메뉴 건너뛰기




Volumn 11, Issue 12, 2010, Pages 1541-1550

Heme oxygenase-1 and iron in liver inflammation: A complex alliance

Author keywords

Antioxidant; Heme oxygenase 1; Hepcidin; Inflammation; Iron; Liver; Oxidative stress

Indexed keywords

AMINOETHYLBENZENSULFONYL FLUORIDE; ANTIINFLAMMATORY AGENT; CORTICOSTEROID; CURCUMIN; GINKGO BILOBA EXTRACT; HEME OXYGENASE 1; HEPCIDIN; IRON; IRON REGULATORY PROTEIN 1; MICRORNA; PEGINTERFERON; PENTOXIFYLLINE; POLYPHENOL; RIBAVIRIN; UNCLASSIFIED DRUG; NONSTEROID ANTIINFLAMMATORY AGENT;

EID: 78149428559     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450111009011541     Document Type: Review
Times cited : (53)

References (131)
  • 1
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen R, Marver HS, Schmid R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc Natl Acad Sci USA 1968; 61: 748-55.
    • (1968) Proc Natl Acad Sci USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD. The heme oxygenase system: a regulator of second messenger gases. Annu Rev Pharmacol Toxicol 1997; 37: 517-54.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 3
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From basic science to therapeutic applications
    • Ryter SW, Alam J, Choi AM. Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. Physiol Rev 2006; 86: 583-650.
    • (2006) Physiol Rev , vol.86 , pp. 583-650
    • Ryter, S.W.1    Alam, J.2    Choi, A.M.3
  • 4
    • 61549122310 scopus 로고    scopus 로고
    • Pleiotropic functions of biliverdin reductase: Cellular signaling and generation of cytoprotective and cytotoxic bilirubin
    • Kapitulnik J, Maines MD. Pleiotropic functions of biliverdin reductase: cellular signaling and generation of cytoprotective and cytotoxic bilirubin. Trends Pharmacol Sci 2009; 30: 129-37.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 129-137
    • Kapitulnik, J.1    Maines, M.D.2
  • 5
    • 0022977615 scopus 로고
    • Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform
    • Trakshel GM, Kutty RK, Maines MD. Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform. J Biol Chem 1986 25; 261: 11131-7.
    • (1986) J Biol Chem , vol.25 , Issue.261 , pp. 11131-11137
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 6
    • 0030188587 scopus 로고    scopus 로고
    • Heme oxygenase-1: Function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury
    • Choi AMK, Alam J. Heme oxygenase-1: Function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury. Am J Respir Cell Mol Biol 1996; 15: 9-19.
    • (1996) Am J Respir Cell Mol Biol , vol.15 , pp. 9-19
    • Choi, A.M.K.1    Alam, J.2
  • 7
    • 0034668216 scopus 로고    scopus 로고
    • Gene regulation of heme oxygenase-1 as a therapeutic target
    • Immenschuh S, Ramadori G. Gene regulation of heme oxygenase-1 as a therapeutic target. Biochem Pharmacol 2000; 60: 1121-8.
    • (2000) Biochem Pharmacol , vol.60 , pp. 1121-1128
    • Immenschuh, S.1    Ramadori, G.2
  • 8
    • 0025105624 scopus 로고
    • Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts
    • Keyse SM, Applegate LA, Tromvoukis Y, Tyrrell RM. Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts. Mol Cell Biol 1990; 10: 4967-9.
    • (1990) Mol Cell Biol , vol.10 , pp. 4967-4969
    • Keyse, S.M.1    Applegate, L.A.2    Tromvoukis, Y.3    Tyrrell, R.M.4
  • 9
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • Vile GF, Basu-Modak S, Waltner C, Tyrrell RM. Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc Natl Acad Sci USA 1994 29; 91: 2607-10.
    • (1994) Proc Natl Acad Sci USA , vol.29 , Issue.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 12
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss KD, Tonegawa S. Reduced stress defense in heme oxygenase 1-deficient cells. Proc Natl Acad Sci USA 1997; 94: 10925-30.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 13
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase is required for mammalian iron reutilization
    • Poss KD, Tonegawa S. Heme oxygenase is required for mammalian iron reutilization. Proc Natl Acad Sci USA 1997; 94: 10919-24.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 14
    • 0032893958 scopus 로고    scopus 로고
    • Oxidative stress causes enhanced endothelial cell injury in human heme oxygenasedeficiency
    • Yachie A, Niida Y, Wada T, et al. Oxidative stress causes enhanced endothelial cell injury in human heme oxygenasedeficiency. J Clin Invest 1999; 103: 129-35.
    • (1999) J Clin Invest , vol.103 , pp. 129-135
    • Yachie, A.1    Niida, Y.2    Wada, T.3
  • 16
    • 0031913770 scopus 로고    scopus 로고
    • Ejaculatory abnormalities in mice with targeted disruption of the gene for heme oxygenase-2
    • Burnett AL, Johns DG, Kriegsfeld LJ, et al. Ejaculatory abnormalities in mice with targeted disruption of the gene for heme oxygenase-2. Nat Med 1998; 4: 84-7.
    • (1998) Nat Med , vol.4 , pp. 84-87
    • Burnett, A.L.1    Johns, D.G.2    Kriegsfeld, L.J.3
  • 17
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC. Balancing acts: molecular control of mammalian iron metabolism. Cell 2004 30; 117: 285-97.
    • (2004) Cell , vol.30 , Issue.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 19
  • 20
    • 0033599057 scopus 로고    scopus 로고
    • Disorders of iron metabolism
    • Andrews NC. Disorders of iron metabolism. N Engl J Med 1999; 341:1986-95.
    • (1999) N Engl J Med , vol.341 , pp. 1986-1995
    • Andrews, N.C.1
  • 21
    • 0025230751 scopus 로고
    • The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution
    • Rothenberger S, Mullner EW, Kuhn LC. The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution. Nucleic Acids Res 1990; 18: 1175-9.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1175-1179
    • Rothenberger, S.1    Mullner, E.W.2    Kuhn, L.C.3
  • 22
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H, Holm RH, Munck E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 1997; 277: 653-9.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 23
    • 0030624029 scopus 로고    scopus 로고
    • Regulation of iron metabolism in eukaryotes
    • Rouault T, Klausner R. Regulation of iron metabolism in eukaryotes. Curr Top Cell Regul 1997; 35: 1-19.
    • (1997) Curr Top Cell Regul , vol.35 , pp. 1-19
    • Rouault, T.1    Klausner, R.2
  • 24
    • 0347988153 scopus 로고    scopus 로고
    • Blotting analysis of native IRP1: A novel approach to distinguish the different forms of IRP1 in cells and tissues
    • Campanella A, Levi S, Cairo G, Biasiotto G, Arosio P. Blotting analysis of native IRP1: a novel approach to distinguish the different forms of IRP1 in cells and tissues. Biochemistry 2004; 43: 195-204.
