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Volumn 194, Issue 6, 2015, Pages 2776-2785

The cyclopentenone prostaglandin 15d-PGJ2 inhibits the NLRP1 and NLRP3 inflammasomes

Author keywords

[No Author keywords available]

Indexed keywords

15 DEOXY DELTA12,14 PROSTAGLANDIN J2; CRYOPYRIN; CYCLOOXYGENASE 1; GLUTATHIONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; MITOGEN ACTIVATED PROTEIN KINASE KINASE; NLR FAMILY LEUCINE RICH REPEAT PROTEIN 1; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA AGONIST; PLACEBO; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; URATE; 15-DEOXYPROSTAGLANDIN J2; APOPTOSIS REGULATORY PROTEIN; BACTERIAL TOXIN; CARRIER PROTEIN; CIAS1 PROTEIN, MOUSE; CYTOKINE; NALP1 PROTEIN, MOUSE; PROSTAGLANDIN D2; PROTECTIVE AGENT; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84924565877     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1401611     Document Type: Article
Times cited : (49)

References (69)
  • 1
    • 84901310586 scopus 로고    scopus 로고
    • Mechanisms and functions of inflammasomes
    • Lamkanfi, M., and V. M. Dixit. 2014. Mechanisms and functions of inflammasomes. Cell 157: 1013.1022.
    • (2014) Cell , vol.157 , pp. 1013-1022
    • Lamkanfi, M.1    Dixit, V.M.2
  • 2
    • 84858677223 scopus 로고    scopus 로고
    • Sensing and reacting to microbes through the inflammasomes
    • Franchi, L., R. Mun.oz-Planillo, and G. Nun.ez. 2012. Sensing and reacting to microbes through the inflammasomes. Nat. Immunol. 13: 325.332.
    • (2012) Nat. Immunol. , vol.13 , pp. 325-332
    • Franchi, L.1    Munoz-Planillo, R.2    Nunez, G.3
  • 3
    • 4143107932 scopus 로고    scopus 로고
    • Cyclooxygenase isozymes: The biology of prostaglandin synthesis and inhibition
    • Simmons, D. L., R. M. Botting, and T. Hla. 2004. Cyclooxygenase isozymes: the biology of prostaglandin synthesis and inhibition. Pharmacol. Rev. 56: 387.437.
    • (2004) Pharmacol. Rev. , vol.56 , pp. 387-437
    • Simmons, D.L.1    Botting, R.M.2    Hla, T.3
  • 4
    • 0035053973 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins: New insights on biological activities and cellular targets
    • Straus, D. S., and C. K. Glass. 2001. Cyclopentenone prostaglandins: new insights on biological activities and cellular targets. Med. Res. Rev. 21: 185.210.
    • (2001) Med. Res. Rev. , vol.21 , pp. 185-210
    • Straus, D.S.1    Glass, C.K.2
  • 5
    • 0035929592 scopus 로고    scopus 로고
    • 15-Deoxy-D12,14-prostaglandin J2 inhibition of NF-kB-DNA binding through covalent modification of the p50 subunit
    • Cernuda-Morollon, E., E. Pineda-Molina, F. J. Can.ada, and D. Perez-Sala. 2001. 15-Deoxy-D12,14-prostaglandin J2 inhibition of NF-kB-DNA binding through covalent modification of the p50 subunit. J. Biol. Chem. 276: 35530.35536.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35530-35536
    • Cernuda-Morollon, E.1    Pineda-Molina, E.2    Canada, F.J.3    Perez-Sala, D.4
  • 6
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkB kinase
    • Rossi, A., P. Kapahi, G. Natoli, T. Takahashi, Y. Chen, M. Karin, and M. G. Santoro. 2000. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkB kinase. Nature 403: 103.108.
