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Volumn 88, Issue Part B, 2015, Pages 189-198

Close teamwork between Nrf2 and peroxiredoxins 1 and 6 for the regulation of prostaglandin D2 and E2 production in macrophages in acute inflammation

Author keywords

15d PGJ2; Free radicals; Lipocalin type prostaglandin D synthase; Lipopolysaccharide; NADPH oxidase 2; NF B; Nrf2; Peroxiredoxin; Polyphenols; Prostaglandin; S glutathionylation; Toll like receptor 4

Indexed keywords

CYCLOOXYGENASE 2; GLUTATHIONE; LIPOCALIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; PEROXIREDOXIN 6; POLYPHENOL; PROSTAGLANDIN D SYNTHASE; PROSTAGLANDIN D2; PROSTAGLANDIN E SYNTHASE 1; PROSTAGLANDIN E2; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SELENIUM; TOLL LIKE RECEPTOR 4; TRANSCRIPTION FACTOR NRF2; PEROXIREDOXIN;

EID: 84976315921     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.04.034     Document Type: Review
Times cited : (41)

References (111)
  • 1
    • 84876931396 scopus 로고    scopus 로고
    • Beyond oxidative stress: an immunologist's guide to reactive oxygen species
    • [1] Nathan, C, Cunningham-Bussel, A., Beyond oxidative stress: an immunologist's guide to reactive oxygen species. Nat. Rev. Immunol. 13 (2013), 349–361.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 349-361
    • Nathan, C.1    Cunningham-Bussel, A.2
  • 4
    • 84880869807 scopus 로고    scopus 로고
    • The complexity of NF-κB signaling in inflammation and cancer
    • [4] Hoesel, B, Schmid, JA., The complexity of NF-κB signaling in inflammation and cancer. Mol. Cancer, 12, 2013, 86.
    • (2013) Mol. Cancer , vol.12 , pp. 86
    • Hoesel, B.1    Schmid, J.A.2
  • 5
    • 84884938910 scopus 로고    scopus 로고
    • The effect of reactive oxygen species on the synthesis of prostanoids from arachidonic acid
    • [5] Korbecki, J, Baranowska-Bosiacka, I, Gutowska, I, Chlubek, D., The effect of reactive oxygen species on the synthesis of prostanoids from arachidonic acid. J. Physiol. Pharmacol. 64 (2013), 409–421.
    • (2013) J. Physiol. Pharmacol. , vol.64 , pp. 409-421
    • Korbecki, J.1    Baranowska-Bosiacka, I.2    Gutowska, I.3    Chlubek, D.4
  • 7
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • [7] Ishii, T, Itoh, K, Takahashi, S, Sato, H, Yanagawa, T, Katoh, Y, Bannai, S, Yamamoto, M., Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J. Biol. Chem. 275 (2000), 16023–16029.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 8
    • 1342301449 scopus 로고    scopus 로고
    • Stress protein activation by the cyclopentenone prostaglandin 15-deoxy-delta12,14-prostaglandin J2 human mesangial cells
    • [8] Zhang, X, Lu, L, Dixon, C, Wilmer, W, Song, H, Chen, X, Rovin, BH., Stress protein activation by the cyclopentenone prostaglandin 15-deoxy-delta12,14-prostaglandin J2 human mesangial cells. Kidney Int. 65 (2004), 798–810.
    • (2004) Kidney Int. , vol.65 , pp. 798-810
    • Zhang, X.1    Lu, L.2    Dixon, C.3    Wilmer, W.4    Song, H.5    Chen, X.6    Rovin, B.H.7
  • 12
    • 0031888958 scopus 로고    scopus 로고
    • PPAR-γ agonist inhibits production of monocyte inflammatory cytokines
    • [12] Jiang, C, Ting, T, Seed, B., PPAR-γ agonist inhibits production of monocyte inflammatory cytokines. Nature 391 (1998), 82–86.
    • (1998) Nature , vol.391 , pp. 82-86
    • Jiang, C.1    Ting, T.2    Seed, B.3
  • 13
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase
    • [13] Rossi, A, Kapahi, P, Natoli, T, Takahashi, T, Chen, Y, Karin, M, Santoro, MG., Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase. Nature 403 (2000), 103–108.
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, T.3    Takahashi, T.4    Chen, Y.5    Karin, M.6    Santoro, M.G.7
  • 15
    • 44849128045 scopus 로고    scopus 로고
    • Toll-like receptor 4 mediates induction of the Bcl10–NFκB–interleukin-8 inflammatory pathway by carrageenan in human intestinal epithelial cells
    • [15] Bhattacharyya, S, Gill, R, Chen, ML, Zhang, F, Linhardt, RJ, Dudeja, PK, Tobacman, JK., Toll-like receptor 4 mediates induction of the Bcl10–NFκB–interleukin-8 inflammatory pathway by carrageenan in human intestinal epithelial cells. J. Biol. Chem. 283 (2008), 10550–10558.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10550-10558
    • Bhattacharyya, S.1    Gill, R.2    Chen, M.L.3    Zhang, F.4    Linhardt, R.J.5    Dudeja, P.K.6    Tobacman, J.K.7
  • 18
    • 84877315077 scopus 로고    scopus 로고
    • Resolution of inflammation: an integrated view
    • [18] Ortega-Gόmez, A, Perretti, M, Soehnlein, O., Resolution of inflammation: an integrated view. EMBO Mol. Med 5 (2013), 661–674.