    • (2004) Biochemistry , vol.43 , pp. 195-204
    • Campanella, A.1    Levi, S.2    Cairo, G.3    Biasiotto, G.4    Arosio, P.5
  • 25
    • 0034717027 scopus 로고    scopus 로고
    • The aconitase function of iron regulatory protein 1. Genetic studies in yeast implicate its role in iron-mediated redox regulation
    • Narahari J, Ma R, Wang M, Walden WE. The aconitase function of iron regulatory protein 1. Genetic studies in yeast implicate its role in iron-mediated redox regulation. J Biol Chem 2000 26; 275: 16227-34.
    • (2000) J Biol Chem , vol.26 , Issue.275 , pp. 16227-16234
    • Narahari, J.1    Ma, R.2    Wang, M.3    Walden, W.E.4
  • 26
    • 0036358643 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 (IRP1) by oxidative stress
    • Mueller S, Pantopoulos K. Activation of iron regulatory protein-1 (IRP1) by oxidative stress. Methods Enzymol 2002; 348: 324-37.
    • (2002) Methods Enzymol , vol.348 , pp. 324-337
    • Mueller, S.1    Pantopoulos, K.2
  • 27
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann N Y Acad Sci 2004; 1012: 1-13.
    • (2004) Ann N Y Acad Sci , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 28
  • 29
    • 0030942257 scopus 로고    scopus 로고
    • Differences in the regulation of IRP-1 (iron regulatory protein-1) by extra-and intracelullar oxidative stress
    • Pantopoulos K, Mueller S, Atzberger A, Ansorge W, Stremmel W, Hentze MW. Differences in the regulation of IRP-1 (iron regulatory protein-1) by extra-and intracelullar oxidative stress. J Biol Chem 1997; 272: 9802-8.
    • (1997) J Biol Chem , vol.272 , pp. 9802-9808
    • Pantopoulos, K.1    Mueller, S.2    Atzberger, A.3    Ansorge, W.4    Stremmel, W.5    Hentze, M.W.6
  • 30
    • 17144445166 scopus 로고    scopus 로고
    • Myeloperoxidase-derived hypochlorous acid antagonizes the oxidative stress-mediated activation of iron regulatory protein 1
    • Mütze S, Hebling U, Stremmel W, et al. Myeloperoxidase-derived hypochlorous acid antagonizes the oxidative stress-mediated activation of iron regulatory protein 1. J Biol Chem 2003; 278: 40542-9.
    • (2003) J Biol Chem , vol.278 , pp. 40542-40549
    • Mütze, S.1    Hebling, U.2    Stremmel, W.3
  • 31
    • 0029972895 scopus 로고    scopus 로고
    • Nitric oxide and oxidative stress (H2O2) control mammalian iron metabolism by different pathways
    • Pantopoulos K, Weiss G, Hentze MW. Nitric oxide and oxidative stress (H2O2) control mammalian iron metabolism by different pathways. Mol Cell Biol 1996; 16: 3781-8.
    • (1996) Mol Cell Biol , vol.16 , pp. 3781-3788
    • Pantopoulos, K.1    Weiss, G.2    Hentze, M.W.3
  • 32
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E, Rivera S, Gabayan V, et al. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J Clin Invest 2004; 113: 1271-6.
    • (2004) J Clin Invest , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3
  • 33
    • 13444252281 scopus 로고    scopus 로고
    • Iron release from macrophages after erythrophagocytosis is upregulated by ferroportin 1 overexpression and down-regulated by hepcidin
    • Knutson MD, Oukka M, Koss LM, Aydemir F, Wessling-Resnick M. Iron release from macrophages after erythrophagocytosis is upregulated by ferroportin 1 overexpression and down-regulated by hepcidin. Proc Natl Acad Sci USA 2005; 102: 1324-8.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1324-1328
    • Knutson, M.D.1    Oukka, M.2    Koss, L.M.3    Aydemir, F.4    Wessling-Resnick, M.5
  • 34
    • 33750133047 scopus 로고    scopus 로고
    • Regulation of iron metabolism by hepcidin
    • Nemeth E, Ganz T. Regulation of iron metabolism by hepcidin. Annu Rev Nutr 2006; 26: 323-42.
    • (2006) Annu Rev Nutr , vol.26 , pp. 323-342
    • Nemeth, E.1    Ganz, T.2
  • 35
    • 0035896581 scopus 로고    scopus 로고
    • A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload
    • Pigeon C, Ilyin G, Courselaud B, et al. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J Biol Chem 2001; 276: 7811-9.
    • (2001) J Biol Chem , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3
  • 36
    • 14744278436 scopus 로고    scopus 로고
    • Anemia of chronic disease
    • Weiss G, Goodnough LT. Anemia of chronic disease. N Engl J Med 2005; 352: 1011-23.
    • (2005) N Engl J Med , vol.352 , pp. 1011-1023
    • Weiss, G.1    Goodnough, L.T.2
  • 37
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • Nicolas G, Chauvet C, Viatte L, et al. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J Clin Invest 2002; 110: 1037-44.
    • (2002) J Clin Invest , vol.110 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3
  • 38
    • 0037564038 scopus 로고    scopus 로고
    • Expression of hepcidin in hereditary hemochromatosis: Evidence for a regulation in response to the serum transferrin saturation and to non-transferrinbound iron
    • Gehrke SG, Kulaksiz H, Herrmann T, et al. Expression of hepcidin in hereditary hemochromatosis: evidence for a regulation in response to the serum transferrin saturation and to non-transferrinbound iron. Blood 2003; 102: 371-6.
    • (2003) Blood , vol.102 , pp. 371-376
    • Gehrke, S.G.1    Kulaksiz, H.2    Herrmann, T.3
  • 39
    • 0037460697 scopus 로고    scopus 로고
    • Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis
    • Bridle KR, Frazer DM, Wilkins SJ, et al. Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis. Lancet 2003; 361: 669-73.
    • (2003) Lancet , vol.361 , pp. 669-673
    • Bridle, K.R.1    Frazer, D.M.2    Wilkins, S.J.3
  • 40
    • 77449083073 scopus 로고    scopus 로고
    • Hepcidin suppression and defective iron recycling account for dysregulation of iron homeostasis in heme oxygenase-1 deficiency
    • Kartikasari AE, Wagener FA, Yachie A, Wiegerinck ET, Kemna EH, Winkels DW. Hepcidin suppression and defective iron recycling account for dysregulation of iron homeostasis in heme oxygenase-1 deficiency. J Cell Mol Med 2009; 13: 3091-102.
    • (2009) J Cell Mol Med , vol.13 , pp. 3091-3102
    • Kartikasari, A.E.1    Wagener, F.A.2    Yachie, A.3    Wiegerinck, E.T.4    Kemna, E.H.5    Winkels, D.W.6
  • 41
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • Ganz T. Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 2003; 102: 783-8.
