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Volumn 133, Issue 2, 2008, Pages 167-177

HBx modulates iron regulatory protein 1-mediated iron metabolism via reactive oxygen species

Author keywords

HBx; Iron; IRP1; LIP; ROS; Total iron level

Indexed keywords

ACETYLCYSTEINE; CD71 ANTIGEN; FERRITIN; HEPATITIS B VIRUS X PROTEIN; IRON REGULATORY PROTEIN 1; REACTIVE OXYGEN METABOLITE;

EID: 41049111566     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2007.12.014     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 0042968962 scopus 로고    scopus 로고
    • Molecular viral oncology of hepatocellular carcinoma
    • Block T.M., Mehta A.S., Fimmel C.J., and Jordan R. Molecular viral oncology of hepatocellular carcinoma. Oncogene 22 33 (2003) 5093-5107
    • (2003) Oncogene , vol.22 , Issue.33 , pp. 5093-5107
    • Block, T.M.1    Mehta, A.S.2    Fimmel, C.J.3    Jordan, R.4
  • 2
    • 0029815291 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective stratagem against oxidative injury
    • Cairo G., Castrusini E., Minotti G., and Bernelli-Zazzera A. Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective stratagem against oxidative injury. FASEB J. 10 11 (1996) 1326-1335
    • (1996) FASEB J. , vol.10 , Issue.11 , pp. 1326-1335
    • Cairo, G.1    Castrusini, E.2    Minotti, G.3    Bernelli-Zazzera, A.4
  • 3
    • 0029128256 scopus 로고
    • Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation
    • Cairo G., and Pietrangelo A. Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation. Eur. J. Biochem. 232 2 (1995) 358-363
    • (1995) Eur. J. Biochem. , vol.232 , Issue.2 , pp. 358-363
    • Cairo, G.1    Pietrangelo, A.2
  • 4
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • Cairo G., and Pietrangelo A. Iron regulatory proteins in pathobiology. Biochem. J. 352 Pt 2 (2000) 241-250
    • (2000) Biochem. J. , vol.352 , Issue.PART 2 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 5
    • 0035138016 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus production associated with high levels of intracellular viral DNA intermediates in iron-depleted HepG2.2. 15 cells
    • Chouteau P., Le Seyec J., Saulier-Le Drean B., Cannie I., Brissot P., Lescoat G., Guguen-Guillouzo C., and Gripon P. Inhibition of hepatitis B virus production associated with high levels of intracellular viral DNA intermediates in iron-depleted HepG2.2. 15 cells. J. Hepatol. 34 1 (2001) 108-113
    • (2001) J. Hepatol. , vol.34 , Issue.1 , pp. 108-113
    • Chouteau, P.1    Le Seyec, J.2    Saulier-Le Drean, B.3    Cannie, I.4    Brissot, P.5    Lescoat, G.6    Guguen-Guillouzo, C.7    Gripon, P.8
  • 6
    • 0033566305 scopus 로고    scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents III: the effect of the ligands on molecular targets involved in proliferation
    • Darnell G., and Richardson D.R. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents III: the effect of the ligands on molecular targets involved in proliferation. Blood 94 2 (1999) 781-792
    • (1999) Blood , vol.94 , Issue.2 , pp. 781-792
    • Darnell, G.1    Richardson, D.R.2
  • 7
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein R.S. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu. Rev. Nutr. 20 (2000) 627-662
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 8
    • 0033571363 scopus 로고    scopus 로고
    • H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties
    • Epsztejn S., Glickstein H., Picard V., Slotki I.N., Breuer W., Beaumont C., and Cabantchik Z.I. H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties. Blood 94 10 (1999) 3593-3603