    • (2013) EMBO Mol. Med , vol.5 , pp. 661-674
    • Ortega-Gόmez, A.1    Perretti, M.2    Soehnlein, O.3
  • 19
    • 80051757801 scopus 로고    scopus 로고
    • Peculiarities of cell death mechanisms in neutrophils
    • [19] Geering, B, Simon, HU., Peculiarities of cell death mechanisms in neutrophils. Cell Death Differ. 18 (2011), 1457–1469.
    • (2011) Cell Death Differ. , vol.18 , pp. 1457-1469
    • Geering, B.1    Simon, H.U.2
  • 20
    • 1642396537 scopus 로고    scopus 로고
    • Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: activation by oxidatively modified LDL and 4-hydroxynonenal
    • [20] Ishii, T, Itoh, K, Ruiz, E, Leake, DS, Unoki, H, Yamamoto, M, Mann, GE., Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: activation by oxidatively modified LDL and 4-hydroxynonenal. Circ. Res. 94 (2004), 609–616.
    • (2004) Circ. Res. , vol.94 , pp. 609-616
    • Ishii, T.1    Itoh, K.2    Ruiz, E.3    Leake, D.S.4    Unoki, H.5    Yamamoto, M.6    Mann, G.E.7
  • 21
    • 0034213842 scopus 로고    scopus 로고
    • Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of gamma-glutamylcysteine synthetase heavy subunit gene
    • [21] Jeyapaul, J, Jaiswal, AK., Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of gamma-glutamylcysteine synthetase heavy subunit gene. Biochem. Pharmacol. 59 (2000), 1433–1439.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1433-1439
    • Jeyapaul, J.1    Jaiswal, A.K.2
  • 22
    • 58049088157 scopus 로고    scopus 로고
    • Oxidant stress stimulates expression of the human peroxiredoxin 6 gene by a transcriptional mechanism involving an antioxidant response element
    • [22] Chowdhury, I, Mo, Y, Gao, L, Kazi, A, Fisher, AB, Feinstein, SI., Oxidant stress stimulates expression of the human peroxiredoxin 6 gene by a transcriptional mechanism involving an antioxidant response element. Free Radic. Biol. Med. 46 (2009), 146–153.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 146-153
    • Chowdhury, I.1    Mo, Y.2    Gao, L.3    Kazi, A.4    Fisher, A.B.5    Feinstein, S.I.6
  • 24
    • 76249112140 scopus 로고    scopus 로고
    • Peroxiredoxin 1 stimulates secretion of proinflammatory cytokines by binding to TLR4
    • [24] Riddell, JR, Wang, X-Y, Minderman, H, Gollnick, SO., Peroxiredoxin 1 stimulates secretion of proinflammatory cytokines by binding to TLR4. J. Immunol. 184 (2010), 1022–1030.
    • (2010) J. Immunol. , vol.184 , pp. 1022-1030
    • Riddell, J.R.1    Wang, X.-Y.2    Minderman, H.3    Gollnick, S.O.4
  • 26
    • 84896096274 scopus 로고    scopus 로고
    • Novel links among peroxiredoxins, endothelial dysfunction, and severity of atherosclerosis in type 2 diabetic patients with peripheral atherosclerotic disease
    • [26] El Eter, E, Al Masri, A, Habib, S, Al Zamil, H, Al Hersi, A, Ai Hussein, F, Al Omran, M., Novel links among peroxiredoxins, endothelial dysfunction, and severity of atherosclerosis in type 2 diabetic patients with peripheral atherosclerotic disease. Cell Stress Chaperones 19 (2014), 173–181.
    • (2014) Cell Stress Chaperones , vol.19 , pp. 173-181
    • El Eter, E.1    Al Masri, A.2    Habib, S.3    Al Zamil, H.4    Al Hersi, A.5    Ai Hussein, F.6    Al Omran, M.7
  • 27
    • 84857835586 scopus 로고    scopus 로고
    • Novel roles of peroxiredoxins in inflammation, cancer and innate immunity
    • [27] Ishii, T, Yanagawa, T, Warabi, E., Novel roles of peroxiredoxins in inflammation, cancer and innate immunity. J. Clin. Biochem. Nutrition 50 (2012), 91–105.
    • (2012) J. Clin. Biochem. Nutrition , vol.50 , pp. 91-105
    • Ishii, T.1    Yanagawa, T.2    Warabi, E.3
  • 28
    • 84930196148 scopus 로고    scopus 로고
    • Cysteine oxidation targets peroxiredoxins 1 and 2 for exosomal release through a novel mechanism of redox-dependent secretion
    • 21
    • [28] Mullen, L, Hanschmann, EM, Lillig, CH, Herzenberg, LA, Ghezzi, P., Cysteine oxidation targets peroxiredoxins 1 and 2 for exosomal release through a novel mechanism of redox-dependent secretion. Mol. Med., 21, 2015, 98–108.