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 42
    • 33744517652 scopus 로고    scopus 로고
    • Iron, HCV, and liver cancer: Hard metal setting the pace?
    • Mueller S, Afdhal NH, Schuppan D. Iron, HCV, and liver cancer: hard metal setting the pace? Gastroenterology 2006; 130: 2229-34.
    • (2006) Gastroenterology , vol.130 , pp. 2229-2234
    • Mueller, S.1    Afdhal, N.H.2    Schuppan, D.3
  • 43
    • 0029834842 scopus 로고    scopus 로고
    • Iron overload in patients with chronic hepatitis C: A clinicopathologic study
    • Haque S, Chandra B, Gerber MA, Lok AS. Iron overload in patients with chronic hepatitis C: a clinicopathologic study. Hum Pathol 1996; 27: 1277-81.
    • (1996) Hum Pathol , vol.27 , pp. 1277-1281
    • Haque, S.1    Chandra, B.2    Gerber, M.A.3    Lok, A.S.4
  • 44
    • 0041382552 scopus 로고    scopus 로고
    • Iron as a co-morbid factor in nonhemochromatotic liver disease
    • Bonkovsky HL, Lambrecht RW, Shan Y. Iron as a co-morbid factor in nonhemochromatotic liver disease. Alcohol 2003;30: 137-44.
    • (2003) Alcohol , vol.30 , pp. 137-144
    • Bonkovsky, H.L.1    Lambrecht, R.W.2    Shan, Y.3
  • 45
    • 0028609224 scopus 로고
    • Iron metabolism in inflammation
    • Konijn AM. Iron metabolism in inflammation. Baillieres Clin Haematol 1994; 7: 829-49.
    • (1994) Baillieres Clin Haematol , vol.7 , pp. 829-849
    • Konijn, A.M.1
  • 46
    • 2442426523 scopus 로고    scopus 로고
    • An Hfe-dependent pathway mediates hyposideremia in response to lipopolysaccharide-induced inflammation in mice
    • Roy CN, Custodio AO, de Graaf J, et al. An Hfe-dependent pathway mediates hyposideremia in response to lipopolysaccharide-induced inflammation in mice. Nat Genet 2004; 36: 481-5.
    • (2004) Nat Genet , vol.36 , pp. 481-485
    • Roy, C.N.1    Custodio, A.O.2    de Graaf, J.3
  • 47
    • 47149095786 scopus 로고    scopus 로고
    • Nramp1 equips macrophages for efficient iron recycling
    • Soe-Lin S, Sheftel AD, Wasyluk B, Ponka P. Nramp1 equips macrophages for efficient iron recycling. Exp Hematol 2008; 36: 929-37.
    • (2008) Exp Hematol , vol.36 , pp. 929-937
    • Soe-Lin, S.1    Sheftel, A.D.2    Wasyluk, B.3    Ponka, P.4
  • 48
    • 0025969686 scopus 로고
    • Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron
    • Eisenstein RS, Garcia-Mayol D, Pettingell W, Munro HN. Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. Proc Natl Acad Sci USA 1991; 88: 688-92.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 688-692
    • Eisenstein, R.S.1    Garcia-Mayol, D.2    Pettingell, W.3    Munro, H.N.4
  • 49
    • 0026657174 scopus 로고
    • Ferritin: A cytoprotective antioxidant strategem of endothelium
    • Balla G, Jacob HS, Balla J, et al. Ferritin: a cytoprotective antioxidant strategem of endothelium. J Biol Chem 1992; 267: 18148-53.
    • (1992) J Biol Chem , vol.267 , pp. 18148-18153
    • Balla, G.1    Jacob, H.S.2    Balla, J.3
  • 50
    • 0027255106 scopus 로고
    • Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenasedependent increase in ferritin
    • Vile GF, Tyrrell RM. Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenasedependent increase in ferritin. J Biol Chem 1993; 268: 14678-81.
    • (1993) J Biol Chem , vol.268 , pp. 14678-14681
    • Vile, G.F.1    Tyrrell, R.M.2
  • 51
    • 0345688910 scopus 로고    scopus 로고
    • Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages
    • Knutson MD, Vafa MR, Haile DJ, Wessling-Resnick M. Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages. Blood 2003; 102: 4191-7.
    • (2003) Blood , vol.102 , pp. 4191-4197
    • Knutson, M.D.1    Vafa, M.R.2    Haile, D.J.3    Wessling-Resnick, M.4
  • 52
    • 41649110613 scopus 로고    scopus 로고
    • Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: Early mRNA induction by haem, followed by iron-dependent protein expression
    • Delaby C, Pilard N, Puy H, Canonne-Hergaux F. Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: early mRNA induction by haem, followed by iron-dependent protein expression. Biochem J 2008; 411: 123-31.
    • (2008) Biochem J , vol.411 , pp. 123-131
    • Delaby, C.1    Pilard, N.2    Puy, H.3    Canonne-Hergaux, F.4
  • 53
    • 77953713414 scopus 로고    scopus 로고
    • Heme controls ferroportin 1(FPN1) transcription involving Bach1, Nrf2 and MARE/ARE sequence motif at position-7007 of the FPN1 promoter
    • Marro S, Chiabrando D, Messana E, et al. Heme controls ferroportin 1(FPN1) transcription involving Bach1, Nrf2 and MARE/ARE sequence motif at position-7007 of the FPN1 promoter. Haematologica 2010; 95: 1261-8.
    • (2010) Haematologica , vol.95 , pp. 1261-1268
    • Marro, S.1    Chiabrando, D.2    Messana, E.3
  • 54
    • 0023876497 scopus 로고
    • Iron metabolism in the erythrophagocytosing Kupffer cell
    • Kondo H, Saito K, Grasso JP, Aisen P. Iron metabolism in the erythrophagocytosing Kupffer cell. Hepatology 1988; 8: 32-8.
    • (1988) Hepatology , vol.8 , pp. 32-38
    • Kondo, H.1    Saito, K.2    Grasso, J.P.3    Aisen, P.4
  • 55
    • 0032031707 scopus 로고    scopus 로고
    • Oxygen toxicity and iron accumulation in the lungs of mice lacking heme oxygenase-2
    • Dennery PA, Spitz DR, Yang G, et al. Oxygen toxicity and iron accumulation in the lungs of mice lacking heme oxygenase-2. J Clin Invest 1998; 101: 1001-11.
    • (1998) J Clin Invest , vol.101 , pp. 1001-1011
    • Dennery, P.A.1    Spitz, D.R.2    Yang, G.3
  • 56
    • 37349070339 scopus 로고    scopus 로고
    • Heme oxygenase-1 deficiency accelerates formation of arterial thrombosis through oxidative damage to the endothelium, which is rescued by inhaled carbon monoxide
    • True AL, Olive M, Boehm M, et al. Heme oxygenase-1 deficiency accelerates formation of arterial thrombosis through oxidative damage to the endothelium, which is rescued by inhaled carbon monoxide. Circ Res 2007; 101: 893-901.