    • (1999) Blood , vol.94 , Issue.10 , pp. 3593-3603
    • Epsztejn, S.1    Glickstein, H.2    Picard, V.3    Slotki, I.N.4    Breuer, W.5    Beaumont, C.6    Cabantchik, Z.I.7
  • 10
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs
    • Gardner P.R., Nguyen D.D., and White C.W. Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc. Natl. Acad. Sci. U.S.A. 91 25 (1994) 12248-12252
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , Issue.25 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.D.2    White, C.W.3
  • 11
    • 0033525713 scopus 로고    scopus 로고
    • Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress
    • Gehring N.H., Hentze M.W., and Pantopoulos K. Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress. J. Biol. Chem. 274 10 (1999) 6219-6225
    • (1999) J. Biol. Chem. , vol.274 , Issue.10 , pp. 6219-6225
    • Gehring, N.H.1    Hentze, M.W.2    Pantopoulos, K.3
  • 12
    • 0024599359 scopus 로고
    • Increased serum ferritin in chronic liver disease: a risk factor for primary hepatocellular carcinoma
    • Hann H.W., Kim C.Y., London W.T., and Blumberg B.S. Increased serum ferritin in chronic liver disease: a risk factor for primary hepatocellular carcinoma. Int. J. Cancer 43 3 (1989) 376-379
    • (1989) Int. J. Cancer , vol.43 , Issue.3 , pp. 376-379
    • Hann, H.W.1    Kim, C.Y.2    London, W.T.3    Blumberg, B.S.4
  • 13
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: molecular control of mammalian iron metabolism
    • Hentze M.W., Muckenthaler M.U., and Andrews N.C. Balancing acts: molecular control of mammalian iron metabolism. Cell 117 3 (2004) 285-297
    • (2004) Cell , vol.117 , Issue.3 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 14
    • 0345708218 scopus 로고    scopus 로고
    • Iron overload and its association with cancer risk in humans: evidence for iron as a carcinogenic metal
    • Huang X. Iron overload and its association with cancer risk in humans: evidence for iron as a carcinogenic metal. Mutat. Res. 533 1-2 (2003) 153-171
    • (2003) Mutat. Res. , vol.533 , Issue.1-2 , pp. 153-171
    • Huang, X.1
  • 15
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: characterization, measurement, and participation in cellular processes(1)
    • Kakhlon O., and Cabantchik Z.I. The labile iron pool: characterization, measurement, and participation in cellular processes(1). Free Radic. Biol. Med. 33 8 (2002) 1037-1046
    • (2002) Free Radic. Biol. Med. , vol.33 , Issue.8 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 17
    • 7044222320 scopus 로고    scopus 로고
    • Iron, hemochromatosis, and hepatocellular carcinoma
    • Kowdley K.V. Iron, hemochromatosis, and hepatocellular carcinoma. Gastroenterology 127 5 Suppl. 1 (2004) S79-S86
    • (2004) Gastroenterology , vol.127 , Issue.5 SUPPL. 1
    • Kowdley, K.V.1
  • 18
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • LeBel C.P., Ischiropoulos H., and Bondy S.C. Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress. Chem. Res. Toxicol. 5 2 (1992) 227-231
    • (1992) Chem. Res. Toxicol. , vol.5 , Issue.2 , pp. 227-231
    • LeBel, C.P.1    Ischiropoulos, H.2    Bondy, S.C.3
  • 19
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs
    • Leibold E.A., and Munro H.N. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs. Proc. Natl. Acad. Sci. U.S.A. 85 7 (1988) 2171-2175
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , Issue.7 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 21