    • (2015) Mol. Med. , pp. 98-108
    • Mullen, L.1    Hanschmann, E.M.2    Lillig, C.H.3    Herzenberg, L.A.4    Ghezzi, P.5
  • 30
    • 79953249112 scopus 로고    scopus 로고
    • Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
    • [30] Fisher, AB., Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. Antioxid. Redox Signaling 15 (2011), 831–844.
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 831-844
    • Fisher, A.B.1
  • 31
    • 84855897060 scopus 로고    scopus 로고
    • 2 activities of peroxiredoxin 6 in protecting pulmonary microvascular endothelial cells against peroxidative stress
    • 2 activities of peroxiredoxin 6 in protecting pulmonary microvascular endothelial cells against peroxidative stress. Antioxid. Redox Signaling 16 (2012), 440–451.
    • (2012) Antioxid. Redox Signaling , vol.16 , pp. 440-451
    • Lien, Y.-C.1    Feinstein, S.I.2    Dodia, C.3    Fisher, A.B.4
  • 32
    • 84855770662 scopus 로고    scopus 로고
    • Peroxiredoxin 6 translocates to the plasma membrane during neutrophil activation and is required for optimal NADPH oxidase activity
    • [32] Ambruso, DR, Ellison, MA, Thurman, GW, Leto, TL., Peroxiredoxin 6 translocates to the plasma membrane during neutrophil activation and is required for optimal NADPH oxidase activity. Biochem. Biophys. Acta 1823 (2012), 306–315.
    • (2012) Biochem. Biophys. Acta , vol.1823 , pp. 306-315
    • Ambruso, D.R.1    Ellison, M.A.2    Thurman, G.W.3    Leto, T.L.4
  • 33
    • 84884938910 scopus 로고    scopus 로고
    • The effect of reactive oxygen species on the synthesis of prostanoids from arachidonic acid
    • [33] Korbecki, J, Baranowska-Bosiacka, I, Gutowska, I, Chlubek, D., The effect of reactive oxygen species on the synthesis of prostanoids from arachidonic acid. J. Physiol. Pharmacol. 64 (2013), 409–421.
    • (2013) J. Physiol. Pharmacol. , vol.64 , pp. 409-421
    • Korbecki, J.1    Baranowska-Bosiacka, I.2    Gutowska, I.3    Chlubek, D.4
  • 34
    • 0035880273 scopus 로고    scopus 로고
    • 2 on arachidonic acid release induced by reactive oxygen species
    • 2 on arachidonic acid release induced by reactive oxygen species. Arch. Biochem. Biophys. 392 (2001), 257–262.
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 257-262
    • Martínez, J.1    Moreno, J.J.2
  • 35
    • 84903202158 scopus 로고    scopus 로고
    • Redox status in mammalian cells and stem cells during culture in vitro: critical roles of Nrf2 and cystine transporter activity in the maintenance of redox balance
    • [35] Ishii, T, Mann, GE., Redox status in mammalian cells and stem cells during culture in vitro: critical roles of Nrf2 and cystine transporter activity in the maintenance of redox balance. Redox Biol 2 (2014), 786–794.
    • (2014) Redox Biol , vol.2 , pp. 786-794
    • Ishii, T.1    Mann, G.E.2
  • 36
    • 84885914465 scopus 로고    scopus 로고
    • Protein glutathionylation in cardiovascular diseases
    • [36] Pastore, A, Piemonte, F., Protein glutathionylation in cardiovascular diseases. Int. J. Mol. Sci 14 (2013), 20845–20876.
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 20845-20876
    • Pastore, A.1    Piemonte, F.2
  • 37
    • 84880727681 scopus 로고    scopus 로고
    • S-glutathionylation in monocyte and macrophage (dys)function
    • [37] Ullevig, S, Kim, HS, Asmis, R., S-glutathionylation in monocyte and macrophage (dys)function. Int. J. Mol. Sci 14 (2013), 15212–15232.
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 15212-15232
    • Ullevig, S.1    Kim, H.S.2    Asmis, R.3
  • 39
    • 84923912767 scopus 로고    scopus 로고
    • S-glutathionylation reactions in mitochondrial function and disease
    • [39] Mailloux, RJ, Willmore, WG., S-glutathionylation reactions in mitochondrial function and disease. Front. Cell. Dev. Biol, 2, 2014, 68.
    • (2014) Front. Cell. Dev. Biol , vol.2 , pp. 68
    • Mailloux, R.J.1    Willmore, W.G.2
  • 40
    • 33947381788 scopus 로고    scopus 로고
    • Redox in redux: emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation
    • [40] Tew, KD., Redox in redux: emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation. Biochem. Pharmacol. 73 (2007), 1257–1269.
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 1257-1269
    • Tew, K.D.1
  • 41
    • 17644390613 scopus 로고    scopus 로고
    • Controlled elimination of intracellular H2O2: regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification
    • [41] Rhee, SG, Yang, KS, Kang, SW, Woo, HA, Chang, TS., Controlled elimination of intracellular H2O2: regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid. Redox Signaling 7 (2005), 619–626.