    • (2007) Circ Res , vol.101 , pp. 893-901
    • True, A.L.1    Olive, M.2    Boehm, M.3
  • 57
    • 12244304860 scopus 로고    scopus 로고
    • Resistance to hyperoxia with heme oxygenase-1 disruption: Role of iron
    • Dennery PA, Visner G, Weng YH, et al. Resistance to hyperoxia with heme oxygenase-1 disruption: role of iron. Free Radic Biol Med 2003; 34: 124-33.
    • (2003) Free Radic Biol Med , vol.34 , pp. 124-133
    • Dennery, P.A.1    Visner, G.2    Weng, Y.H.3
  • 58
    • 66049098514 scopus 로고    scopus 로고
    • Myeloid heme oxygenase-1 regulates innate immunity and autoimmunity by modulating IFN-beta production
    • Tzima S, Victoratos P, Kranidioti K, Alexiou M, Kollias G. Myeloid heme oxygenase-1 regulates innate immunity and autoimmunity by modulating IFN-beta production. J Exp Med 2009; 206: 1167-79.
    • (2009) J Exp Med , vol.206 , pp. 1167-1179
    • Tzima, S.1    Victoratos, P.2    Kranidioti, K.3    Alexiou, M.4    Kollias, G.5
  • 59
    • 0031915553 scopus 로고    scopus 로고
    • Expression pattern of heme oxygenase isoenzymes 1 and 2 in normal and stress-exposed rat liver
    • Bauer I, Wanner GA, Rensing H, et al. Expression pattern of heme oxygenase isoenzymes 1 and 2 in normal and stress-exposed rat liver. Hepatology 1998; 27: 829-38.
    • (1998) Hepatology , vol.27 , pp. 829-838
    • Bauer, I.1    Wanner, G.A.2    Rensing, H.3
  • 60
    • 0032921697 scopus 로고    scopus 로고
    • Nitric oxide mediates the lipopolysaccharide dependent upregulation of the heme oxygenase-1 gene expression in cultured rat Kupffer cells
    • Immenschuh S, Tan M, Ramadori G. Nitric oxide mediates the lipopolysaccharide dependent upregulation of the heme oxygenase-1 gene expression in cultured rat Kupffer cells. J Hepatol 1999;30: 61-9.
    • (1999) J Hepatol , vol.30 , pp. 61-69
    • Immenschuh, S.1    Tan, M.2    Ramadori, G.3
  • 61
    • 0041967387 scopus 로고    scopus 로고
    • Different faces of the heme-heme oxygenase system in inflammation
    • Wagener FA, Volk HD, Willis D, et al. Different faces of the heme-heme oxygenase system in inflammation. Pharmacol Rev 2003; 55: 551-71.
    • (2003) Pharmacol Rev , vol.55 , pp. 551-571
    • Wagener, F.A.1    Volk, H.D.2    Willis, D.3
  • 63
    • 35948985622 scopus 로고    scopus 로고
    • Innate immune response and hepatic inflammation
    • Szabo G, Mandrekar P, Dolganiuc A. Innate immune response and hepatic inflammation. Semin Liver Dis 2007; 27: 339-50.
    • (2007) Semin Liver Dis , vol.27 , pp. 339-350
    • Szabo, G.1    Mandrekar, P.2    Dolganiuc, A.3
  • 64
    • 0036074141 scopus 로고    scopus 로고
    • Lipopolysaccharides in liver injury: Molecular mechanisms of Kupffer cell activation
    • Su GL. Lipopolysaccharides in liver injury: molecular mechanisms of Kupffer cell activation. Am J Physiol Gastrointest Liver Physiol 2002; 283: G256-65.
    • (2002) Am J Physiol Gastrointest Liver Physiol , vol.283
    • Su, G.L.1
  • 65
    • 33644544110 scopus 로고    scopus 로고
    • The liver as an immunological organ
    • Racanelli V, Rehermann B. The liver as an immunological organ. Hepatology 2006; 43: S54-62.
    • (2006) Hepatology , vol.43 , pp. 54-62
    • Racanelli, V.1    Rehermann, B.2
  • 66
    • 61949261267 scopus 로고    scopus 로고
    • Inflammatory pathways in liver homeostasis and liver injury
    • Tacke F, Luedde T, Trautwein C. Inflammatory pathways in liver homeostasis and liver injury. Clin Rev Allergy Immunol 2009; 36: 4-12.
    • (2009) Clin Rev Allergy Immunol , vol.36 , pp. 4-12
    • Tacke, F.1    Luedde, T.2    Trautwein, C.3
  • 67
    • 0036127426 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the antiinflammatory effect of interleukin-10 in mice
    • Lee TS, Chau LY. Heme oxygenase-1 mediates the antiinflammatory effect of interleukin-10 in mice. Nat Med 2002; 8: 240-6.
    • (2002) Nat Med , vol.8 , pp. 240-246
    • Lee, T.S.1    Chau, L.Y.2
  • 68
    • 4344566310 scopus 로고    scopus 로고
    • Heme oxygenase-1 modulates early inflammatory responses: Evidence from the heme oxygenase-1-deficient mouse
    • Kapturczak MH, Wasserfall C, Brusko T, et al. Heme oxygenase-1 modulates early inflammatory responses: evidence from the heme oxygenase-1-deficient mouse. Am J Pathol 2004; 165: 1045-53.
    • (2004) Am J Pathol , vol.165 , pp. 1045-1053
    • Kapturczak, M.H.1    Wasserfall, C.2    Brusko, T.3
  • 69
    • 33846924300 scopus 로고    scopus 로고
    • How many transcription factors does it take to turn on the heme oxygenase-1 gene?
    • Alam J, Cook JL. How many transcription factors does it take to turn on the heme oxygenase-1 gene? Am J Respir Cell Mol Biol 2007; 36: 166-74.
    • (2007) Am J Respir Cell Mol Biol , vol.36 , pp. 166-174
    • Alam, J.1    Cook, J.L.2
  • 70
    • 33645530745 scopus 로고    scopus 로고
    • Nrf2 is a critical regulator of the innate immune response and survival during experimental sepsis
    • Thimmulappa RK, Lee H, Rangasamy T, et al. Nrf2 is a critical regulator of the innate immune response and survival during experimental sepsis. J Clin Invest 2006; 116: 984-95.
