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Volumn 157, Issue 3, 2005, Pages 175-188

Free heme toxicity and its detoxification systems in human

Author keywords

Heme; Heme detoxification; Inflammation; Reactive oxygen species; Toxicity

Indexed keywords

ALBUMIN; ALPHA 1 MICROGLOBULIN; CYTOSKELETON PROTEIN; DNA; GLUTATHIONE TRANSFERASE; HEME; HEME OXYGENASE; HEMOPEXIN; LIPID PEROXIDE;

EID: 19444386445     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxlet.2005.03.004     Document Type: Review
Times cited : (678)

References (115)
  • 1
    • 31044445303 scopus 로고
    • Molecular regulation: Biological role of heme in hematopoiesis
    • N.G. Abraham Molecular regulation: biological role of heme in hematopoiesis Blood Rev. 5 1991 19 28
    • (1991) Blood Rev. , vol.5 , pp. 19-28
    • Abraham, N.G.1
  • 2
    • 0021100151 scopus 로고
    • Hemin-mediated DNA strand scission
    • R.L. Aft, and G.C. Mueller Hemin-mediated DNA strand scission J. Biol. Chem. 258 1983 12069 12072
    • (1983) J. Biol. Chem. , vol.258 , pp. 12069-12072
    • Aft, R.L.1    Mueller, G.C.2
  • 3
    • 3242741986 scopus 로고    scopus 로고
    • Heme inhibits human neutrophil apoptosis: Involvement of phosphoinositide 3-kinase, MAPK, and NF-κB
    • M.A. Arruda, A.G. Rossi, M.S. De Freitas, C. Barja-Fidalgo, and A.V. Graca-Souza Heme inhibits human neutrophil apoptosis: involvement of phosphoinositide 3-kinase, MAPK, and NF-κB J. Immunol. 173 2004 2023 2030
    • (2004) J. Immunol. , vol.173 , pp. 2023-2030
    • Arruda, M.A.1    Rossi, A.G.2    De Freitas, M.S.3    Barja-Fidalgo, C.4    Graca-Souza, A.V.5
  • 4
    • 0028828562 scopus 로고
    • Heme degradation in the presence of glutathione
    • H. Atamna, Atamna, and H. Ginsburg Heme degradation in the presence of glutathione J. Biol. Chem. 270 1995 24876 24883
    • (1995) J. Biol. Chem. , vol.270 , pp. 24876-24883
    • Atamna, H.1    Atamna2    Ginsburg, H.3
  • 5
    • 0034210202 scopus 로고    scopus 로고
    • Ferriporphyrins and endothelium: A 2-edged sword-promotion of oxidation and induction of cytoprotectants
    • J. Balla, G. Balla, V. Jeney, G. Kakuk, H.S. Jacob, and G.M. Vercellotti Ferriporphyrins and endothelium: a 2-edged sword-promotion of oxidation and induction of cytoprotectants Blood 95 2000 3442 3450
    • (2000) Blood , vol.95 , pp. 3442-3450
    • Balla, J.1    Balla, G.2    Jeney, V.3    Kakuk, G.4    Jacob, H.S.5    Vercellotti, G.M.6
  • 7
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage
    • J. Balla, H.S. Jacob, G. Balla, K. Nath, J.W. Eaton, and G.M. Vercellotti Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage Proc. Natl. Acad. Sci. U.S.A. 90 1993 9285 9289
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 9
    • 0025819677 scopus 로고
    • Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species
    • G. Balla, G.M. Vercellotti, U. Muller-Eberhard, J.W. Eaton, and H.S. Jacob Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species Lab. Invest. 64 1991 648 655
    • (1991) Lab. Invest. , vol.64 , pp. 648-655
    • Balla, G.1    Vercellotti, G.M.2    Muller-Eberhard, U.3    Eaton, J.W.4    Jacob, H.S.5
  • 10
    • 0037051177 scopus 로고    scopus 로고
    • Extrathyroidal actions of antithyroid thionamides
    • U. Bandyopadhyay, K. Biswas, and R.K. Banerjee Extrathyroidal actions of antithyroid thionamides Toxicol. Lett. 128 2002 117 128
    • (2002) Toxicol. Lett. , vol.128 , pp. 117-128