    • (2005) Antioxid. Redox Signaling , vol.7 , pp. 619-626
    • Rhee, S.G.1    Yang, K.S.2    Kang, S.W.3    Woo, H.A.4    Chang, T.S.5
  • 42
    • 84863012241 scopus 로고    scopus 로고
    • Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidase that function as antioxidants, molecular chaperones, and signal modulators
    • [42] Chae, HZ, Oubrahim, H, Park, JW, Rhee, SG, Chock, PB., Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidase that function as antioxidants, molecular chaperones, and signal modulators. Antioxid. Redox Signaling 16 (2012), 506–523.
    • (2012) Antioxid. Redox Signaling , vol.16 , pp. 506-523
    • Chae, H.Z.1    Oubrahim, H.2    Park, J.W.3    Rhee, S.G.4    Chock, P.B.5
  • 43
    • 79953871561 scopus 로고    scopus 로고
    • Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity
    • [43] Park, JW, Piszczek, G, Rhee, SG, Chock, PB., Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity. Biochemistry 50 (2011), 3204–3210.
    • (2011) Biochemistry , vol.50 , pp. 3204-3210
    • Park, J.W.1    Piszczek, G.2    Rhee, S.G.3    Chock, P.B.4
  • 44
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • [44] Park, JW, Mieyal, JJ, Rhee, SG, Chock, PB., Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. J. Biol. Chem. 284 (2009), 23364–23374.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23364-23374
    • Park, J.W.1    Mieyal, J.J.2    Rhee, S.G.3    Chock, P.B.4
  • 47
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid: immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • [47] Woo, HA, Kang, SW, Kim, HK, Yang, K-S, Chae, HZ, Rhee, SG., Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid: immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence. J. Biol. Chem. 278 (2003), 47361–47364.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.-S.4    Chae, H.Z.5    Rhee, S.G.6
  • 48
    • 78650177088 scopus 로고    scopus 로고
    • Influence of iNOS and COX on peroxiredoxin gene expression in primary macrophages
    • [48] Bast, A, Erttmann, SF, Walther, R, Steinmetz, I., Influence of iNOS and COX on peroxiredoxin gene expression in primary macrophages. Free Radic. Biol. Med. 49 (2010), 1881–1891.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1881-1891
    • Bast, A.1    Erttmann, S.F.2    Walther, R.3    Steinmetz, I.4
  • 49
    • 0035877718 scopus 로고    scopus 로고
    • Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex: transfer from CD14 to TLR4 and MD-2
    • [49] Da Silva Correia, J, Soldau, K, Christen, U, Tobias, PS, Ulevitch, RJ., Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex: transfer from CD14 to TLR4 and MD-2. J. Biol. Chem. 276 (2001), 21129–21135.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21129-21135
    • Da Silva Correia, J.1    Soldau, K.2    Christen, U.3    Tobias, P.S.4    Ulevitch, R.J.5
  • 51
    • 57649142987 scopus 로고    scopus 로고
    • Beta2-integrin-induced p38 MAPK activation is a key mediator in the CD14/TLR4/MD2-dependent uptake of lipopolysaccharide by hepatocytes
    • [51] Scott, MJ, Billiar, TR., Beta2-integrin-induced p38 MAPK activation is a key mediator in the CD14/TLR4/MD2-dependent uptake of lipopolysaccharide by hepatocytes. J. Biol. Chem. 283 (2008), 29433–29446.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29433-29446
    • Scott, M.J.1    Billiar, T.R.2
  • 52
    • 33746601126 scopus 로고    scopus 로고
    • Oxidative stress generated by hemorrhagic shock recruits Toll-like receptor 4 to the plasma membrane in macrophages
    • [52] Powers, KA, Szászi, K, Khadaroo, RG, Tawadros, PS, Marshall, JC, Kapus, A, Rotstein, OD., Oxidative stress generated by hemorrhagic shock recruits Toll-like receptor 4 to the plasma membrane in macrophages. J. Exp. Med. 203 (2006), 1951–1961.
    • (2006) J. Exp. Med. , vol.203 , pp. 1951-1961
    • Powers, K.A.1    Szászi, K.2    Khadaroo, R.G.3    Tawadros, P.S.4    Marshall, J.C.5    Kapus, A.6    Rotstein, O.D.7
  • 54
    • 28444454083 scopus 로고    scopus 로고
    • 1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome
    • [54] Guo, Y, Ma, SF, Grigoryev, D, Van Eyk, J, Barcia, JG., 1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome. Proteomics 5 (2005), 4608–4624.