    • (2006) J Clin Invest , vol.116 , pp. 984-995
    • Thimmulappa, R.K.1    Lee, H.2    Rangasamy, T.3
  • 71
    • 57349116768 scopus 로고    scopus 로고
    • Coordinate regulation of enzyme markers for inflammation and for protection against oxidants and electrophiles
    • Liu H, Dinkova-Kostova AT, Talalay P. Coordinate regulation of enzyme markers for inflammation and for protection against oxidants and electrophiles. Proc Natl Acad Sci USA 2008; 105: 15926-31.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15926-15931
    • Liu, H.1    Dinkova-Kostova, A.T.2    Talalay, P.3
  • 72
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • Kensler TW, Wakabayashi N, Biswal S. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol 2007; 47: 89-116.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 73
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant response elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, et al. Keap1 represses nuclear activation of antioxidant response elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 1999; 13: 76-86.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3
  • 74
    • 14044254798 scopus 로고    scopus 로고
    • Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation
    • Kobayashi M, Yamamoto M. Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation. Antioxid Redox Signal 2005; 7: 385-94.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 385-394
    • Kobayashi, M.1    Yamamoto, M.2
  • 75
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M, Kurokawa H, Waguri S, et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat Cell Biol 2010; 12: 213-23.
    • (2010) Nat Cell Biol , vol.12 , pp. 213-223
    • Komatsu, M.1    Kurokawa, H.2    Waguri, S.3
  • 76
    • 0027953712 scopus 로고
    • Differential effects of metalloporphyrins on messenger RNA levels of d-aminolevulinate synthase and heme oxygenase
    • Cable EE, Pepe JA, Karamtsios NC, Lambrecht RW, Bonkovsky HL. Differential effects of metalloporphyrins on messenger RNA levels of d-aminolevulinate synthase and heme oxygenase. J Clin Invest 1994; 94: 649-54.
    • (1994) J Clin Invest , vol.94 , pp. 649-654
    • Cable, E.E.1    Pepe, J.A.2    Karamtsios, N.C.3    Lambrecht, R.W.4    Bonkovsky, H.L.5
  • 77
    • 8544284074 scopus 로고    scopus 로고
    • The antioxidant defense protein heme oxygenase 1 is a novel target for statins in endothelial cells
    • Grosser N, Hemmerle A, Berndt G, et al. The antioxidant defense protein heme oxygenase 1 is a novel target for statins in endothelial cells. Free Radic Biol Med 2004; 37: 2064-2071.
    • (2004) Free Radic Biol Med , vol.37 , pp. 2064-2071
    • Grosser, N.1    Hemmerle, A.2    Berndt, G.3
  • 78
    • 33750532308 scopus 로고    scopus 로고
    • Regulation of inflammation and redox signaling by dietary polyphenols
    • Rahman I, Biswas SK, Kirkham PA. Regulation of inflammation and redox signaling by dietary polyphenols. Biochem Pharmacol 2006; 72: 1439-52.
    • (2006) Biochem Pharmacol , vol.72 , pp. 1439-1452
    • Rahman, I.1    Biswas, S.K.2    Kirkham, P.A.3
  • 79
    • 34250753928 scopus 로고    scopus 로고
    • Activation of endothelial nitric oxide synthase by dietary isoflavones: Role of NO in Nrf2-mediated antioxidant gene expression
    • Mann GE, Rowlands DJ, Li FY, de Winter P, Siow RC. Activation of endothelial nitric oxide synthase by dietary isoflavones: role of NO in Nrf2-mediated antioxidant gene expression. Cardiovasc Res 2007; 75: 261-74.
    • (2007) Cardiovasc Res , vol.75 , pp. 261-274
    • Mann, G.E.1    Rowlands, D.J.2    Li, F.Y.3    de Winter, P.4    Siow, R.C.5
  • 80
    • 34347392509 scopus 로고    scopus 로고
    • Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways
    • Yao P, Nussler A, Liu L, et al. Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways. J Hepatol 2007; 47: 253-61.
    • (2007) J Hepatol , vol.47 , pp. 253-261
    • Yao, P.1    Nussler, A.2    Liu, L.3
  • 81
    • 67049145006 scopus 로고    scopus 로고
    • The protective role of HO-1 and its generated products (CO, bilirubin, and Fe) in ethanol-induced human hepatocyte damage
    • Yao P, Hao L, Nussler N, et al. The protective role of HO-1 and its generated products (CO, bilirubin, and Fe) in ethanol-induced human hepatocyte damage. Am J Physiol Gastrointest Liver Physiol 2009; 296: G1318-23.
    • (2009) Am J Physiol Gastrointest Liver Physiol , vol.296
    • Yao, P.1    Hao, L.2    Nussler, N.3
  • 82
    • 0032528947 scopus 로고    scopus 로고
    • Transcriptional activation of the haem oxygenase-1 gene by cGMP via a cAMP response element/activator protein-1 element in primary cultures of rat hepatocytes
    • Immenschuh S, Hinke V, Ohlmann A, Gifhorn-Katz S, Katz N, Jungermann K, Kietzmann T. Transcriptional activation of the haem oxygenase-1 gene by cGMP via a cAMP response element/activator protein-1 element in primary cultures of rat hepatocytes. Biochem J 1998; 334: 141-6.
    • (1998) Biochem J , vol.334 , pp. 141-146
    • Immenschuh, S.1    Hinke, V.2    Ohlmann, A.3    Gifhorn-Katz, S.4    Katz, N.5    Jungermann, K.6    Kietzmann, T.7
  • 83
    • 0031956516 scopus 로고    scopus 로고
    • The rat heme oxygenase-1 gene is transcriptionally induced via the protein kinase A signaling pathway in rat hepatocyte cultures
    • Immenschuh S, Kietzmann T, Hinke V, Wiederhold M, Katz N, Muller-Eberhard U. The rat heme oxygenase-1 gene is transcriptionally induced via the protein kinase A signaling pathway in rat hepatocyte cultures. Mol Pharmacol 1998; 53: 483-91.
    • (1998) Mol Pharmacol , vol.53 , pp. 483-491
    • Immenschuh, S.1    Kietzmann, T.2    Hinke, V.3    Wiederhold, M.4    Katz, N.5    Muller-Eberhard, U.6
  • 84
    • 77950625277 scopus 로고    scopus 로고
    • The antiinflammatory effects of adiponectin are mediated via a heme oxygenase-1-dependent pathway in rat Kupffer cells
    • Mandal P, Park PH, McMullen MR, Pratt BT, Nagy LE. The antiinflammatory effects of adiponectin are mediated via a heme oxygenase-1-dependent pathway in rat Kupffer cells. Hepatology 2010; 51: 1420-9.
    • (2010) Hepatology , vol.51 , pp. 1420-1429
    • Mandal, P.1    Park, P.H.2    McMullen, M.R.3    Pratt, B.T.4    Nagy, L.E.5
  • 85
    • 0037386113 scopus 로고    scopus 로고
    • Kupffer-cell specific induction of heme oxygenase 1 (hsp32) by the atrial natriuretic peptide--role of cGMP
    • Kiemer AK, Gerwig T, Gerbes AL, Meissner H, Bilzer M, Vollmar AM. Kupffer-cell specific induction of heme oxygenase 1 (hsp32) by the atrial natriuretic peptide--role of cGMP. J Hepatol; 38: 490-8.