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6    Santoro, M.G.7
  • 8
    • 0026627948 scopus 로고
    • Antiproliferative prostaglandins activate heat shock transcription factor
    • Amici, C., L. Sistonen, M. G. Santoro, and R. I. Morimoto. 1992. Antiproliferative prostaglandins activate heat shock transcription factor. Proc. Natl. Acad. Sci. USA 89: 6227.6231.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6227-6231
    • Amici, C.1    Sistonen, L.2    Santoro, M.G.3    Morimoto, R.I.4
  • 9
    • 11444261543 scopus 로고    scopus 로고
    • 15d-PGJ2: The anti-inflammatory prostaglandin? Clin
    • Scher, J. U., and M. H. Pillinger. 2005. 15d-PGJ2: the anti-inflammatory prostaglandin? Clin. Immunol. 114: 100.109.
    • (2005) Immunol. , vol.114 , pp. 100-109
    • Scher, J.U.1    Pillinger, M.H.2
  • 10
    • 0028972025 scopus 로고
    • 15-Deoxy-D12,14-prostaglandin J2 is a ligand for the adipocyte determination factor PPARg
    • Forman, B. M., P. Tontonoz, J. Chen, R. P. Brun, B. M. Spiegelman, and R. M. Evans. 1995. 15-Deoxy-D12,14-prostaglandin J2 is a ligand for the adipocyte determination factor PPARg. Cell 83: 803.812.
    • (1995) Cell , vol.83 , pp. 803-812
    • Forman, B.M.1    Tontonoz, P.2    Chen, J.3    Brun, R.P.4    Spiegelman, B.M.5    Evans, R.M.6
  • 11
    • 0028972026 scopus 로고
    • A prostaglandin J2 metabolite binds peroxisome proliferatoractivated receptor g and promotes adipocyte differentiation
    • Kliewer, S. A., J. M. Lenhard, T. M. Willson, I. Patel, D. C. Morris, and J. M. Lehmann. 1995. A prostaglandin J2 metabolite binds peroxisome proliferatoractivated receptor g and promotes adipocyte differentiation. Cell 83: 813.819.
    • (1995) Cell , vol.83 , pp. 813-819
    • Kliewer, S.A.1    Lenhard, J.M.2    Willson, T.M.3    Patel, I.4    Morris, D.C.5    Lehmann, J.M.6
  • 12
    • 70349801984 scopus 로고    scopus 로고
    • Regulation of Nrf2-dependent gene expression by 15-deoxy-D12,14-prostaglandin J2
    • Kansanen, E., A. M. Kivela, and A.-L. Levonen. 2009. Regulation of Nrf2-dependent gene expression by 15-deoxy-D12,14-prostaglandin J2. Free Radic. Biol. Med. 47: 1310.1317.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1310-1317
    • Kansanen, E.1    Kivela, A.M.2    Levonen, A.-L.3
  • 13
    • 79954416526 scopus 로고    scopus 로고
    • The cytoprotective role of the Keap1.Nrf2 pathway
    • Baird, L., and A. T. Dinkova-Kostova. 2011. The cytoprotective role of the Keap1.Nrf2 pathway. Arch. Toxicol. 85: 241.272.
    • (2011) Arch. Toxicol. , vol.85 , pp. 241-272
    • Baird, L.1    Dinkova-Kostova, A.T.2
  • 14
    • 0036521594 scopus 로고    scopus 로고
    • The role of PPARs in inflammation and immunity
    • Clark, R. B. 2002. The role of PPARs in inflammation and immunity. J. Leukoc. Biol. 71: 388.400.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 388-400
    • Clark, R.B.1
  • 15
    • 80054702892 scopus 로고    scopus 로고
    • 15-Deoxy-D,ù-prostaglandin J2, an electrophilic lipid mediator of antiinflammatory and pro-resolving signaling
    • Surh, Y.-J., H.-K. Na, J.-M. Park, H.-N. Lee, W. Kim, I.-S. Yoon, and D.-D. Kim. 2011. 15-Deoxy-D,ù-prostaglandin J2, an electrophilic lipid mediator of antiinflammatory and pro-resolving signaling. Biochem. Pharmacol. 82: 1335.1351.
