메뉴 건너뛰기




Volumn 287, Issue 32, 2012, Pages 26630-26646

Correction: Impact of intravascular hemolysis in malaria on liver dysfunction: Involvement of hepatic free heme overload, NF-κB activation, and neutrophil infiltration (Journal of Biological Chemistry (2012) 287 (26630–26646) DOI: 10.1074/jbc.M112.341255);Impact of intravascular hemolysis in malaria on liver dysfunction: Involvement of hepatic free heme overload, NF-κB activation, and neutrophil infiltration

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BLOOD; CELL ADHESION; CELL DEATH; CHEMICAL ACTIVATION; DISEASES; ELECTROPHORETIC MOBILITY; IRON; MAMMALS; MOLECULES; OXIDANTS;

EID: 84864543003     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.AAC119.012033     Document Type: Erratum
Times cited : (70)

References (92)
  • 2
    • 76449093221 scopus 로고    scopus 로고
    • Pleiotropic effects of intravascular hemolysis on vascular homeostasis
    • Kato, G. J., and Taylor, J. G., 6th (2010) Pleiotropic effects of intravascular hemolysis on vascular homeostasis. Br. J. Haematol. 148, 690-701
    • (2010) Br. J. Haematol. , vol.148 , pp. 690-701
    • Kato, G.J.1    Taylor VI, J.G.2
  • 3
    • 67649703927 scopus 로고    scopus 로고
    • Erythrocyte hemolysis and hemoglobin oxidation promote ferric chloride-induced vascular injury
    • Woollard, K. J., Sturgeon, S., Chin-Dusting, J. P., Salem, H. H., and Jackson, S. P. (2009) Erythrocyte hemolysis and hemoglobin oxidation promote ferric chloride-induced vascular injury. J. Biol. Chem. 284, 13110-13118
    • (2009) J. Biol. Chem. , vol.284 , pp. 13110-13118
    • Woollard, K.J.1    Sturgeon, S.2    Chin-Dusting, J.P.3    Salem, H.H.4    Jackson, S.P.5
  • 6
    • 68849122521 scopus 로고    scopus 로고
    • Haptoglobin halts hemoglobin's havoc
    • Kato, G. J. (2009) Haptoglobin halts hemoglobin's havoc. J. Clin. Invest. 119, 2140-2142
    • (2009) J. Clin. Invest. , vol.119 , pp. 2140-2142
    • Kato, G.J.1
  • 7
    • 0036893587 scopus 로고    scopus 로고
    • Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis
    • DOI 10.1182/blood-2002-04-1270
    • Tolosano, E., Fagoonee, S., Hirsch, E., Berger, F. G., Baumann, H., Silengo, L., and Altruda, F. (2002) Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis. Blood 100, 4201-4208 (Pubitemid 35402055)
    • (2002) Blood , vol.100 , Issue.12 , pp. 4201-4208
    • Tolosano, E.1    Fagoonee, S.2    Hirsch, E.3    Berger, F.G.4    Baumann, H.5    Silengo, L.6    Altruda, F.7
  • 8
    • 0019877615 scopus 로고
    • Hemopexin-mediated transport of heme into isolated rat hepatocytes
    • Smith, A., and Morgan, W. T. (1981) Hemopexin-mediated transport of heme into isolated rat hepatocytes. J. Biol. Chem. 256, 10902-10909
    • (1981) J. Biol. Chem. , vol.256 , pp. 10902-10909
    • Smith, A.1    Morgan, W.T.2
  • 9
    • 0021127103 scopus 로고
    • Hemopexin-mediated heme uptake by liver. Characterization of the interaction of heme-hemopexin with isolated rabbit liver plasma membranes
    • Smith, A., and Morgan, W. T. (1984) Hemopexin-mediated heme uptake by liver. Characterization of the interaction of heme-hemopexin with isolated rabbit liver plasma membranes. J. Biol. Chem. 259, 12049-12053 (Pubitemid 14022137)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.19 , pp. 12049-12053
    • Smith, A.1    Morgan, W.T.2
  • 10
    • 79957795889 scopus 로고    scopus 로고
    • Synthesis of novel heme-interacting acridone derivatives to prevent free heme-mediated protein oxidation and degradation
    • Pal, C., Kundu, M. K., Bandyopadhyay, U., and Adhikari, S. (2011) Synthesis of novel heme-interacting acridone derivatives to prevent free heme-mediated protein oxidation and degradation. Bioorg. Med. Chem. Lett. 21, 3563-3567
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 3563-3567
    • Pal, C.1    Kundu, M.K.2    Bandyopadhyay, U.3    Adhikari, S.4
  • 12
    • 77949513218 scopus 로고    scopus 로고
    • Toxicological consequences of extracellular hemoglobin. Biochemical and physiological perspectives
    • Buehler, P. W., and D'Agnillo, F. (2010) Toxicological consequences of extracellular hemoglobin. Biochemical and physiological perspectives. Antioxid. Redox Signal. 12, 275-291
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 275-291
    • Buehler, P.W.1    D'Agnillo, F.2
  • 13
    • 7244243910 scopus 로고    scopus 로고
    • The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology
    • DOI 10.1089/ars.2004.6.954
    • Reeder, B. J., Svistunenko, D. A., Cooper, C. E., and Wilson, M. T. (2004) The radical and redox chemistry of myoglobin and hemoglobin. From in vitro studies to human pathology. Antioxid. Redox Signal. 6, 954-966 (Pubitemid 39434932)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.6 , pp. 954-966
    • Reeder, B.J.1    Svistunenko, D.A.2    Cooper, C.E.3    Wilson, M.T.4
  • 15
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • DOI 10.1016/j.toxlet.2005.03.004, PII S0378427405000883
    • Kumar, S., and Bandyopadhyay, U. (2005) Free heme toxicity and its detoxification systems in human. Toxicol. Lett. 157, 175-188 (Pubitemid 40726102)
    • (2005) Toxicology Letters , vol.157 , Issue.3 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 16
    • 15944398355 scopus 로고    scopus 로고
    • The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: A novel mechanism of human disease
    • DOI 10.1001/jama.293.13.1653
    • Rother, R. P., Bell, L., Hillmen, P., and Gladwin, M. T. (2005) The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin. A novel mechanism of human disease. JAMA 293, 1653-1662 (Pubitemid 40471796)
    • (2005) Journal of the American Medical Association , vol.293 , Issue.13 , pp. 1653-1662
    • Rother, R.P.1    Bell, L.2    Hillmen, P.3    Gladwin, M.T.4
  • 17
    • 0036682472 scopus 로고    scopus 로고
    • Pro-oxidant and cytotoxic effects of circulating heme
    • DOI 10.1182/blood.V100.3.879
    • Jeney, V., Balla, J., Yachie, A., Varga, Z., Vercellotti, G. M., Eaton, J. W., and Balla, G. (2002) Pro-oxidant and cytotoxic effects of circulating heme. Blood 100, 879-887 (Pubitemid 34832613)
    • (2002) Blood , vol.100 , Issue.3 , pp. 879-887
    • Jeney, V.1    Balla, J.2    Yachie, A.3    Varga, Z.4    Vercellotti, G.M.5    Eaton, J.W.6    Balla, G.7
  • 18
    • 7244240720 scopus 로고    scopus 로고
    • Heme degradation by reactive oxygen species
    • DOI 10.1089/ars.2004.6.967
    • Nagababu, E., and Rifkind, J. M. (2004) Heme degradation by reactive oxygen species. Antioxid. Redox Signal. 6, 967-978 (Pubitemid 39434933)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.6 , pp. 967-978
    • Nagababu, E.1    Rifkind, J.M.2
  • 19
  • 20
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivityHeme oxygenase has both pro- and antioxidant properties
    • DOI 10.1016/S0891-5849(99)00223-3, PII S0891584999002233
    • Ryter, S. W., and Tyrrell, R. M. (2000) The heme synthesis and degradation pathways. Role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties. Free Radic. Biol. Med. 28, 289-309 (Pubitemid 30084022)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.2 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 21
    • 35848957274 scopus 로고    scopus 로고
    • Heme, heme oxygenase, and ferritin: How the vascular endothelium survives (and dies) in an iron-rich environment
    • DOI 10.1089/ars.2007.1787
    • Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Jacob, H. S., Eaton, J. W., and Balla, G. (2007) Heme, heme oxygenase, and ferritin. How the vascular endothelium survives (and dies) in an iron-rich environment. Antioxid. Redox Signal. 9, 2119-2137 (Pubitemid 350059014)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.12 , pp. 2119-2137
    • Balla, J.1    Vercellotti, G.M.2    Jeney, V.3    Yachie, A.4    Varga, Z.5    Jacob, H.S.6    Eaton, J.W.7    Balla, G.8
  • 22
    • 67650698991 scopus 로고    scopus 로고
    • Eradicating malaria
    • Breman, J. G. (2009) Eradicating malaria. Sci. Prog. 92, 1-38
    • (2009) Sci. Prog. , vol.92 , pp. 1-38
    • Breman, J.G.1
  • 26
    • 23644452120 scopus 로고    scopus 로고
    • Plasmodium parasite proteins and the infected erythrocyte
    • DOI 10.1016/j.pt.2005.07.003, PII S147149220500190X
    • Haldar, K., Hiller, N. L., van Ooij, C., and Bhattacharjee, S. (2005) Plasmodium parasite proteins and the infected erythrocyte. Trends Parasitol. 21, 402-403 (Pubitemid 41116713)
    • (2005) Trends in Parasitology , vol.21 , Issue.9 , pp. 402-403
    • Haldar, K.1    Hiller, N.L.2    Van Ooij, C.3    Bhattacharjee, S.4
  • 27
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparium
    • DOI 10.1146/annurev.micro.51.1.97
    • Francis, S. E., Sullivan, D. J., Jr., and Goldberg, D. E. (1997) Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu. Rev. Microbiol. 51, 97-123 (Pubitemid 27433044)