    • (2005) Proteomics , vol.5 , pp. 4608-4624
    • Guo, Y.1    Ma, S.F.2    Grigoryev, D.3    Van Eyk, J.4    Barcia, J.G.5
  • 55
    • 0037015001 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage
    • [55] Manevich, Y, Sweitzer, T, Pak, JH, Feinstein, SI, Muzykantov, V, Fisher, AB., 1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage. Proc. Natl. Acad. Sci. USA 99 (2002), 11599–11604.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11599-11604
    • Manevich, Y.1    Sweitzer, T.2    Pak, J.H.3    Feinstein, S.I.4    Muzykantov, V.5    Fisher, A.B.6
  • 57
    • 77956174802 scopus 로고    scopus 로고
    • Comparison of glutathione peroxidase 1 and peroxiredoxin 6 in protection against stress in the mouse lung
    • [57] Liu, G, Feinstein, SI, Wang, Y, Dodia, C, Fisher, D, Yu, K, Ho, YS, Fisher, AB., Comparison of glutathione peroxidase 1 and peroxiredoxin 6 in protection against stress in the mouse lung. Free Radic. Biol. Med. 49 (2010), 1172–1181.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1172-1181
    • Liu, G.1    Feinstein, S.I.2    Wang, Y.3    Dodia, C.4    Fisher, D.5    Yu, K.6    Ho, Y.S.7    Fisher, A.B.8
  • 60
    • 49449116792 scopus 로고    scopus 로고
    • Oxidative innate immune defenses by Nox/Duox family NADPH oxidases
    • [60] Rada, B, Leto, TL., Oxidative innate immune defenses by Nox/Duox family NADPH oxidases. Contrib. Microbiol 15 (2008), 164–187.
    • (2008) Contrib. Microbiol , vol.15 , pp. 164-187
    • Rada, B.1    Leto, T.L.2
  • 65
  • 68
    • 84877105539 scopus 로고    scopus 로고
    • LPS-mediated endothelial activation in pulmonary endothelial cells: role of Nox2-dependent IKK-β phosphorylation
    • [68] Menden, H, Tate, E, Hogg, N, Sampath, V., LPS-mediated endothelial activation in pulmonary endothelial cells: role of Nox2-dependent IKK-β phosphorylation. Am. J. Physiol. Lung Cell. Mol. Physiol 304 (2013), L445–455.
    • (2013) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.304 , pp. L445-455
    • Menden, H.1    Tate, E.2    Hogg, N.3    Sampath, V.4
  • 69
    • 84905985979 scopus 로고    scopus 로고
    • Lambeth JD. Nox4: a hydrogen peroxide-generating oxygen sensor
    • [69] Nishimoto, Y, Diebold, BA, Cosentino-Gomes, D, Lambeth JD. Nox4: a hydrogen peroxide-generating oxygen sensor. Biochemistry 53 (2014), 5111–5120.
    • (2014) Biochemistry , vol.53 , pp. 5111-5120
    • Nishimoto, Y.1    Diebold, B.A.2    Cosentino-Gomes, D.3
  • 70
    • 4644350365 scopus 로고    scopus 로고
    • Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-κB
    • [70] Park, HS, Jung, HY, Park, EY, Kim, J, Lee, WJ, Bae, YS., Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-κB. J. Immunol. 173 (2004), 3589–3593.
    • (2004) J. Immunol. , vol.173 , pp. 3589-3593
    • Park, H.S.1    Jung, H.Y.2    Park, E.Y.3    Kim, J.4    Lee, W.J.5    Bae, Y.S.6
  • 71
    • 84900547292 scopus 로고    scopus 로고
    • Protection against LPS-induced acute lung injury by a mechanism-based inhibitor of NADPH oxidase (type 2)
    • [71] Lee, I, Dodia, C, Chatterjee, S, Feinstein, SI, Fisher, AB., Protection against LPS-induced acute lung injury by a mechanism-based inhibitor of NADPH oxidase (type 2). Am. J. Physiol. Lung Cell. Mol. Physiol 306 (2014), L635–644.
    • (2014) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.306 , pp. L635-644
    • Lee, I.1    Dodia, C.2    Chatterjee, S.3    Feinstein, S.I.4    Fisher, A.B.5
  • 72
    • 79953176614 scopus 로고    scopus 로고
    • Deletion of peroxiredoxin 6 potentiates lipopolysaccharide-induced acute lung injury in mice
    • [72] Yang, D, Song, Y, Wang, X, Sun, J, Ben, Y, An, X, Tong, L, Bi, J, Wang, X, Bai, C., Deletion of peroxiredoxin 6 potentiates lipopolysaccharide-induced acute lung injury in mice. Crit. Care Med. 39 (2011), 756–764.
    • (2011) Crit. Care Med. , vol.39 , pp. 756-764
    • Yang, D.1    Song, Y.2    Wang, X.3    Sun, J.4    Ben, Y.5    An, X.6    Tong, L.7    Bi, J.8    Wang, X.9    Bai, C.10
  • 80
    • 0030962545 scopus 로고    scopus 로고
    • Stereoselective conjugation of prostaglandin A2 and prostaglandin J2 with glutathione, catalyzed by the human glutathione S-transferases A1-1, A2-2, M1a-1a, and P1-1
    • [80] Bogaards, JJ, Venekamp, JC, van Bladeren, PJ., Stereoselective conjugation of prostaglandin A2 and prostaglandin J2 with glutathione, catalyzed by the human glutathione S-transferases A1-1, A2-2, M1a-1a, and P1-1. Chem. Res. Toxicol. 10 (1997), 310–317.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 310-317
    • Bogaards, J.J.1    Venekamp, J.C.2    van Bladeren, P.J.3
  • 81
    • 1442300929 scopus 로고    scopus 로고
    • inhibit transcriptional activation by the peroxisomal proliferator-activated receptor gamma (PPARγ) ligand, 15-d-∆12,14prostaglandin J2 (15-d-PGJ2)
    • [81] Paumi, CM, Smitherman, PK, Townsend, AJ, Morrow, CS., Glutathione S-transferases, (GSTs), inhibit transcriptional activation by the peroxisomal proliferator-activated receptor gamma (PPARγ) ligand, 15-d-∆12,14prostaglandin J2 (15-d-PGJ2). Biochemistry 43 (2004), 2345–2352.