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1335-1351
    • Surh, Y.-J.1    Na, H.-K.2    Park, J.-M.3    Lee, H.-N.4    Kim, W.5    Yoon, I.-S.6    Kim, D.-D.7
  • 16
    • 33947139688 scopus 로고    scopus 로고
    • Characterization of the interaction between anthrax toxin and its cellular receptors
    • Liu, S., H. J. Leung, and S. H. Leppla. 2007. Characterization of the interaction between anthrax toxin and its cellular receptors. Cell. Microbiol. 9: 977.987.
    • (2007) Cell. Microbiol. , vol.9 , pp. 977-987
    • Liu, S.1    Leung, H.J.2    Leppla, S.H.3
  • 17
    • 0034049623 scopus 로고    scopus 로고
    • Optimized production and purification of Bacillus anthracis lethal factor
    • Park, S., and S. H. Leppla. 2000. Optimized production and purification of Bacillus anthracis lethal factor. Protein Expr. Purif. 18: 293.302.
    • (2000) Protein Expr. Purif. , vol.18 , pp. 293-302
    • Park, S.1    Leppla, S.H.2
  • 18
    • 0027403919 scopus 로고
    • Residues 1.254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides
    • Arora, N., and S. H. Leppla. 1993. Residues 1.254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides. J. Biol. Chem. 268: 3334.3341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3334-3341
    • Arora, N.1    Leppla, S.H.2
  • 19
    • 0034326255 scopus 로고    scopus 로고
    • Tumor cell-selective cytotoxicity of matrix metalloproteinase-activated anthrax toxin
    • Liu, S., S. Netzel-Arnett, H. Birkedal-Hansen, and S. H. Leppla. 2000. Tumor cell-selective cytotoxicity of matrix metalloproteinase-activated anthrax toxin. Cancer Res. 60: 6061.6067.
    • (2000) Cancer Res. , vol.60 , pp. 6061-6067
    • Liu, S.1    Netzel-Arnett, S.2    Birkedal-Hansen, H.3    Leppla, S.H.4
  • 23
    • 78651258397 scopus 로고    scopus 로고
    • Inflammasome sensor Nlrp1bdependent resistance to anthrax is mediated by caspase-1, IL-1 signaling and neutrophil recruitment
    • Moayeri, M., D. Crown, Z. L. Newman, S. Okugawa, M. Eckhaus, C. Cataisson, S. Liu, I. Sastalla, and S. H. Leppla. 2010. Inflammasome sensor Nlrp1bdependent resistance to anthrax is mediated by caspase-1, IL-1 signaling and neutrophil recruitment. PLoS Pathog. 6: e1001222.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001222
    • Moayeri, M.1    Crown, D.2    Newman, Z.L.3    Okugawa, S.4    Eckhaus, M.5    Cataisson, C.6    Liu, S.7    Sastalla, I.8    Leppla, S.H.9
  • 24
    • 32944468985 scopus 로고    scopus 로고
    • Goutassociated uric acid crystals activate the NALP3 inflammasome
    • Martinon, F., V. Petrilli, A. Mayor, A. Tardivel, and J. Tschopp. 2006. Goutassociated uric acid crystals activate the NALP3 inflammasome. Nature 440: 237.241.
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 25
    • 58249116545 scopus 로고    scopus 로고
    • Resident macrophages initiating and driving inflammation in a monosodium urate monohydrate crystal-induced murine peritoneal model of acute gout
    • Martin, W. J., M. Walton, and J. Harper. 2009. Resident macrophages initiating and driving inflammation in a monosodium urate monohydrate crystal-induced murine peritoneal model of acute gout. Arthritis Rheum. 60: 281.289.