    • (1997) Annual Review of Microbiology , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan Jr., D.J.2    Goldberg, D.E.3
  • 28
    • 84858767754 scopus 로고    scopus 로고
    • (Becker, K., ed) Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany
    • Bandyopadhyay, U., and Dey, S. (2011) in Apicomplexan Parasites (Becker, K., ed) pp. 205-234, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany
    • (2011) Apicomplexan Parasites , pp. 205-234
    • Bandyopadhyay, U.1    Dey, S.2
  • 31
    • 33947356275 scopus 로고    scopus 로고
    • Malaria: Mechanisms of erythrocytic infection and pathological correlates of severe disease
    • DOI 10.1146/annurev.pathol.2.010506.091913, Annual Review of Pathology: Mechanisms of Disease
    • Haldar, K., Murphy, S. C., Milner, D. A., and Taylor, T. E. (2007) Malaria. Mechanisms of erythrocytic infection and pathological correlates of severe disease. Annu. Rev. Pathol. 2, 217-249 (Pubitemid 46448065)
    • (2007) Annual Review of Pathology , vol.2 , pp. 217-249
    • Haldar, K.1    Murphy, S.C.2    Milner Jr., D.A.3    Taylor, T.E.4
  • 32
    • 0029783192 scopus 로고    scopus 로고
    • Oxidative stress in malaria; implications for prevention and therapy
    • Postma, N. S., Mommers, E. C., Eling, W. M., and Zuidema, J. (1996) Oxidative stress in malaria; implications for prevention and therapy. Pharm. World Sci. 18, 121-129 (Pubitemid 26270457)
    • (1996) Pharmacy World and Science , vol.18 , Issue.4 , pp. 121-129
    • Postma, N.S.1    Mommers, E.C.2    Eling, W.M.C.3    Zuidema, J.4
  • 33
    • 0019842424 scopus 로고
    • Hemin lyses malaria parasites
    • Orjih, A. U., Banyal, H. S., Chevli, R., and Fitch, C. D. (1981) Hemin lyses malaria parasites. Science 214, 667-669 (Pubitemid 12208587)
    • (1981) Science , vol.214 , Issue.4521 , pp. 667-669
    • Orjih, A.U.1    Banyal, H.S.2    Chevli, R.3    Fitch, C.D.4
  • 34
    • 34548226931 scopus 로고    scopus 로고
    • Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors
    • DOI 10.1074/jbc.M703570200
    • Porto, B. N., Alves, L. S., Fernández, P. L., Dutra, T. P., Figueiredo, R. T., Graça-Souza, A. V., and Bozza, M. T. (2007) Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors. J. Biol. Chem. 282, 24430-24436 (Pubitemid 47328067)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.33 , pp. 24430-24436
    • Porto, B.N.1    Alves, L.S.2    Fernandez, P.L.3    Dutra, T.P.4    Figueiredo, R.T.5    Graca-Souza, A.V.6    Bozza, M.T.7
  • 35
    • 33845651700 scopus 로고    scopus 로고
    • Apoptosis in liver during malaria. Role of oxidative stress and implication of mitochondrial pathway
    • Guha, M., Kumar, S., Choubey, V., Maity, P., and Bandyopadhyay, U. (2006) Apoptosis in liver during malaria. Role of oxidative stress and implication of mitochondrial pathway. FASEB J. 20, 1224-1226
    • (2006) FASEB J. , vol.20 , pp. 1224-1226
    • Guha, M.1    Kumar, S.2    Choubey, V.3    Maity, P.4    Bandyopadhyay, U.5
  • 36
    • 58049208254 scopus 로고    scopus 로고
    • Malarial infection develops mitochondrial pathology and mitochondrial oxidative stress to promote hepatocyte apoptosis
    • Dey, S., Guha, M., Alam, A., Goyal, M., Bindu, S., Pal, C., Maity, P., Mitra, K., and Bandyopadhyay, U. (2009) Malarial infection develops mitochondrial pathology and mitochondrial oxidative stress to promote hepatocyte apoptosis. Free Radic. Biol. Med. 46, 271-281
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 271-281
    • Dey, S.1    Guha, M.2    Alam, A.3    Goyal, M.4    Bindu, S.5    Pal, C.6    Maity, P.7    Mitra, K.8    Bandyopadhyay, U.9
  • 37
    • 39149106003 scopus 로고    scopus 로고
    • Curcumin attenuates dimethylnitrosamine-induced liver injury in rats through Nrf2-mediated induction of heme oxygenase-1
    • DOI 10.1016/j.fct.2007.09.095, PII S0278691507004292
    • Farombi, E. O., Shrotriya, S., Na, H. K., Kim, S. H., and Surh, Y. J. (2008) Curcumin attenuates dimethylnitrosamine-induced liver injury in rats through Nrf2-mediated induction of heme oxygenase-1. Food Chem. Toxicol. 46, 1279-1287 (Pubitemid 351258204)
    • (2008) Food and Chemical Toxicology , vol.46 , Issue.4 , pp. 1279-1287
    • Farombi, E.O.1    Shrotriya, S.2    Na, H.-K.3    Kim, S.-H.4    Surh, Y.-J.5
  • 38
    • 80655125027 scopus 로고    scopus 로고
    • Translocation of heme oxygenase-1 to mitochondria is a novel cytoprotective mechanism against nonsteroidal anti-inflammatory drug-induced mitochondrial oxidative stress, apoptosis and gastric mucosal injury