    • J Hepatol , vol.38 , pp. 490-498
    • Kiemer, A.K.1    Gerwig, T.2    Gerbes, A.L.3    Meissner, H.4    Bilzer, M.5    Vollmar, A.M.6
  • 86
    • 20444459893 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene activation by the NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride via a protein kinase B, p38-dependent signaling pathway in monocytes
    • Wijayanti N, Kietzmann T, Immenschuh S. Heme oxygenase-1 gene activation by the NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride via a protein kinase B, p38-dependent signaling pathway in monocytes. J Biol Chem 2005; 280: 21820-9.
    • (2005) J Biol Chem , vol.280 , pp. 21820-21829
    • Wijayanti, N.1    Kietzmann, T.2    Immenschuh, S.3
  • 87
    • 77950601100 scopus 로고    scopus 로고
    • Therapeutic RNA manipulation in liver disease
    • Kerr TA, Davidson NO. Therapeutic RNA manipulation in liver disease. Hepatology 2010; 51: 1055-61.
    • (2010) Hepatology , vol.51 , pp. 1055-1061
    • Kerr, T.A.1    Davidson, N.O.2
  • 88
    • 0033452790 scopus 로고    scopus 로고
    • Upregulation of heme oxygenase-1 protects genetically fat Zucker rat livers from ischemia/reperfusion injury
    • Amersi F, Buelow R, Kato H, et al. Upregulation of heme oxygenase-1 protects genetically fat Zucker rat livers from ischemia/reperfusion injury. J Clin Invest 1999; 104: 1631-9.
    • (1999) J Clin Invest , vol.104 , pp. 1631-1639
    • Amersi, F.1    Buelow, R.2    Kato, H.3
  • 89
    • 56149124383 scopus 로고    scopus 로고
    • Heme oxygenase-1 suppresses hepatitis C virus replication and increases resistance of hepatocytes to oxidant injury
    • Zhu Z, Wilson AT, Mathahs MM, et al. Heme oxygenase-1 suppresses hepatitis C virus replication and increases resistance of hepatocytes to oxidant injury. Hepatology 2008; 48: 1430-9.
    • (2008) Hepatology , vol.48 , pp. 1430-1439
    • Zhu, Z.1    Wilson, A.T.2    Mathahs, M.M.3
  • 90
    • 34848878881 scopus 로고    scopus 로고
    • Reciprocal effects of micro-RNA-122 on expression of heme oxygenase-1 and hepatitis C virus genes in human hepatocytes
    • Shan Y, Zheng J, Lambrecht RW, Bonkovsky HL. Reciprocal effects of micro-RNA-122 on expression of heme oxygenase-1 and hepatitis C virus genes in human hepatocytes. Gastroenterology 2007; 133: 1166-74.
    • (2007) Gastroenterology , vol.133 , pp. 1166-1174
    • Shan, Y.1    Zheng, J.2    Lambrecht, R.W.3    Bonkovsky, H.L.4
  • 91
    • 77951460055 scopus 로고    scopus 로고
    • MicroRNA-196 represses Bach1 protein and hepatitis C virus gene expression in human hepatoma cells expressing hepatitis C viral proteins
    • Hou W, Tian Q, Zheng J, Bonkovsky HL. MicroRNA-196 represses Bach1 protein and hepatitis C virus gene expression in human hepatoma cells expressing hepatitis C viral proteins. Hepatology 2010; 51: 1494-504.
    • (2010) Hepatology , vol.51 , pp. 1494-1504
    • Hou, W.1    Tian, Q.2    Zheng, J.3    Bonkovsky, H.L.4
  • 94
    • 0036828783 scopus 로고    scopus 로고
    • Course and outcome of hepatitis C
    • Hoofnagle JH. Course and outcome of hepatitis C. Hepatology 2002; 36: S21-9.
    • (2002) Hepatology , vol.36
    • Hoofnagle, J.H.1
  • 95
    • 70349567521 scopus 로고    scopus 로고
    • Alcoholic liver disease and hepatitis C: A frequently underestimated combination
    • Mueller S, Millonig G, Seitz HK. Alcoholic liver disease and hepatitis C: a frequently underestimated combination. World J Gastroenterol 2009; 15: 3462-71.
    • (2009) World J Gastroenterol , vol.15 , pp. 3462-3471
    • Mueller, S.1    Millonig, G.2    Seitz, H.K.3
  • 96
    • 34848825909 scopus 로고    scopus 로고
    • Antiviral activity and hepatoprotection by heme oxygenase-1 in hepatitis B virus infection
    • Protzer U, Seyfried S, Quasdorff M, et al. Antiviral activity and hepatoprotection by heme oxygenase-1 in hepatitis B virus infection. Gastroenterology 2007; 133: 1156-65.
    • (2007) Gastroenterology , vol.133 , pp. 1156-1165
    • Protzer, U.1    Seyfried, S.2    Quasdorff, M.3
  • 97
    • 21744438136 scopus 로고    scopus 로고
    • Hepatitis C virus-core and non structural proteins lead to different effects on cellular antioxidant defenses
    • Abdalla MY, Ahmad IM, Spitz DR, Schmidt WN, Britigan BE. Hepatitis C virus-core and non structural proteins lead to different effects on cellular antioxidant defenses. J Med Virol 2005; 76: 489-97.
    • (2005) J Med Virol , vol.76 , pp. 489-497
    • Abdalla, M.Y.1    Ahmad, I.M.2    Spitz, D.R.3    Schmidt, W.N.4    Britigan, B.E.5
  • 98
    • 4444238755 scopus 로고    scopus 로고
    • Down-regulation of heme oxygenase-1 by hepatitis C virus infection in vivo and by the in vitro expression of hepatitis C core protein
    • Abdalla MY, Britigan BE, Wen F, et al. Down-regulation of heme oxygenase-1 by hepatitis C virus infection in vivo and by the in vitro expression of hepatitis C core protein. J Infect Dis 2004; 190: 1109-18.
    • (2004) J Infect Dis , vol.190 , pp. 1109-1118
    • Abdalla, M.Y.1    Britigan, B.E.2    Wen, F.3
  • 99
    • 33744942680 scopus 로고    scopus 로고
    • HCV proteins increase expression of heme oxygenase-1 (HO-1) and decrease expression of Bach1 in human hepatoma cells
    • Ghaziani T, Shan Y, Lambrecht RW, et al. HCV proteins increase expression of heme oxygenase-1 (HO-1) and decrease expression of Bach1 in human hepatoma cells. J Hepatol 2006; 45: 5-12.