    • (2009) Arthritis Rheum. , vol.60 , pp. 281-289
    • Martin, W.J.1    Walton, M.2    Harper, J.3
  • 27
    • 55749111567 scopus 로고    scopus 로고
    • Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin
    • Levin, T. C., K. E. Wickliffe, S. H. Leppla, and M. Moayeri. 2008. Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin. Cell. Microbiol. 10: 2434.2446.
    • (2008) Cell. Microbiol. , vol.10 , pp. 2434-2446
    • Levin, T.C.1    Wickliffe, K.E.2    Leppla, S.H.3    Moayeri, M.4
  • 28
    • 84879508269 scopus 로고    scopus 로고
    • Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor
    • Chavarra-Smith, J., and R. E. Vance. 2013. Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor. PLoS Pathog. 9: e1003452.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003452
    • Chavarra-Smith, J.1    Vance, R.E.2
  • 31
    • 80052179138 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptotic cell death
    • Miao, E. A., J. V. Rajan, and A. Aderem. 2011. Caspase-1-induced pyroptotic cell death. Immunol. Rev. 243: 206.214.
    • (2011) Immunol. Rev. , vol.243 , pp. 206-214
    • Miao, E.A.1    Rajan, J.V.2    Aderem, A.3
  • 32
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden, E. D., and W. F. Dietrich. 2006. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat. Genet. 38: 240.244.
    • (2006) Nat. Genet. , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 33
    • 41949127121 scopus 로고    scopus 로고
    • Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
    • Fink, S. L., T. Bergsbaken, and B. T. Cookson. 2008. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Proc. Natl. Acad. Sci. USA 105: 4312.4317.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4312-4317
    • Fink, S.L.1    Bergsbaken, T.2    Cookson, B.T.3
  • 35
    • 38049119726 scopus 로고    scopus 로고
    • Anthrax lethal toxininduced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome
    • Wickliffe, K. E., S. H. Leppla, and M. Moayeri. 2008. Anthrax lethal toxininduced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome. Cell. Microbiol. 10: 332.343.
    • (2008) Cell. Microbiol. , vol.10 , pp. 332-343
    • Wickliffe, K.E.1    Leppla, S.H.2    Moayeri, M.3
  • 36
    • 0024209566 scopus 로고
    • Induction of 68,000-dalton heat shock proteins by cyclopentenone prostaglandins. Its association with prostaglandin-induced G1 block in cell cycle progression
    • Ohno, K., M. Fukushima, M. Fujiwara, and S. Narumiya. 1988. Induction of 68,000-dalton heat shock proteins by cyclopentenone prostaglandins. Its association with prostaglandin-induced G1 block in cell cycle progression. J. Biol. Chem. 263: 19764.19770.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19764-19770
    • Ohno, K.1    Fukushima, M.2    Fujiwara, M.3    Narumiya, S.4
  • 37
    • 0001065185 scopus 로고
    • Prostaglandins with antiproliferative activity induce the synthesis of a heat shock protein in human cells
    • Santoro, M. G., E. Garaci, and C. Amici. 1989. Prostaglandins with antiproliferative activity induce the synthesis of a heat shock protein in human cells. Proc. Natl. Acad. Sci. USA 86: 8407.8411.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8407-8411
    • Santoro, M.G.1    Garaci, E.2    Amici, C.3
  • 39
    • 0021892922 scopus 로고
    • D12-Prostaglandin J2, an ultimate metabolite of prostaglandin D2 exerting cell growth inhibition
    • Narumiya, S., and M. Fukushima. 1985. D12-Prostaglandin J2, an ultimate metabolite of prostaglandin D2 exerting cell growth inhibition. Biochem. Biophys. Res. Commun. 127: 739.745.