    • Bindu, S., Pal, C., Dey, S., Goyal, M., Alam, A., Iqbal, M. S., Dutta, S., Sarkar, S., Kumar, R., Maity, P., and Bandyopadhyay, U. (2011) Translocation of heme oxygenase-1 to mitochondria is a novel cytoprotective mechanism against nonsteroidal anti-inflammatory drug-induced mitochondrial oxidative stress, apoptosis and gastric mucosal injury. J. Biol. Chem. 286, 39387-39402
    • (2011) J. Biol. Chem. , vol.286 , pp. 39387-39402
    • Bindu, S.1    Pal, C.2    Dey, S.3    Goyal, M.4    Alam, A.5    Iqbal, M.S.6    Dutta, S.7    Sarkar, S.8    Kumar, R.9    Maity, P.10    Bandyopadhyay, U.11
  • 39
    • 39149117334 scopus 로고    scopus 로고
    • Improved isolation of murine hepatocytes for in vitro malaria liver stage studies
    • Gonçalves, L. A., Vigário, A. M., and Penha- Gonçalves, C. (2007) Improved isolation of murine hepatocytes for in vitro malaria liver stage studies. Malar. J. 6, 169
    • (2007) Malar. J. , vol.6 , pp. 169
    • Gonçalves, L.A.1    Vigário, A.M.2    Penha-Gonçalves, C.3
  • 41
    • 0031031148 scopus 로고    scopus 로고
    • Nitric oxide protects cultured rat hepatocytes from tumor necrosis factor-α-induced apoptosis by inducing heat shock protein 70 expression
    • DOI 10.1074/jbc.272.2.1402
    • Kim, Y. M., de Vera, M. E., Watkins, S. C., and Billiar, T. R. (1997) Nitric oxide protects cultured rat hepatocytes from tumor necrosis factor-α-induced apoptosis by inducing heat shock protein 70 expression. J. Biol. Chem. 272, 1402-1411 (Pubitemid 27034647)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 1402-1411
    • Kim, Y.-M.1    De Vera, M.E.2    Watkins, S.C.3    Billiar, T.R.4
  • 43
    • 59149086582 scopus 로고    scopus 로고
    • Indomethacin, a nonsteroidal anti-inflammatory drug, develops gastropathy by inducing reactive oxygen species-mediated mitochondrial pathology and associated apoptosis in gastric mucosa. Anovel role of mitochondrial aconitase oxidation
    • Maity, P., Bindu, S., Dey, S., Goyal, M., Alam, A., Pal, C., Mitra, K., and Bandyopadhyay, U. (2009) Indomethacin, a nonsteroidal anti-inflammatory drug, develops gastropathy by inducing reactive oxygen species-mediated mitochondrial pathology and associated apoptosis in gastric mucosa. Anovel role of mitochondrial aconitase oxidation. J. Biol. Chem. 284, 3058-3068
    • (2009) J. Biol. Chem. , vol.284 , pp. 3058-3068
    • Maity, P.1    Bindu, S.2    Dey, S.3    Goyal, M.4    Alam, A.5    Pal, C.6    Mitra, K.7    Bandyopadhyay, U.8
  • 45
    • 3142754211 scopus 로고    scopus 로고
    • 1 protection against D-galactosamine-induced cell death in cultured rat hepatocytes
    • Fouad, D., Siendones, E., Costán, G., and Muntané, J. (2004) Role of NF-κB activation and nitric oxide expression during PGE protection against D-galactosamine-induced cell death in cultured rat hepatocytes. Liver Int. 24, 227-236 (Pubitemid 38930862)
    • (2004) Liver International , vol.24 , Issue.3 , pp. 227-236
    • Fouad, D.1    Siendones, E.2    Costan, G.3    Muntane, J.4
  • 47
    • 72949116148 scopus 로고    scopus 로고
    • Calpain inhibition impairs TNF-α-mediated neutrophil adhesion, arrest, and oxidative burst
    • Wiemer, A. J., Lokuta, M. A., Surfus, J. C., Wernimont, S. A., and Huttenlocher, A. (2010) Calpain inhibition impairs TNF-α-mediated neutrophil adhesion, arrest, and oxidative burst. Mol. Immunol. 47, 894-902
    • (2010) Mol. Immunol. , vol.47 , pp. 894-902
    • Wiemer, A.J.1    Lokuta, M.A.2    Surfus, J.C.3    Wernimont, S.A.4    Huttenlocher, A.5
  • 48
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • Weiss, S. J., Klein, R., Slivka, A., and Wei, M. (1982) Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J. Clin. Invest. 70, 598-607 (Pubitemid 12054584)
    • (1982) Journal of Clinical Investigation , vol.70 , Issue.3 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 50
    • 84863405358 scopus 로고    scopus 로고
    • Tryptamine-gallic acid hybrid prevents nonsteroidal anti-inflammatory drug-induced gastropathy. Correction of mitochondrial dysfunction and inhibition of apoptosis in gastric mucosal cells
    • Pal, C., Bindu, S., Dey, S., Alam, A., Goyal, M., Iqbal, M. S., Sarkar, S., Kumar, R., Halder, K. K., Debnath, M. C., Adhikari, S., and Bandyopadhyay, U. (2012) Tryptamine-gallic acid hybrid prevents nonsteroidal anti-inflammatory drug-induced gastropathy. Correction of mitochondrial dysfunction and inhibition of apoptosis in gastric mucosal cells. J. Biol. Chem. 287, 3495-3509