    • (2004) Biochemistry , vol.43 , pp. 2345-2352
    • Paumi, C.M.1    Smitherman, P.K.2    Townsend, A.J.3    Morrow, C.S.4    Glutathione S-transferases, G.5
  • 82
    • 84870613866 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced expression of microsomal prostaglandin E synthase-1 mediates late-phase PGE2 production in bone marrow derived macrophages
    • [82] Xiao, L, Ornatowska, M, Zhao, G, Cao, H, Yu, R, Deng, J, Li, Y, Zhao, Q, Sadikot, RT, Christman, JW., Lipopolysaccharide-induced expression of microsomal prostaglandin E synthase-1 mediates late-phase PGE2 production in bone marrow derived macrophages. PLoS One, 7, 2012, e50244.
    • (2012) PLoS One , vol.7 , pp. e50244
    • Xiao, L.1    Ornatowska, M.2    Zhao, G.3    Cao, H.4    Yu, R.5    Deng, J.6    Li, Y.7    Zhao, Q.8    Sadikot, R.T.9    Christman, J.W.10
  • 83
    • 77954537848 scopus 로고    scopus 로고
    • Coordinated up-regulation of cyclooxygenase-2 and microsomal prostaglandin E synthase 1 transcription by nuclear factor kappa B and early growth response-1 in macrophages
    • [83] Díaz-Muñoz, MD, Osma-Garcia, IC, Cacheiro-Llaguno, C, Fresno, M, Iñiquez, MA., Coordinated up-regulation of cyclooxygenase-2 and microsomal prostaglandin E synthase 1 transcription by nuclear factor kappa B and early growth response-1 in macrophages. Cell. Signalling 22 (2010), 1427–1436.
    • (2010) Cell. Signalling , vol.22 , pp. 1427-1436
    • Díaz-Muñoz, M.D.1    Osma-Garcia, I.C.2    Cacheiro-Llaguno, C.3    Fresno, M.4    Iñiquez, M.A.5
  • 84
    • 0033594963 scopus 로고    scopus 로고
    • Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target
    • [84] Jakobsson, PJ, Thorén, S, Morgenstern, R, Samuelsson, B., Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc. Natl. Acad. Sci. USA 96 (1999), 7220–7225.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7220-7225
    • Jakobsson, P.J.1    Thorén, S.2    Morgenstern, R.3    Samuelsson, B.4
  • 86
    • 84859459694 scopus 로고    scopus 로고
    • Involvement of PGE2 and the cAMP signaling pathway in the upregulation of COX-2 and mPGES-1 expression in LPS-activated macrophages
    • [86] Díaz-Muñoz, MD, Osma-Garcia, IC, Fresno, M, Iñiquez, MA., Involvement of PGE2 and the cAMP signaling pathway in the upregulation of COX-2 and mPGES-1 expression in LPS-activated macrophages. Biochem. J. 443 (2012), 451–461.
    • (2012) Biochem. J. , vol.443 , pp. 451-461
    • Díaz-Muñoz, M.D.1    Osma-Garcia, I.C.2    Fresno, M.3    Iñiquez, M.A.4
  • 87
    • 84883430746 scopus 로고    scopus 로고
    • Remold HG. The prostaglandin E2 receptor EP4 is integral to a positive feedback loop for prostaglandin E2 production in human macrophages infected with Mycobacterium tuberculosis
    • [87] Nishimura, T, Zhao, X, Gan, H, Koyasu, S, Remold HG. The prostaglandin E2 receptor EP4 is integral to a positive feedback loop for prostaglandin E2 production in human macrophages infected with Mycobacterium tuberculosis. FASEB J 27 (2013), 3827–3836.
    • (2013) FASEB J , vol.27 , pp. 3827-3836
    • Nishimura, T.1    Zhao, X.2    Gan, H.3    Koyasu, S.4
  • 88
    • 84871552220 scopus 로고    scopus 로고
    • Pivotal role of reactive oxygen species in differential regulation of lipopolysaccharide-induced prostaglandins production in macrophages
    • [88] Zhao, G, Yu, R, Deng, J, Zhao, Q, Li, Y, Joo, M, van Breemen, RB, Christman, JW, Xiao, L., Pivotal role of reactive oxygen species in differential regulation of lipopolysaccharide-induced prostaglandins production in macrophages. Mol. Pharmacol. 83 (2013), 167–178.