    • (1985) Biochem. Biophys. Res. Commun. , vol.127 , pp. 739-745
    • Narumiya, S.1    Fukushima, M.2
  • 40
    • 42449119839 scopus 로고    scopus 로고
    • Accumulation of 15-deoxy-D12,14-prostaglandin J2 adduct formation with Keap1 over time: Effects on potency for intracellular antioxidant defence induction
    • Oh, J. Y., N. Giles, A. Landar, and V. Darley-Usmar. 2008. Accumulation of 15-deoxy-D12,14-prostaglandin J2 adduct formation with Keap1 over time: effects on potency for intracellular antioxidant defence induction. Biochem. J. 411: 297.306.
    • (2008) Biochem. J. , vol.411 , pp. 297-306
    • Oh, J.Y.1    Giles, N.2    Landar, A.3    Darley-Usmar, V.4
  • 42
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • Vitale, G., L. Bernardi, G. Napolitani, M. Mock, and C. Montecucco. 2000. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 352: 739-745.
    • (2000) Biochem. J. , vol.352 , pp. 739-745
    • Vitale, G.1    Bernardi, L.2    Napolitani, G.3    Mock, M.4    Montecucco, C.5
  • 43
    • 84892770596 scopus 로고    scopus 로고
    • Arsenic trioxide and other arsenical compounds inhibit the NLRP1, NLRP3, and NAIP5/ NLRC4 inflammasomes
    • Maier, N. K., D. Crown, J. Liu, S. H. Leppla, and M. Moayeri. 2014. Arsenic trioxide and other arsenical compounds inhibit the NLRP1, NLRP3, and NAIP5/ NLRC4 inflammasomes. J. Immunol. 192: 763-770.
    • (2014) J. Immunol. , vol.192 , pp. 763-770
    • Maier, N.K.1    Crown, D.2    Liu, J.3    Leppla, S.H.4    Moayeri, M.5
  • 44
    • 84862339477 scopus 로고    scopus 로고
    • NAIPs: Building an innate immune barrier against bacterial pathogens. NAIPs function as sensors that initiate innate immunity by detection of bacterial proteins in the host cell cytosol
    • Kofoed, E. M., and R. E. Vance. 2012. NAIPs: building an innate immune barrier against bacterial pathogens. NAIPs function as sensors that initiate innate immunity by detection of bacterial proteins in the host cell cytosol. BioEssays 34: 589-598.
    • (2012) BioEssays , vol.34 , pp. 589-598
    • Kofoed, E.M.1    Vance, R.E.2
  • 45
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao, Y., J. Yang, J. Shi, Y.-N. Gong, Q. Lu, H. Xu, L. Liu, and F. Shao. 2011. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 477: 596-600.
    • (2011) Nature , vol.477 , pp. 596-600
    • Zhao, Y.1    Yang, J.2    Shi, J.3    Gong, Y.-N.4    Lu, Q.5    Xu, H.6    Liu, L.7    Shao, F.8
  • 46
    • 17144381253 scopus 로고    scopus 로고
    • A,b-Unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor g
    • Shiraki, T., N. Kamiya, S. Shiki, T. S. Kodama, A. Kakizuka, and H. Jingami. 2005. a,b-Unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor g. J. Biol. Chem. 280: 14145-14153.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14145-14153
    • Shiraki, T.1    Kamiya, N.2    Shiki, S.3    Kodama, T.S.4    Kakizuka, A.5    Jingami, H.6
  • 47
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh, K., N. Wakabayashi, Y. Katoh, T. Ishii, T. O'Connor, and M. Yamamoto. 2003. Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cells 8: 379-391.