    • (2012) J. Biol. Chem. , vol.287 , pp. 3495-3509
    • Pal, C.1    Bindu, S.2    Dey, S.3    Alam, A.4    Goyal, M.5    Iqbal, M.S.6    Sarkar, S.7    Kumar, R.8    Halder, K.K.9    Debnath, M.C.10    Adhikari, S.11    Bandyopadhyay, U.12
  • 51
    • 34848826062 scopus 로고    scopus 로고
    • Melatonin inhibits free radical-mediated mitochondrial-dependent hepatocyte apoptosis and liver damage induced during malarial infection
    • DOI 10.1111/j.1600-079X.2007.00488.x
    • Guha, M., Maity, P., Choubey, V., Mitra, K., Reiter, R. J., and Bandyopadhyay, U. (2007) Melatonin inhibits free radical-mediated mitochondrially dependent hepatocyte apoptosis and liver damage induced during malarial infection. J. Pineal Res. 43, 372-381 (Pubitemid 47512269)
    • (2007) Journal of Pineal Research , vol.43 , Issue.4 , pp. 372-381
    • Guha, M.1    Maity, P.2    Choubey, V.3    Mitra, K.4    Reiter, R.J.5    Bandyopadhyay, U.6
  • 52
    • 0038175547 scopus 로고    scopus 로고
    • A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical
    • DOI 10.1074/jbc.M210328200
    • Biswas, K., Bandyopadhyay, U., Chattopadhyay, I., Varadaraj, A., Ali, E., and Banerjee, R. K. (2003) A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical. J. Biol. Chem. 278, 10993-11001 (Pubitemid 36792647)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 10993-11001
    • Biswas, K.1    Bandyopadhyay, U.2    Chattopadhyay, I.3    Varadaraj, A.4    Ali, E.5    Banerjee, R.K.6
  • 53
    • 77953609415 scopus 로고    scopus 로고
    • Gallic acid prevents non-steroidal anti-inflammatory drug-induced gastropathy in rat by blocking oxidative stress and apoptosis
    • Pal, C., Bindu, S., Dey, S., Alam, A., Goyal, M., Iqbal, M. S., Maity, P., Adhikari, S. S., and Bandyopadhyay, U. (2010) Gallic acid prevents non-steroidal anti-inflammatory drug-induced gastropathy in rat by blocking oxidative stress and apoptosis. Free Radic. Biol. Med. 49, 258-267
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 258-267
    • Pal, C.1    Bindu, S.2    Dey, S.3    Alam, A.4    Goyal, M.5    Iqbal, M.S.6    Maity, P.7    Adhikari, S.S.8    Bandyopadhyay, U.9
  • 54
    • 62449189195 scopus 로고    scopus 로고
    • Melatonin reduces indomethacin-induced gastric mucosal cell apoptosis by preventing mitochondrial oxidative stress and the activation of mitochondrial pathway of apoptosis
    • Maity, P., Bindu, S., Dey, S., Goyal, M., Alam, A., Pal, C., Reiter, R., and Bandyopadhyay, U. (2009) Melatonin reduces indomethacin-induced gastric mucosal cell apoptosis by preventing mitochondrial oxidative stress and the activation of mitochondrial pathway of apoptosis. J. Pineal Res. 46, 314-323
    • (2009) J. Pineal Res. , vol.46 , pp. 314-323
    • Maity, P.1    Bindu, S.2    Dey, S.3    Goyal, M.4    Alam, A.5    Pal, C.6    Reiter, R.7    Bandyopadhyay, U.8
  • 55
    • 0022262310 scopus 로고
    • Hemopexin-mediated heme transport to the liver. Evidence for a heme-binding protein in liver plasma membranes
    • Smith, A., and Morgan, W. T. (1985) Hemopexin-mediated heme transport to the liver. Evidence for a heme-binding protein in liver plasma membranes. J. Biol. Chem. 260, 8325-8329 (Pubitemid 15249836)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.14 , pp. 8325-8329
    • Smith, A.1    Morgan, W.T.2
  • 56
    • 0033534451 scopus 로고    scopus 로고
    • Cellular protection mechanisms against extracellular heme. Heme-hemopexin, but not free heme, activates the N-terminal c-Jun kinase
    • Eskew, J. D., Vanacore, R. M., Sung, L., Morales, P. J., and Smith, A. (1999) Cellular protection mechanisms against extracellular heme. Heme-hemopexin, but not free heme, activates the N-terminal c-Jun kinase. J. Biol. Chem. 274, 638-648
    • (1999) J. Biol. Chem. , vol.274 , pp. 638-648
    • Eskew, J.D.1    Vanacore, R.M.2    Sung, L.3    Morales, P.J.4    Smith, A.5
  • 57
    • 0036781052 scopus 로고    scopus 로고
    • NF-κB regulation in the immune system
    • Li, Q., and Verma, I. M. (2002) NF-κB regulation in the immune system. Nat. Rev. Immunol. 2, 725-734
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 58
    • 33644842206 scopus 로고    scopus 로고
    • NF-κB and its regulation on the immune system
    • Liang, Y., Zhou, Y., and Shen, P. (2004) NF-κB and its regulation on the immune system. Cell. Mol. Immunol. 1, 343-350