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins E.A., Robalinho R.L., and Meneghini R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch. Biochem. Biophys. 316 1 (1995) 128-134
    • (1995) Arch. Biochem. Biophys. , vol.316 , Issue.1 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 24
    • 28644443925 scopus 로고    scopus 로고
    • Iron regulatory protein 1 as a sensor of reactive oxygen species
    • Mueller S. Iron regulatory protein 1 as a sensor of reactive oxygen species. Biofactors 24 1-4 (2005) 171-181
    • (2005) Biofactors , vol.24 , Issue.1-4 , pp. 171-181
    • Mueller, S.1
  • 25
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Mullner E.W., Neupert B., and Kuhn L.C. A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58 2 (1989) 373-382
    • (1989) Cell , vol.58 , Issue.2 , pp. 373-382
    • Mullner, E.W.1    Neupert, B.2    Kuhn, L.C.3
  • 26
    • 17144445166 scopus 로고    scopus 로고
    • Myeloperoxidase-derived hypochlorous acid antagonizes the oxidative stress-mediated activation of iron regulatory protein 1
    • Mutze S., Hebling U., Stremmel W., Wang J., Arnhold J., Pantopoulos K., and Mueller S. Myeloperoxidase-derived hypochlorous acid antagonizes the oxidative stress-mediated activation of iron regulatory protein 1. J. Biol. Chem. 278 42 (2003) 40542-40549
    • (2003) J. Biol. Chem. , vol.278 , Issue.42 , pp. 40542-40549
    • Mutze, S.1    Hebling, U.2    Stremmel, W.3    Wang, J.4    Arnhold, J.5    Pantopoulos, K.6    Mueller, S.7
  • 28
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos K., and Hentze M.W. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J. 14 12 (1995) 2917-2924
    • (1995) EMBO J. , vol.14 , Issue.12 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 29
    • 0030600134 scopus 로고    scopus 로고
    • Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1
    • Paraskeva E., and Hentze M.W. Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1. FEBS Lett. 389 1 (1996) 40-43
    • (1996) FEBS Lett. , vol.389 , Issue.1 , pp. 40-43
    • Paraskeva, E.1    Hentze, M.W.2
  • 30
    • 0033535941 scopus 로고    scopus 로고
    • Ultraviolet A radiation induces immediate release of iron in human primary skin fibroblasts: the role of ferritin
    • Pourzand C., Watkin R.D., Brown J.E., and Tyrrell R.M. Ultraviolet A radiation induces immediate release of iron in human primary skin fibroblasts: the role of ferritin. Proc. Natl. Acad. Sci. U.S.A. 96 12 (1999) 6751-6756
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.12 , pp. 6751-6756
    • Pourzand, C.1    Watkin, R.D.2    Brown, J.E.3    Tyrrell, R.M.4
  • 31
    • 3242657100 scopus 로고    scopus 로고
    • Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells
    • Riemer J., Hoepken H.H., Czerwinska H., Robinson S.R., and Dringen R. Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells. Anal. Biochem. 331 2 (2004) 370-375
    • (2004) Anal. Biochem. , vol.331 , Issue.2 , pp. 370-375
    • Riemer, J.1    Hoepken, H.H.2    Czerwinska, H.3    Robinson, S.R.4    Dringen, R.5
  • 32
    • 33746968581 scopus 로고    scopus 로고
    • Induction of H-ferritin synthesis by oxalomalate is regulated at both the transcriptional and post-transcriptional levels
    • Santamaria R., Bevilacqua M.A., Maffettone C., Irace C., Iovine B., and Colonna A. Induction of H-ferritin synthesis by oxalomalate is regulated at both the transcriptional and post-transcriptional levels. Biochim. Biophys. Acta 1763 8 (2006) 815-822
    • (2006) Biochim. Biophys. Acta , vol.1763 , Issue.8 , pp. 815-822
    • Santamaria, R.1    Bevilacqua, M.A.2    Maffettone, C.3    Irace, C.4    Iovine, B.5    Colonna, A.6
  • 33