    • Bandyopadhyay, U.1    Biswas, K.2    Banerjee, R.K.3
  • 11
    • 0026716947 scopus 로고
    • Localization of gastric peroxidase and its inhibition by mercaptomethylimidazole, an inducer of gastric acid secretion
    • U. Bandyopadhyay, D.K. Bhattacharyya, R. Chatterjee, and R.K. Banerjee Localization of gastric peroxidase and its inhibition by mercaptomethylimidazole, an inducer of gastric acid secretion Biochem. J. 284 1992 305 312
    • (1992) Biochem. J. , vol.284 , pp. 305-312
    • Bandyopadhyay, U.1    Bhattacharyya, D.K.2    Chatterjee, R.3    Banerjee, R.K.4
  • 12
    • 0028941087 scopus 로고
    • Irreversible inactivation of lactoperoxidase by mercaptomethylimidazole through generation of a thiyl radical: Its use as a probe to study the active site
    • U. Bandyopadhyay, D.K. Bhattacharyya, R. Chatterjee, and R.K. Banerjee Irreversible inactivation of lactoperoxidase by mercaptomethylimidazole through generation of a thiyl radical: its use as a probe to study the active site Biochem. J. 306 1995 751 757
    • (1995) Biochem. J. , vol.306 , pp. 751-757
    • Bandyopadhyay, U.1    Bhattacharyya, D.K.2    Chatterjee, R.3    Banerjee, R.K.4
  • 14
    • 15744383185 scopus 로고    scopus 로고
    • Role of active site residues in peroxidase catalysis: Studies on horseradish peroxidase
    • U. Bandyopadhyay, S. Adak, and R.K. Banerjee Role of active site residues in peroxidase catalysis: studies on horseradish peroxidase Proc. Ind. Natl. Sci. Acad. B 65 1999 315 330
    • (1999) Proc. Ind. Natl. Sci. Acad. B , vol.65 , pp. 315-330
    • Bandyopadhyay, U.1    Adak, S.2    Banerjee, R.K.3
  • 15
    • 0022842729 scopus 로고
    • Role of heme compounds in the erythrocyte membrane damage induced by lipid hydroperoxide
    • M. Beppu, M. Nagoya, and K. Kikugawa Role of heme compounds in the erythrocyte membrane damage induced by lipid hydroperoxide Chem. Pharm. Bull. 34 1986 5063 5070
    • (1986) Chem. Pharm. Bull. , vol.34 , pp. 5063-5070
    • Beppu, M.1    Nagoya, M.2    Kikugawa, K.3
  • 16
    • 0026666350 scopus 로고
    • Chemical and kinetic evidence for an essential histidine in horseradish peroxidase for iodine oxidation
    • D.K. Bhattacharyya, U. Bandyopadhyay, and R.K. Banerjee Chemical and kinetic evidence for an essential histidine in horseradish peroxidase for iodine oxidation J. Biol. Chem. 267 1992 9800 9804
    • (1992) J. Biol. Chem. , vol.267 , pp. 9800-9804
    • Bhattacharyya, D.K.1    Bandyopadhyay, U.2    Banerjee, R.K.3
  • 19
    • 0031965781 scopus 로고    scopus 로고
    • Hemin binding and oxidation of lipoproteins in serum: Mechanisms and effect on the interaction of LDL with human macrophages
    • G. Camejo, C. Halberg, A. Manschik-Lundin, H. Olsson, G.B. Forsberg, and B. Ylhen Hemin binding and oxidation of lipoproteins in serum: mechanisms and effect on the interaction of LDL with human macrophages J. lipid Res. 39 1998 755 766
    • (1998) J. Lipid Res. , vol.39 , pp. 755-766
    • Camejo, G.1    Halberg, C.2    Manschik-Lundin, A.3    Olsson, H.4    Forsberg, G.B.5    Ylhen, B.6
  • 20
    • 0019343952 scopus 로고
    • Loss of haem and haemoproteins during the generation of superoxide anion and hydrogen peroxide: A pathway not involving production of carbon monoxide
    • L. Cantoni, A.H. Gibbs, and F. De Matteis Loss of haem and haemoproteins during the generation of superoxide anion and hydrogen peroxide: a pathway not involving production of carbon monoxide Int. J. Biochem. 13 1981 823 830