    • (2004) Cell. Mol. Immunol. , vol.1 , pp. 343-350
    • Liang, Y.1    Zhou, Y.2    Shen, P.3
  • 59
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-κB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • DOI 10.1089/ars.2005.7.395
    • Kabe, Y., Ando, K., Hirao, S., Yoshida, M., and Handa, H. (2005) Redox regulation of NF-κB activation. Distinct redox regulation between the cytoplasm and the nucleus. Antioxid. Redox Signal. 7, 395-403 (Pubitemid 40279807)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.3-4 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 60
    • 3543150814 scopus 로고    scopus 로고
    • Tumour necrosis factor-α mediates neutrophil migration to the knee synovial cavity during immune inflammation
    • DOI 10.1016/j.ejphar.2004.06.003, PII S001429990400603X
    • Bombini, G., Canetti, C., Rocha, F. A., and Cunha, F. Q. (2004) Tumor necrosis factor-α mediates neutrophil migration to the knee synovial cavity during immune inflammation. Eur. J. Pharmacol. 496, 197-204 (Pubitemid 39024333)
    • (2004) European Journal of Pharmacology , vol.496 , Issue.1-3 , pp. 197-204
    • Bombini, G.1    Canetti, C.2    Rocha, F.A.C.3    Cunha, F.Q.4
  • 61
    • 22144438655 scopus 로고    scopus 로고
    • TNF-α promotes a stop signal that inhibits neutrophil polarization and migration via a p38 MAPK pathway
    • DOI 10.1189/jlb.0205067
    • Lokuta, M. A., and Huttenlocher, A. (2005) TNF-α promotes a stop signal that inhibits neutrophil polarization and migration via a p38 MAPK pathway. J. Leukocyte Biol. 78, 210-219 (Pubitemid 40979960)
    • (2005) Journal of Leukocyte Biology , vol.78 , Issue.1 , pp. 210-219
    • Lokuta, M.A.1    Huttenlocher, A.2
  • 63
    • 29844457587 scopus 로고    scopus 로고
    • The evolution of iron chelators for the treatment of iron overload disease and cancer
    • DOI 10.1124/pr.57.4.2
    • Kalinowski, D. S., and Richardson, D. R. (2005) The evolution of iron chelators for the treatment of iron overload disease and cancer. Pharmacol. Rev. 57, 547-583 (Pubitemid 43036441)
    • (2005) Pharmacological Reviews , vol.57 , Issue.4 , pp. 547-583
    • Kalinowski, D.S.1    Richardson, D.R.2
  • 64
    • 0029089089 scopus 로고
    • Dual effect of deferoxamine on free radical formation and reoxygenation injury in isolated hepatocytes
    • Caraceni, P., Van Thiel, D. H., and Borle, A. B. (1995) Dual effect of deferoxamine on free radical formation and reoxygenation injury in isolated hepatocytes. Am. J. Physiol. 269, G132-G137
    • (1995) Am. J. Physiol. , vol.269
    • Caraceni, P.1    Van Thiel, D.H.2    Borle, A.B.3
  • 65
    • 0026542568 scopus 로고
    • Inhibition of hemin-induced hemolysis by desferrioxamine. Binding of hemin to red cell membranes and the effects of alteration of membrane sulfhydryl groups
    • Sullivan, S. G., Baysal, E., and Stern, A. (1992) Inhibition of hemin-induced hemolysis by desferrioxamine. Binding of hemin to red cell membranes and the effects of alteration of membrane sulfhydryl groups. Biochim. Biophys. Acta 1104, 38-44
    • (1992) Biochim. Biophys. Acta , vol.1104 , pp. 38-44
    • Sullivan, S.G.1    Baysal, E.2    Stern, A.3
  • 68
    • 0032103942 scopus 로고    scopus 로고
    • A pathogenic role of IL-12 in blood-stage murine malaria lethal strain Plasmodium berghei NK65 infection
    • Yoshimoto, T., Takahama, Y., Wang, C. R., Yoneto, T., Waki, S., and Nariuchi, H. (1998) A pathogenic role of IL-12 in blood-stage murine malaria lethal strain Plasmodium berghei NK65 infection. J. Immunol. 160, 5500-5505 (Pubitemid 28267842)
    • (1998) Journal of Immunology , vol.160 , Issue.11 , pp. 5500-5505
    • Yoshimoto, T.1    Takahama, Y.2    Wang, C.-R.3    Yoneto, T.4    Waki, S.5    Nariuchi, H.6
  • 69
    • 44349091446 scopus 로고    scopus 로고
    • An experimental model for fatal malaria due to TNF-α-dependent hepatic damage
    • DOI 10.1017/S0031182008004344, PII S0031182008004344
    • Seixas, E., Oliveira, P., Moura Nunes, J. F., and Coutinho, A. (2008) An experimental model for fatal malaria due to TNF-α-dependent hepatic damage. Parasitology 135, 683-690 (Pubitemid 351733163)
    • (2008) Parasitology , vol.135 , Issue.6 , pp. 683-690
    • Seixas, E.1    Oliveira, P.2    Moura, N.J.F.3    Coutinho, A.4
  • 70
    • 33750471197 scopus 로고    scopus 로고
    • Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: Molecular basis and biological significance