    • (2003) Genes Cells , vol.8 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'connor, T.5    Yamamoto, M.6
  • 48
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon, M., K. Itoh, M. Yamamoto, and J. D. Hayes. 2003. Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem. 278: 21592-21600.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 49
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome
    • Nguyen, T., P. J. Sherratt, H.-C. Huang, C. S. Yang, and C. B. Pickett. 2003. Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome. J. Biol. Chem. 278: 4536-4541.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.-C.3    Yang, C.S.4    Pickett, C.B.5
  • 50
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart, D., E. Killeen, R. Naquin, S. Alam, and J. Alam. 2003. Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J. Biol. Chem. 278: 2396-2402.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 51
    • 0025304632 scopus 로고
    • Conjugation of 9-deoxy-D9,D12(E)-prostaglandin D2 with intracellular glutathione and enhancement of its antiproliferative activity by glutathione depletion
    • Atsmon, J., M. L. Freeman, M. J. Meredith, B. J. Sweetman, and L. J. Roberts, II. 1990. Conjugation of 9-deoxy-D9,D12(E)-prostaglandin D2 with intracellular glutathione and enhancement of its antiproliferative activity by glutathione depletion. Cancer Res. 50: 1879-1885.
    • (1990) Cancer Res. , vol.50 , pp. 1879-1885
    • Atsmon, J.1    Freeman, M.L.2    Meredith, M.J.3    Sweetman, B.J.4    Roberts, I.I.L.J.5
  • 52
    • 0035853707 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins as potential inducers of intracellular oxidative stress
    • Kondo, M., T. Oya-Ito, T. Kumagai, T. Osawa, and K. Uchida. 2001. Cyclopentenone prostaglandins as potential inducers of intracellular oxidative stress. J. Biol. Chem. 276: 12076-12083.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12076-12083
    • Kondo, M.1    Oya-Ito, T.2    Kumagai, T.3    Osawa, T.4    Uchida, K.5
  • 53
    • 84868314921 scopus 로고    scopus 로고
    • Redox control of NLRP3 inflammasome activation in health and disease
    • Rubartelli, A. 2012. Redox control of NLRP3 inflammasome activation in health and disease. J. Leukoc. Biol. 92: 951-958.
    • (2012) J. Leukoc. Biol. , vol.92 , pp. 951-958
    • Rubartelli, A.1
  • 54
    • 0035132330 scopus 로고    scopus 로고
    • PPAR-g dependent and independent effects on macrophage-gene expression in lipid metabolism and inflammation
    • Chawla, A., Y. Barak, L. Nagy, D. Liao, P. Tontonoz, and R. M. Evans. 2001. PPAR-g dependent and independent effects on macrophage-gene expression in lipid metabolism and inflammation. Nat. Med. 7: 48-52.
    • (2001) Nat. Med. , vol.7 , pp. 48-52
    • Chawla, A.1    Barak, Y.2    Nagy, L.3    Liao, D.4    Tontonoz, P.5    Evans, R.M.6
  • 55
    • 84902440210 scopus 로고    scopus 로고
    • Nuclear factor E2-related factor-2 (Nrf2) is required for NLRP3 and AIM2 inflammasome activation
    • Zhao, C., D. D. Gillette, X. Li, Z. Zhang, and H. Wen. 2014. Nuclear factor E2-related factor-2 (Nrf2) is required for NLRP3 and AIM2 inflammasome activation. J. Biol. Chem. 289: 17020-17029.
    • (2014) J. Biol. Chem. , vol.289 , pp. 17020-17029
    • Zhao, C.1    Gillette, D.D.2    Li, X.3    Zhang, Z.4    Wen, H.5
  • 58
    • 84896376445 scopus 로고    scopus 로고
    • Proresolving lipid mediators and mechanisms in the resolution of acute inflammation
    • Buckley, C. D., D. W. Gilroy, and C. N. Serhan. 2014. Proresolving lipid mediators and mechanisms in the resolution of acute inflammation. Immunity 40: 315-327.