    • (2006) J Hepatol , vol.45 , pp. 5-12
    • Ghaziani, T.1    Shan, Y.2    Lambrecht, R.W.3
  • 100
    • 75449117083 scopus 로고    scopus 로고
    • The heme oxygenase 1 product biliverdin interferes with hepatitis C virus replication by increasing antiviral interferon response
    • Lehmann E, El-Tantawy WH, Ocker M, et al. The heme oxygenase 1 product biliverdin interferes with hepatitis C virus replication by increasing antiviral interferon response. Hepatology 2010; 51: 398-404.
    • (2010) Hepatology , vol.51 , pp. 398-404
    • Lehmann, E.1    El-Tantawy, W.H.2    Ocker, M.3
  • 102
    • 0032451389 scopus 로고    scopus 로고
    • Alcoholic liver disease: Proposed recommendationss for the American College of Gastroenterology
    • McCullough AJ, O'Connor JFB. Alcoholic liver disease: proposed recommendationss for the American College of Gastroenterology. Am J Gastroenterol 1998; 93: 2022-36.
    • (1998) Am J Gastroenterol , vol.93 , pp. 2022-2036
    • McCullough, A.J.1    O'Connor, J.F.B.2
  • 103
    • 0036288123 scopus 로고    scopus 로고
    • Is obesity an independent risk factor for hepatocellular carcinoma in cirrhosis?
    • Nair S, Mason A, Eason J, Loss G, Perrillo RP. Is obesity an independent risk factor for hepatocellular carcinoma in cirrhosis? Hepatology 2002; 36: 150-5.
    • (2002) Hepatology , vol.36 , pp. 150-155
    • Nair, S.1    Mason, A.2    Eason, J.3    Loss, G.4    Perrillo, R.P.5
  • 104
    • 0042034405 scopus 로고    scopus 로고
    • Ethanol toxicity and nutritional status
    • In: Kotsonis F, Mackey M, Eds., 2nd ed. London. New York: Taylor and Francis
    • Seitz HK, Suter P. Ethanol toxicity and nutritional status. In: Kotsonis F, Mackey M, Eds. Nutritional Toxicology. 2nd ed. London. New York: Taylor and Francis; 2002. pp. 122-54.
    • (2002) Nutritional Toxicology , pp. 122-154
    • Seitz, H.K.1    Suter, P.2
  • 105
    • 0032185432 scopus 로고    scopus 로고
    • Alcoholic liver injury involves activation of Kupffer cells by endotoxin
    • Thurman RG. II. Alcoholic liver injury involves activation of Kupffer cells by endotoxin. Am J Physiol 1998; 275: G605-11.
    • (1998) Am J Physiol , vol.275
    • Thurman II, R.G.1
  • 106
    • 0034676629 scopus 로고    scopus 로고
    • Cytokines in alcoholic and nonalcoholic steatohepatitis
    • Tilg H, Diehl AM. Cytokines in alcoholic and nonalcoholic steatohepatitis. N Engl J Med 2000; 343: 1467-76.
    • (2000) N Engl J Med , vol.343 , pp. 1467-1476
    • Tilg, H.1    Diehl, A.M.2
  • 107
    • 0035834684 scopus 로고    scopus 로고
    • Stabilization of tumor necrosis factor alpha mRNA by chronic ethanol: Role of A + U-rich elements and p38 mitogen-activated protein kinase signaling pathway
    • Kishore R, McMullen MR, Nagy LE. Stabilization of tumor necrosis factor alpha mRNA by chronic ethanol: role of A + U-rich elements and p38 mitogen-activated protein kinase signaling pathway. J Biol Chem 2001; 276: 41930-7.
    • (2001) J Biol Chem , vol.276 , pp. 41930-41937
    • Kishore, R.1    McMullen, M.R.2    Nagy, L.E.3
  • 108
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel T. Oxidant signals and oxidative stress. Curr Opin Cell Biol 2003; 15: 247-54.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 247-254
    • Finkel, T.1
  • 109
    • 0041302377 scopus 로고    scopus 로고
    • The fatderived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice
    • Xu A, Wang Y, Keshaw H, Xu LY, Lam KS, Cooper GJ. The fatderived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice. J Clin Invest 2003; 112: 91-100.
    • (2003) J Clin Invest , vol.112 , pp. 91-100
    • Xu, A.1    Wang, Y.2    Keshaw, H.3    Xu, L.Y.4    Lam, K.S.5    Cooper, G.J.6
  • 110
    • 24144496133 scopus 로고    scopus 로고
    • Role of adiponectin in the protective action of dietary saturated fat against alcoholic fatty liver in mice
    • You M, Considine RV, Leone TC, Kelly DP, Crabb DW. Role of adiponectin in the protective action of dietary saturated fat against alcoholic fatty liver in mice. Hepatology 2005; 42: 568-77.
    • (2005) Hepatology , vol.42 , pp. 568-577
    • You, M.1    Considine, R.V.2    Leone, T.C.3    Kelly, D.P.4    Crabb, D.W.5
  • 111
    • 33645804223 scopus 로고    scopus 로고
    • Adiponectin normalizes LPS-stimulated TNF-alpha production by rat Kupffer cells after chronic ethanol feeding
    • Thakur V, Pritchard MT, McMullen MR, Nagy LE. Adiponectin normalizes LPS-stimulated TNF-alpha production by rat Kupffer cells after chronic ethanol feeding. Am J Physiol Gastrointest Liver Physiol 2006; 290: G998-1007.
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.290 , pp. 998-1007
    • Thakur, V.1    Pritchard, M.T.2    McMullen, M.R.3    Nagy, L.E.4
  • 113
    • 21644472266 scopus 로고    scopus 로고
    • Increased lipopolysaccharide sensitivity in alcoholic fatty livers is independent of leptin deficiency and toll-like receptor 4 (TLR4) or TLR2 mRNA expression
    • Romics L, Jr., Mandrekar P, Kodys K, et al. Increased lipopolysaccharide sensitivity in alcoholic fatty livers is independent of leptin deficiency and toll-like receptor 4 (TLR4) or TLR2 mRNA expression. Alcohol Clin Exp Res 2005; 29: 1018-26.
    • (2005) Alcohol Clin Exp Res , vol.29 , pp. 1018-1026
    • Romics Jr., L.1    Mandrekar, P.2    Kodys, K.3
  • 114
    • 34447134884 scopus 로고    scopus 로고
    • Heme oxygenase-1 upregulated by Ginkgo biloba extract: Potential protection against ethanol-induced oxidative liver damage
    • Yao P, Li K, Song F, et al. Heme oxygenase-1 upregulated by Ginkgo biloba extract: potential protection against ethanol-induced oxidative liver damage. Food Chem Toxicol 2007; 45: 1333-42.
    • (2007) Food Chem Toxicol , vol.45 , pp. 1333-1342
    • Yao, P.1    Li, K.2    Song, F.3
  • 115
    • 77649189669 scopus 로고    scopus 로고
    • Curcumin alleviates ethanol-induced hepatocytes oxidative damage involving heme oxygenase-1 induction
    • Bao W, Li K, Rong S, et al. Curcumin alleviates ethanol-induced hepatocytes oxidative damage involving heme oxygenase-1 induction. J Ethnopharmacol 2010; 128: 549-53.
