AMPK in human periodontal ligament cells
Jeong, G., Lee, D., Li, B., Kim, J.-J., Kim, E.-C., & Kim, Y. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.08.008 · Cited by 22
Deferoxamine-induced neurite outgrowth and synapse formation in postnatal rat dorsal root ganglion (DRG) cell cultures
Nowicki, M., Kosacka, J., Spanel‐Borowski, K., & Borlak, J. T. (2009) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2009.05.003 · Cited by 22
“Its activity is regulated by the Keap1-Nrf2-ARE signaling pathway (Itoh et al., 2004; Kensler et al., 2007; Satoh et al., 2006) with HO-1 expression being augmented by the hypoxia-inducible factor (Siddiq et al., 2005). edium for 2 days, then switched to serum-free condition and immunostained for…”
Background
Albumin-Binding and Tumor Vasculature Determine the Antitumor Effect of 15-Deoxy-Δ12,14-Prostaglandin-J2in vivo
Prakash, J., Bansal, R., Post, E., de Jager-Krikken, A., Hooge, M. N. L., & Poelstra, K. (2009) · Neoplasia · doi:10.1593/neo.91188 · Cited by 22
Bioactive lipid mediator class switching regulates myogenic cell progression and muscle regeneration
Fabre, P., Molina, T., Larose, J., Greffard, K., Généreux-Gamache, G., Deprez, A., Mokhtari, I., Pellerito, O., Duchesne, É., Dort, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60586-8 · Cited by 24
Kynurenine monooxygenase inhibition and associated reduced quinolinic acid reverses depression-like behaviour by upregulating Nrf2/ARE pathway in mouse model of depression: In-vivo and In-silico studies
Bansal, Y., Singh, R., Sodhi, R. K., Khare, P., Dhingra, R., Dhingra, N., Bishnoi, M., Kondepudi, K. K., & Kuhad, A. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109169 · Cited by 24
Galangin attenuates doxorubicin‐induced cardiotoxicity via activating nuclear factor erythroid 2‐related factor 2/heme oxygenase 1 signaling pathway to suppress oxidative stress and inflammation
Fang, G., Li, X., Yang, F., Huang, T., Qiu, C., Peng, K., Yang, Y., & Lan, C. (2023) · Phytotherapy Research · doi:10.1002/ptr.7991 · Cited by 21
“Another role of Nrf2 is its anti-inflammatory capacity as it regulates ARE-mediated anti-inflammatory genes, including NQO-1 , HO-1 , and PRX1 (Braun et al., 2002; Chen et al., 2006; Itoh et al., 2004; Rushworth et al., 2008).”
Background
Sulforaphane reduces lipopolysaccharide-induced proinflammatory markers in hippocampus and liver but does not improve sickness behavior
Townsend, B. E., & Johnson, R. W. (2015) · Nutritional Neuroscience · doi:10.1080/1028415x.2015.1103463 · Cited by 21

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