    • DOI 10.1038/sj.onc.1209936, PII 1209936
    • Bubici, C., Papa, S., Dean, K., and Franzoso, G. (2006) Mutual cross-talk between reactive oxygen species and nuclear factor-κB. Molecular basis and biological significance. Oncogene 25, 6731-6748 (Pubitemid 44657849)
    • (2006) Oncogene , vol.25 , Issue.51 , pp. 6731-6748
    • Bubici, C.1    Papa, S.2    Dean, K.3    Franzoso, G.4
  • 71
    • 0027199115 scopus 로고
    • Reactive oxygen intermediates activate NF-κB in a tyrosine kinase- dependent mechanism and in combination with vanadate activate the p56(lck) and p59(fyn) tyrosine kinases in human lymphocytes
    • Schieven, G. L., Kirihara, J. M., Myers, D. E., Ledbetter, J. A., and Uckun, F. M. (1993) Reactive oxygen intermediates activate NF-κB in a tyrosine kinase-dependent mechanism and in combination with vanadate activate the p56lck and p59fyn tyrosine kinases in human lymphocytes. Blood 82, 1212-1220 (Pubitemid 23253996)
    • (1993) Blood , vol.82 , Issue.4 , pp. 1212-1220
    • Schieven, G.L.1    Kirihara, J.M.2    Myers, D.E.3    Ledbetter, J.A.4    Uckun, F.M.5
  • 72
    • 0034655179 scopus 로고    scopus 로고
    • Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl- terminal PEST domain of IκBα in NF-κB activation by an oxidative stress
    • Schoonbroodt, S., Ferreira, V., Best-Belpomme, M., Boelaert, J. R., Legrand-Poels, S., Korner, M., and Piette, J. (2000) Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress. J. Immunol. 164, 4292-4300 (Pubitemid 30215091)
    • (2000) Journal of Immunology , vol.164 , Issue.8 , pp. 4292-4300
    • Schoonbroodt, S.1    Ferreira, V.2    Best-Belpomme, M.3    Boelaert, J.R.4    Legrand-Poels, S.5    Korner, M.6    Piette, J.7
  • 73
    • 0037591401 scopus 로고    scopus 로고
    • Hydrogen peroxide activates NF-κB through tyrosine phosphorylation of IκB and serαine phosphorylation of p65. Evidence for the involvement of IκBα kinase and Syk protein-tyrosine kinase
    • DOI 10.1074/jbc.M212389200
    • Takada, Y., Mukhopadhyay, A., Kundu, G. C., Mahabeleshwar, G. H., Singh, S., and Aggarwal, B. B. (2003) Hydrogen peroxide activates NF-κB through tyrosine phosphorylation of IκBα and serine phosphorylation of p65. Evidence for the involvement of IκBα kinase and Syk protein-tyrosine kinase. J. Biol. Chem. 278, 24233-24241 (Pubitemid 36830260)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 24233-24241
    • Takada, Y.1    Mukhopadhyay, A.2    Kundu, G.C.3    Mahabeleshwar, G.H.4    Singh, S.5    Aggarwal, B.B.6
  • 74
    • 78650894319 scopus 로고    scopus 로고
    • Cross-talk of reactive oxygen species and NF-κB signaling
    • Morgan, M. J., and Liu, Z. G. (2011) Cross-talk of reactive oxygen species and NF-κB signaling. Cell Res. 21, 103-115
    • (2011) Cell Res. , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 75
    • 33645971047 scopus 로고    scopus 로고
    • Good cop, bad cop. The different faces of NF-κB
    • Perkins, N. D., and Gilmore, T. D. (2006) Good cop, bad cop. The different faces of NF-κB. Cell Death Differ. 13, 759-772
    • (2006) Cell Death Differ. , vol.13 , pp. 759-772
    • Perkins, N.D.1    Gilmore, T.D.2
  • 76
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins. New discoveries and insights
    • Baldwin, A. S., Jr. (1996) The NF-κB and IκB proteins. New discoveries and insights. Annu. Rev. Immunol. 14, 649-683
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 78
    • 77952575494 scopus 로고    scopus 로고
    • Pathology of immune-mediated liver injury
    • Dienes, H. P., and Drebber, U. (2010) Pathology of immune-mediated liver injury. Dig. Dis. 28, 57-62
    • (2010) Dig. Dis. , vol.28 , pp. 57-62
    • Dienes, H.P.1    Drebber, U.2
  • 80
    • 0032862559 scopus 로고    scopus 로고
    • Activation of nuclear factor kappa B and cytokine imbalance in experimental alcoholic liver disease in the rat
    • DOI 10.1002/hep.510300402
    • Nanji, A. A., Jokelainen, K., Rahemtulla, A., Miao, L., Fogt, F., Matsumoto, H., Tahan, S. R., and Su, G. L. (1999) Activation of nuclear factor κB and cytokine imbalance in experimental alcoholic liver disease in the rat. Hepatology 30, 934-943 (Pubitemid 29458282)
    • (1999) Hepatology , vol.30 , Issue.4 , pp. 934-943
    • Nanji, A.A.1    Jokelainen, K.2    Rahemtulla, A.3    Miao, L.4    Fogt, F.5    Matsumoto, H.6    Tahan, S.R.7    Su, G.L.8
  • 81
    • 84858787280 scopus 로고    scopus 로고