    • (2010) J Ethnopharmacol , vol.128 , pp. 549-553
    • Bao, W.1    Li, K.2    Rong, S.3
  • 116
    • 77950625277 scopus 로고    scopus 로고
    • The antiinflammatory effects of adiponectin are mediated via a heme oxygenase-1-dependent pathway in rat Kupffer cells
    • Mandal P, Park PH, McMullen MR, Pratt BT, Nagy LE. The antiinflammatory effects of adiponectin are mediated via a heme oxygenase-1-dependent pathway in rat Kupffer cells. Hepatology 2010; 51: 1420-9.
    • (2010) Hepatology , vol.51 , pp. 1420-1429
    • Mandal, P.1    Park, P.H.2    McMullen, M.R.3    Pratt, B.T.4    Nagy, L.E.5
  • 117
    • 0035083842 scopus 로고    scopus 로고
    • Nonalcoholic steatohepatitis: Definition and pathology
    • Brunt EM. Nonalcoholic steatohepatitis: definition and pathology. Semin Liver Dis 2001; 21: 3-16.
    • (2001) Semin Liver Dis , vol.21 , pp. 3-16
    • Brunt, E.M.1
  • 119
    • 0036829092 scopus 로고    scopus 로고
    • AGA technical review on nonalcoholic fatty liver disease
    • Sanyal AJ. AGA technical review on nonalcoholic fatty liver disease. Gastroenterology 2002; 123: 1705-25.
    • (2002) Gastroenterology , vol.123 , pp. 1705-1725
    • Sanyal, A.J.1
  • 121
    • 0023801758 scopus 로고
    • Alcohol-like liver disease in nonalcoholics. A clinical and histologic comparison with alcoholinduced liver injury
    • Diehl AM, Goodman Z, Ishak KG. Alcohol-like liver disease in nonalcoholics. A clinical and histologic comparison with alcoholinduced liver injury. Gastroenterology 1988; 95: 1056-62.
    • (1988) Gastroenterology , vol.95 , pp. 1056-1062
    • Diehl, A.M.1    Goodman, Z.2    Ishak, K.G.3
  • 122
    • 0037129380 scopus 로고    scopus 로고
    • Nonalcoholic fatty liver disease
    • Angulo P. Nonalcoholic fatty liver disease. N Engl J Med 2002; 346: 1221-31.
    • (2002) N Engl J Med , vol.346 , pp. 1221-1231
    • Angulo, P.1
  • 123
    • 0033231294 scopus 로고    scopus 로고
    • Association of nonalcoholic fatty liver disease with insulin resistance
    • Marchesini G, Brizi M, Morselli-Labate AM, et al. Association of nonalcoholic fatty liver disease with insulin resistance. Am J Med 1999; 107: 450-5.
    • (1999) Am J Med , vol.107 , pp. 450-455
    • Marchesini, G.1    Brizi, M.2    Morselli-Labate, A.M.3
  • 124
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha-and obesity-induced insulin resistance
    • Hotamisligil GS, Peraldi P, Budavari A, Ellis R, White MF, Spiegelman BM. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha-and obesity-induced insulin resistance. Science 1996; 271: 665-8.
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 125
    • 0036154816 scopus 로고    scopus 로고
    • NASH: From liver diseases to metabolic disorders and back to clinical hepatology
    • Marchesini G, Forlani G. NASH: from liver diseases to metabolic disorders and back to clinical hepatology. Hepatology 2002; 35: 497-9.
    • (2002) Hepatology , vol.35 , pp. 497-499
    • Marchesini, G.1    Forlani, G.2
  • 126
    • 0035084699 scopus 로고    scopus 로고
    • Nonalcoholic steatohepatitis: Association of insulin resistance and mitochondrial abnormalities
    • Sanyal AJ, Campbell-Sargent C, Mirshahi F, et al. Nonalcoholic steatohepatitis: association of insulin resistance and mitochondrial abnormalities. Gastroenterology 2001; 120: 1183-92.
    • (2001) Gastroenterology , vol.120 , pp. 1183-1192
    • Sanyal, A.J.1    Campbell-Sargent, C.2    Mirshahi, F.3
  • 127
    • 0344011135 scopus 로고    scopus 로고
    • Antioxidant paraoxonase 1 activity in the metabolic syndrome
    • Senti M, Tomas M, Fito M, et al. Antioxidant paraoxonase 1 activity in the metabolic syndrome. J Clin Endocrinol Metab 2003; 88: 5422-6.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 5422-5426
    • Senti, M.1    Tomas, M.2    Fito, M.3
  • 128
    • 14844288046 scopus 로고    scopus 로고
    • Heme oxygenase-1 levels and oxidative stress-related parameters in non-alcoholic fatty liver disease patients
    • Malaguarnera L, Madeddu R, Palio E, Arena N, Malaguarnera M. Heme oxygenase-1 levels and oxidative stress-related parameters in non-alcoholic fatty liver disease patients. J Hepatol 2005; 42: 585-91.
    • (2005) J Hepatol , vol.42 , pp. 585-591
    • Malaguarnera, L.1    Madeddu, R.2    Palio, E.3    Arena, N.4    Malaguarnera, M.5
  • 129
    • 69049107570 scopus 로고    scopus 로고
    • Effect of dietary fat to produce non-alcoholic fatty liver in the rat
    • Ahmed U, Redgrave TG, Oates PS. Effect of dietary fat to produce non-alcoholic fatty liver in the rat. J Gastroenterol Hepatol 2009; 24: 1463-71.
    • (2009) J Gastroenterol Hepatol , vol.24 , pp. 1463-1471
    • Ahmed, U.1    Redgrave, T.G.2    Oates, P.S.3
  • 130
    • 75149160667 scopus 로고    scopus 로고
    • Heme oxygenase-1 protects against steatohepatitis in both cultured hepatocytes and mice
    • Yu J, Chu ES, Wang R, et al. Heme oxygenase-1 protects against steatohepatitis in both cultured hepatocytes and mice. Gastroenterology 2010; 138: 694-704.
    • (2010) Gastroenterology , vol.138 , pp. 694-704
    • Yu, J.1    Chu, E.S.2    Wang, R.3
  • 131
    • 72649103895 scopus 로고    scopus 로고
    • Loss of Nrf2 markedly exacerbates nonalcoholic steatohepatitis
    • Chowdhry S, Nazmy MH, Meakin PJ, et al. Loss of Nrf2 markedly exacerbates nonalcoholic steatohepatitis. Free Radic Biol Med 2010; 48: 357-71.
    • (2010) Free Radic Biol Med , vol.48 , pp. 357-371
    • Chowdhry, S.1    Nazmy, M.H.2    Meakin, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.