    • 0038158319 scopus 로고    scopus 로고
    • Hepatitis B virus X protein induces cell death by causing loss of mitochondrial membrane potential
    • Shirakata Y., and Koike K. Hepatitis B virus X protein induces cell death by causing loss of mitochondrial membrane potential. J. Biol. Chem. 278 24 (2003) 22071-22078
    • (2003) J. Biol. Chem. , vol.278 , Issue.24 , pp. 22071-22078
    • Shirakata, Y.1    Koike, K.2
  • 34
    • 14244254585 scopus 로고    scopus 로고
    • Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism
    • Starzynski R.R., Lipinski P., Drapier J.C., Diet A., Smuda E., Bartlomiejczyk T., Gralak M.A., and Kruszewski M. Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism. J. Biol. Chem. 280 6 (2005) 4207-4212
    • (2005) J. Biol. Chem. , vol.280 , Issue.6 , pp. 4207-4212
    • Starzynski, R.R.1    Lipinski, P.2    Drapier, J.C.3    Diet, A.4    Smuda, E.5    Bartlomiejczyk, T.6    Gralak, M.A.7    Kruszewski, M.8
  • 36
    • 0033548251 scopus 로고    scopus 로고
    • Hypoxia alters iron-regulatory protein-1 binding capacity and modulates cellular iron homeostasis in human hepatoma and erythroleukemia cells
    • Toth I., Yuan L., Rogers J.T., Boyce H., and Bridges K.R. Hypoxia alters iron-regulatory protein-1 binding capacity and modulates cellular iron homeostasis in human hepatoma and erythroleukemia cells. J. Biol. Chem. 274 7 (1999) 4467-4473
    • (1999) J. Biol. Chem. , vol.274 , Issue.7 , pp. 4467-4473
    • Toth, I.1    Yuan, L.2    Rogers, J.T.3    Boyce, H.4    Bridges, K.R.5
  • 37
    • 0036381371 scopus 로고    scopus 로고
    • Iron and carcinogenesis: from Fenton reaction to target genes
    • Toyokuni S. Iron and carcinogenesis: from Fenton reaction to target genes. Redox Rep. 7 4 (2002) 189-197
    • (2002) Redox Rep. , vol.7 , Issue.4 , pp. 189-197
    • Toyokuni, S.1
  • 38
    • 0034774463 scopus 로고    scopus 로고
    • Mitochondrially associated hepatitis B virus X protein constitutively activates transcription factors STAT-3 and NF-kappa B via oxidative stress
    • Waris G., Huh K.W., and Siddiqui A. Mitochondrially associated hepatitis B virus X protein constitutively activates transcription factors STAT-3 and NF-kappa B via oxidative stress. Mol. Cell Biol. 21 22 (2001) 7721-7730
    • (2001) Mol. Cell Biol. , vol.21 , Issue.22 , pp. 7721-7730
    • Waris, G.1    Huh, K.W.2    Siddiqui, A.3
  • 39
    • 22544439946 scopus 로고    scopus 로고
    • Distinct roles of basal steady-state and induced H-ferritin in tumor necrosis factor-induced death in L929 cells
    • Xie C., Zhang N., Zhou H., Li J., Li Q., Zarubin T., Lin S.C., and Han J. Distinct roles of basal steady-state and induced H-ferritin in tumor necrosis factor-induced death in L929 cells. Mol. Cell Biol. 25 15 (2005) 6673-6681
    • (2005) Mol. Cell Biol. , vol.25 , Issue.15 , pp. 6673-6681
    • Xie, C.1    Zhang, N.2    Zhou, H.3    Li, J.4    Li, Q.5    Zarubin, T.6    Lin, S.C.7    Han, J.8
  • 41
    • 0036128705 scopus 로고    scopus 로고
    • The labile iron pool of hepatocytes in chronic and acute iron overload and chelator-induced iron deprivation
    • Zanninelli G., Loreal O., Brissot P., Konijn A.M., Slotki I.N., Hider R.C., and Ioav Cabantchik Z. The labile iron pool of hepatocytes in chronic and acute iron overload and chelator-induced iron deprivation. J. Hepatol. 36 1 (2002) 39-46
    • (2002) J. Hepatol. , vol.36 , Issue.1 , pp. 39-46
    • Zanninelli, G.1    Loreal, O.2    Brissot, P.3    Konijn, A.M.4    Slotki, I.N.5    Hider, R.C.6    Ioav Cabantchik, Z.7


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