    • (2014) Immunity , vol.40 , pp. 315-327
    • Buckley, C.D.1    Gilroy, D.W.2    Serhan, C.N.3
  • 60
    • 0033574541 scopus 로고    scopus 로고
    • Formation of reactive cyclopentenone compounds in vivo as products of the isoprostane pathway
    • Chen, Y., J. D. Morrow, and L. J. Roberts, II. 1999. Formation of reactive cyclopentenone compounds in vivo as products of the isoprostane pathway. J. Biol. Chem. 274: 10863-10868.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10863-10868
    • Chen, Y.1    Morrow, J.D.2    Roberts, I.I.L.J.3
  • 61
    • 78651419168 scopus 로고    scopus 로고
    • Effects of 15d-PGJ2-loaded poly(D,L-lactide-co-glycolide) nanocapsules on inflammation
    • Alves, C., N. de Melo, L. Fraceto, D. de Araú jo, and M. Napimoga. 2011. Effects of 15d-PGJ2-loaded poly(D,L-lactide-co-glycolide) nanocapsules on inflammation. Br. J. Pharmacol. 162: 623-632.
    • (2011) Br. J. Pharmacol. , vol.162 , pp. 623-632
    • Alves, C.1    De Melo, N.2    Fraceto, L.3    De Jo Araú, D.4    Napimoga, M.5
  • 63
    • 29244437849 scopus 로고    scopus 로고
    • Inhibition of skin sclerosis by 15-deoxy-D12,14-prostaglandin J2 and retrovirally transfected prostaglandin D synthase in a mouse model of bleomycin-induced scleroderma
    • Kohno, S., H. Endo, A. Hashimoto, I. Hayashi, Y. Murakami, H. Kitasato, F. Kojima, S. Kawai, and H. Kondo. 2006. Inhibition of skin sclerosis by 15-deoxy-D12,14-prostaglandin J2 and retrovirally transfected prostaglandin D synthase in a mouse model of bleomycin-induced scleroderma. Biomed. Pharmacother. 60: 18-25.
    • (2006) Biomed. Pharmacother. , vol.60 , pp. 18-25
    • Kohno, S.1    Endo, H.2    Hashimoto, A.3    Hayashi, I.4    Murakami, Y.5    Kitasato, H.6    Kojima, F.7    Kawai, S.8    Kondo, H.9
  • 65
    • 33751161701 scopus 로고    scopus 로고
    • Induction of apoptosis in estrogen receptor-negative breast cancer cells by natural and synthetic cyclopentenones: Role of the IkB kinase/ nuclear factor-kappaB pathway
    • Ciucci, A., P. Gianferretti, R. Piva, T. Guyot, T. J. Snape, S. M. Roberts, and M. G. Santoro. 2006. Induction of apoptosis in estrogen receptor-negative breast cancer cells by natural and synthetic cyclopentenones: role of the IkB kinase/ nuclear factor-kappaB pathway. Mol. Pharmacol. 70: 1812-1821.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1812-1821
    • Ciucci, A.1    Gianferretti, P.2    Piva, R.3    Guyot, T.4    Snape, T.J.5    Roberts, S.M.6    Santoro, M.G.7
  • 66
    • 0034614206 scopus 로고    scopus 로고
    • Preparation and evaluation of o/w type emulsions containing antitumor prostaglandin
    • Fukushima, S., S. Kishimoto, Y. Takeuchi, and M. Fukushima. 2000. Preparation and evaluation of o/w type emulsions containing antitumor prostaglandin. Adv. Drug Deliv. Rev. 45: 65-75.
    • (2000) Adv. Drug Deliv. Rev. , vol.45 , pp. 65-75
    • Fukushima, S.1    Kishimoto, S.2    Takeuchi, Y.3    Fukushima, M.4
  • 69
    • 43449092551 scopus 로고    scopus 로고
    • Killing of macrophages by anthrax lethal toxin: Involvement of the N-end rule pathway
    • Wickliffe, K. E., S. H. Leppla, and M. Moayeri. 2008. Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway. Cell. Microbiol. 10: 1352-1362.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1352-1362
    • Wickliffe, K.E.1    Leppla, S.H.2    Moayeri, M.3


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