    • (2013) Mol. Pharmacol. , vol.83 , pp. 167-178
    • Zhao, G.1    Yu, R.2    Deng, J.3    Zhao, Q.4    Li, Y.5    Joo, M.6    van Breemen, R.B.7    Christman, J.W.8    Xiao, L.9
  • 89
    • 0032527962 scopus 로고    scopus 로고
    • Sequence, catalytic properties and expression of chicken glutathione-dependent prostaglandin D2 synthase, a novel class Sigma glutathione S-transferase
    • [89] Thomson, AM, Meyer, DJ, Hayes, JD., Sequence, catalytic properties and expression of chicken glutathione-dependent prostaglandin D2 synthase, a novel class Sigma glutathione S-transferase. Biochem. J. 333 (1998), 317–325.
    • (1998) Biochem. J. , vol.333 , pp. 317-325
    • Thomson, A.M.1    Meyer, D.J.2    Hayes, J.D.3
  • 90
    • 0035504857 scopus 로고    scopus 로고
    • Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases
    • [90] Jowsey, IR, Thomson, AM, Flanagan, JU, Murdock, PR, Moore, GB, Meyer, DJ, Murphy, GJ, Smith, SA, Hayes, JD., Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases. Biochem. J. 359 (2001), 507–516.
    • (2001) Biochem. J. , vol.359 , pp. 507-516
    • Jowsey, I.R.1    Thomson, A.M.2    Flanagan, J.U.3    Murdock, P.R.4    Moore, G.B.5    Meyer, D.J.6    Murphy, G.J.7    Smith, S.A.8    Hayes, J.D.9
  • 92
    • 84908330354 scopus 로고    scopus 로고
    • Pro-oxidant activity of indicaxanthin from Opuntia ficus indica modulates arachidonate metabolism and prostaglandin synthesis through lipid peroxide production in LPS-stimulated RAW264.7 macrophages
    • [92] Allegra, M, D'Acquisto, F, Tesoriere, L, Attanzio, A, Livrea, MA., Pro-oxidant activity of indicaxanthin from Opuntia ficus indica modulates arachidonate metabolism and prostaglandin synthesis through lipid peroxide production in LPS-stimulated RAW264.7 macrophages. Redox Biol 2 (2014), 892–900.
    • (2014) Redox Biol , vol.2 , pp. 892-900
    • Allegra, M.1    D'Acquisto, F.2    Tesoriere, L.3    Attanzio, A.4    Livrea, M.A.5
  • 94
    • 63349098916 scopus 로고    scopus 로고
    • NADPH oxidase-derived reactive oxygen species are essential for differentiation of a mouse macrophage cell line (RAW264.7) into osteoclasts
    • [94] Sasaki, H, Yamamoto, H, Tominaga, K, Masuda, K, Kawai, T, Teshima-Kondo, S, Rokutan, K., NADPH oxidase-derived reactive oxygen species are essential for differentiation of a mouse macrophage cell line (RAW264.7) into osteoclasts. J. Med. Invest. 56 (2009), 33–41.
    • (2009) J. Med. Invest. , vol.56 , pp. 33-41
    • Sasaki, H.1    Yamamoto, H.2    Tominaga, K.3    Masuda, K.4    Kawai, T.5    Teshima-Kondo, S.6    Rokutan, K.7
  • 95
    • 45449098664 scopus 로고    scopus 로고
    • Strain differences regarding susceptibility to ursolic acid-induced interleukin-1β release in murine macrophages
    • [95] Ikeda, Y, Murakami, A, Ohigashi, H., Strain differences regarding susceptibility to ursolic acid-induced interleukin-1β release in murine macrophages. Life Sci. 83 (2008), 43–49.
    • (2008) Life Sci. , vol.83 , pp. 43-49
    • Ikeda, Y.1    Murakami, A.2    Ohigashi, H.3
  • 96
    • 84892662851 scopus 로고    scopus 로고
    • Indicaxanthin from cactus pear fruit exerts anti-inflammatory effects in carrageenan-induced rat pleurisy
    • [96] Allegra, M, Ianaro, A, Tersigni, M, Panza, E, Tesoriere, L, Livrea, MA., Indicaxanthin from cactus pear fruit exerts anti-inflammatory effects in carrageenan-induced rat pleurisy. J. Nutr. 144 (2014), 185–192.
    • (2014) J. Nutr. , vol.144 , pp. 185-192
    • Allegra, M.1    Ianaro, A.2    Tersigni, M.3    Panza, E.4    Tesoriere, L.5    Livrea, M.A.6
  • 97
    • 79961014471 scopus 로고    scopus 로고
    • Selenoprotein-dependent up-regulation of hematopoietic prostaglandin D2 synthase in macrophages is mediated through the activation of peroxisome proliferator-activated receptor (PPAR) γ
    • [97] Gandhi, UH, Kaushal, N, Ravindra, KC, Hegde, S, Nelson, SM, Narayan, V, Vunta, H, Paulson, RF, Prabhu, KS., Selenoprotein-dependent up-regulation of hematopoietic prostaglandin D2 synthase in macrophages is mediated through the activation of peroxisome proliferator-activated receptor (PPAR) γ. J. Biol. Chem. 286 (2011), 27471–27482.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27471-27482
    • Gandhi, U.H.1    Kaushal, N.2    Ravindra, K.C.3    Hegde, S.4    Nelson, S.M.5    Narayan, V.6    Vunta, H.7    Paulson, R.F.8    Prabhu, K.S.9
  • 98
    • 84864914338 scopus 로고    scopus 로고
    • PGD synthases and PGD2 in immune response
    • [98] Joo, M, Sadikot, RT., PGD synthases and PGD2 in immune response. Mediators Inflammation, 2012, 2012, 503128.