    • Neutrophils and intravascular immunity in the liver during infection and sterile inflammation
    • McDonald, B., and Kubes, P. (2012) Neutrophils and intravascular immunity in the liver during infection and sterile inflammation. Toxicol. Pathol. 40, 157-165
    • (2012) Toxicol. Pathol. , vol.40 , pp. 157-165
    • McDonald, B.1    Kubes, P.2
  • 82
    • 33646867426 scopus 로고    scopus 로고
    • Mechanisms of liver injury. II. Mechanisms of neutrophil-induced liver cell injury during hepatic ischemia-reperfusion and other acute inflammatory conditions
    • Jaeschke, H. (2006) Mechanisms of liver injury. II. Mechanisms of neutrophil-induced liver cell injury during hepatic ischemia-reperfusion and other acute inflammatory conditions. Am. J. Physiol. Gastrointest. Liver Physiol. 290, G1083-L1088
    • (2006) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.290
    • Jaeschke, H.1
  • 83
    • 1342324592 scopus 로고    scopus 로고
    • Hemozoin-Inducible Proinflammatory Events In Vivo: Potential Role in Malaria Infection
    • Jaramillo, M., Plante, I., Ouellet, N., Vandal, K., Tessier, P. A., and Olivier, M. (2004) Hemozoin-inducible proinflammatory events in vivo. Potential role in malaria infection. J. Immunol. 172, 3101-3110 (Pubitemid 38263700)
    • (2004) Journal of Immunology , vol.172 , Issue.5 , pp. 3101-3110
    • Jaramillo, M.1    Plante, I.2    Ouellet, N.3    Vandal, K.4    Tessier, P.A.5    Olivier, M.6
  • 84
    • 74049105256 scopus 로고    scopus 로고
    • Pure Hemozoin is inflammatory in vivo and activates the NALP3 inflammasome via release of uric acid
    • Griffith, J. W., Sun, T., McIntosh, M. T., and Bucala, R. (2009) Pure Hemozoin is inflammatory in vivo and activates the NALP3 inflammasome via release of uric acid. J. Immunol. 183, 5208-5220
    • (2009) J. Immunol. , vol.183 , pp. 5208-5220
    • Griffith, J.W.1    Sun, T.2    McIntosh, M.T.3    Bucala, R.4
  • 85
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase. Friend and foe
    • Klebanoff, S. J. (2005) Myeloperoxidase. Friend and foe. J. Leukocyte Biol. 77, 598-625
    • (2005) J. Leukocyte Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 86
    • 27844442307 scopus 로고    scopus 로고
    • Myeloperoxidase-generated oxidants modulate left ventricular remodeling but not infarct size after myocardial infarction
    • DOI 10.1161/CIRCULATIONAHA.105.542340
    • Vasilyev, N., Williams, T., Brennan, M. L., Unzek, S., Zhou, X., Heinecke, J. W., Spitz, D. R., Topol, E. J., Hazen, S. L., and Penn, M. S. (2005) Myeloperoxidase-generated oxidants modulate left ventricular remodeling but not infarct size after myocardial infarction. Circulation 112, 2812-2820 (Pubitemid 41643823)
    • (2005) Circulation , vol.112 , Issue.18 , pp. 2812-2820
    • Vasilyev, N.1    Williams, T.2    Brennan, M.-L.3    Unzek, S.4    Zhou, X.5    Heinecke, J.W.6    Spitz, D.R.7    Topol, E.J.8    Hazen, S.L.9    Pen, M.S.10
  • 87
    • 0033956503 scopus 로고    scopus 로고
    • Neutrophil elastase inhibition reduces cerebral ischemic damage in the middle cerebral artery occlusion
    • DOI 10.1016/S0006-8993(99)02431-2, PII S0006899399024312
    • Shimakura, A., Kamanaka, Y., Ikeda, Y., Kondo, K., Suzuki, Y., and Umemura, K. (2000) Neutrophil elastase inhibition reduces cerebral ischemic damage in the middle cerebral artery occlusion. Brain Res. 858, 55-60 (Pubitemid 30105781)
    • (2000) Brain Research , vol.858 , Issue.1 , pp. 55-60
    • Shimakura, A.1    Kamanaka, Y.2    Ikeda, Y.3    Kondo, K.4    Suzuki, Y.5    Umemura, K.6
  • 88
    • 51349126118 scopus 로고    scopus 로고
    • Physiology and pathophysiology of liver inflammation, damage, and repair
    • Ramadori, G., Moriconi, F., Malik, I., and Dudas, J. (2008) Physiology and pathophysiology of liver inflammation, damage, and repair. J. Physiol. Pharmacol. 59, 107-117
    • (2008) J. Physiol. Pharmacol. , vol.59 , pp. 107-117
    • Ramadori, G.1    Moriconi, F.2    Malik, I.3    Dudas, J.4
  • 91
    • 79551583880 scopus 로고    scopus 로고
    • N-Acetylcysteine attenuates dimethylnitrosamine-induced oxidative stress in rats
    • Sathish, P., Paramasivan, V., Palani, V., and Sivanesan, K. (2011) N-Acetylcysteine attenuates dimethylnitrosamine-induced oxidative stress in rats. Eur. J. Pharmacol. 654, 181-186
    • (2011) Eur. J. Pharmacol. , vol.654 , pp. 181-186
    • Sathish, P.1    Paramasivan, V.2    Palani, V.3    Sivanesan, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.