    • (2012) Mediators Inflammation , vol.2012 , pp. 503128
    • Joo, M.1    Sadikot, R.T.2
  • 99
    • 66149161799 scopus 로고    scopus 로고
    • Lipopolysaccharide-dependent interaction between PU.1 and cJun determines production of lipocalin-type prostaglandin D synthase and prostaglandin D2 in macrophages
    • [99] Joo, M, Kwon, M, Cho, Y-J, Hu, N, Pedchenko, TV, Sadikot, RT, Blackwell, TS, Christman, JW., Lipopolysaccharide-dependent interaction between PU.1 and cJun determines production of lipocalin-type prostaglandin D synthase and prostaglandin D2 in macrophages. Am. J. Physiol. Lung Cell. Mol. Physiol 296 (2009), L771–779.
    • (2009) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.296 , pp. L771-779
    • Joo, M.1    Kwon, M.2    Cho, Y.-J.3    Hu, N.4    Pedchenko, T.V.5    Sadikot, R.T.6    Blackwell, T.S.7    Christman, J.W.8
  • 103
    • 84915745381 scopus 로고    scopus 로고
    • Dexamethasone protects neonatal hypoxic–ischemic brain injury via L-PGDS-dependent PGD2–DP1–pERK signaling pathway
    • [103] Gonzalez-Rodriguez, PJ, Li, Y, Martinez, F, Zhang, L., Dexamethasone protects neonatal hypoxic–ischemic brain injury via L-PGDS-dependent PGD2–DP1–pERK signaling pathway. PLoS One, 9, 2014, e114470.
    • (2014) PLoS One , vol.9 , pp. e114470
    • Gonzalez-Rodriguez, P.J.1    Li, Y.2    Martinez, F.3    Zhang, L.4
  • 104
    • 84926665590 scopus 로고    scopus 로고
    • The new deal: a potential role for secreted vesicles in innate immunity and tumor progression
    • [104] Benito-Martin, A, Giannatale, AD, Ceder, S, Peinado, H., The new deal: a potential role for secreted vesicles in innate immunity and tumor progression. Front. Immunol, 6, 2015, 66.
    • (2015) Front. Immunol , vol.6 , pp. 66
    • Benito-Martin, A.1    Giannatale, A.D.2    Ceder, S.3    Peinado, H.4
  • 105
    • 84926637754 scopus 로고    scopus 로고
    • Exosomes: tiny clues for mast cell communication
    • [105] D'Incá, F, Pucillo, CE., Exosomes: tiny clues for mast cell communication. Front. Immunol, 6, 2015, 73.
    • (2015) Front. Immunol , vol.6 , pp. 73
    • D'Incá, F.1    Pucillo, C.E.2
  • 106
    • 0029888411 scopus 로고    scopus 로고
    • Recombinant natural killer enhancing factor augments natural killer cytotoxicity
    • [106] Sauri, H, Ashjian, PH, Kim, AT, Shau, H., Recombinant natural killer enhancing factor augments natural killer cytotoxicity. J. Leukocyte Biol. 59 (1996), 925–931.
    • (1996) J. Leukocyte Biol. , vol.59 , pp. 925-931
    • Sauri, H.1    Ashjian, P.H.2    Kim, A.T.3    Shau, H.4
  • 107
    • 0037449797 scopus 로고    scopus 로고
    • Luster AD, Walker BD. HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family
    • [107] Geiben-Lynn, R, Kursar, M, Brown, NV, Addo, MM, Shau, H, Lieberman, J, Luster AD, Walker BD. HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family. J. Biol. Chem. 278 (2003), 1569–1574.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1569-1574
    • Geiben-Lynn, R.1    Kursar, M.2    Brown, N.V.3    Addo, M.M.4    Shau, H.5    Lieberman, J.6
  • 111
    • 84892967156 scopus 로고    scopus 로고
    • Resveratrol regulates type II collagen and COX-2 expression via the ERK, p38 and Akt signaling pathways in rabbit articular chondrocytes
    • [111] Eo, S-H, Cho, H-S, Kim, S-J., Resveratrol regulates type II collagen and COX-2 expression via the ERK, p38 and Akt signaling pathways in rabbit articular chondrocytes. Exp. Ther. Med 7 (2014), 640–648.
    • (2014) Exp. Ther. Med , vol.7 , pp. 640-648
    • Eo, S.-H.1    Cho, H.-S.2    Kim, S.-J.3


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