    • (1981) Int. J. Biochem. , vol.13 , pp. 823-830
    • Cantoni, L.1    Gibbs, A.H.2    De Matteis, F.3
  • 22
    • 0019868276 scopus 로고
    • Hemin enhances the differentiation of mouse 3T3 cells to adipocytes
    • J.J. Chen, and I.M. London Hemin enhances the differentiation of mouse 3T3 cells to adipocytes Cell 26 1981 117 122
    • (1981) Cell , vol.26 , pp. 117-122
    • Chen, J.J.1    London, I.M.2
  • 23
    • 0019355321 scopus 로고
    • Mechanism of hemolysis induced by FP (IX)
    • A.C. Chou, and C.D. Fitch Mechanism of hemolysis induced by FP (IX) J. Clin. Invest. 68 1981 672 677
    • (1981) J. Clin. Invest. , vol.68 , pp. 672-677
    • Chou, A.C.1    Fitch, C.D.2
  • 25
    • 0038521317 scopus 로고    scopus 로고
    • Heme, not protein or inorganic iron, is responsible for endogenous intestinal N-nitrosation arising from red meat
    • A.J. Cross, J.R. Pollock, and S.A. Bingham Heme, not protein or inorganic iron, is responsible for endogenous intestinal N-nitrosation arising from red meat Cancer Res. 63 2003 2358 2360
    • (2003) Cancer Res. , vol.63 , pp. 2358-2360
    • Cross, A.J.1    Pollock, J.R.2    Bingham, S.A.3
  • 26
    • 0024294403 scopus 로고
    • Probing structure-function relations in heme containing oxygenases and peroxidases
    • J.H. Dawson Probing structure-function relations in heme containing oxygenases and peroxidases Science 240 1988 433 439
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 27
    • 0034806977 scopus 로고    scopus 로고
    • Hemopexin: A review of biological aspects and the role in laboratory medicine
    • J.R. Delanghe, and M.R. Langlois Hemopexin: a review of biological aspects and the role in laboratory medicine Clin. Chim. Acta 312 2001 13 23
    • (2001) Clin. Chim. Acta , vol.312 , pp. 13-23
    • Delanghe, J.R.1    Langlois, M.R.2
  • 28
    • 0021693485 scopus 로고
    • Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase
    • J.C. Docherty, G.D. Firneisz, and B.A. Schacter Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase Arch. Biochem. Biophys. 235 1984 657 664
    • (1984) Arch. Biochem. Biophys. , vol.235 , pp. 657-664
    • Docherty, J.C.1    Firneisz, G.D.2    Schacter, B.A.3
  • 29
    • 0025969686 scopus 로고
    • Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron
    • R.S. Eisenstein, D. Garcia-Mayol, W. Pettingell, and H.N. Munro Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron Proc. Natl. Acad. Sci. U.S.A. 88 1991 688 692
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 688-692
    • Eisenstein, R.S.1    Garcia-Mayol, D.2    Pettingell, W.3    Munro, H.N.4
  • 30
    • 0017353198 scopus 로고
    • Enzymatic formation and cellular regulation of heme synthesis
    • A.S. Gidari, and R.D. Levere Enzymatic formation and cellular regulation of heme synthesis Semin. Hematol. 14 1977 145 168
    • (1977) Semin. Hematol. , vol.14 , pp. 145-168
    • Gidari, A.S.1    Levere, R.D.2
  • 31
    • 0037716283 scopus 로고    scopus 로고
    • Hemin induces an iron-dependent, oxidative injury to human neuron-like cells
    • L. Goldstein, Z.P. Teng, E. Zeserson, M. Patel, and R.F. Regan Hemin induces an iron-dependent, oxidative injury to human neuron-like cells J. Neurosci. Res. 73 2003 113 121
    • (2003) J. Neurosci. Res. , vol.73 , pp. 113-121
    • Goldstein, L.1    Teng, Z.P.2    Zeserson, E.3    Patel, M.4    Regan, R.F.5
  • 33
    • 0027978986 scopus 로고
    • Bilirubin and ascorbate antioxidant activity in neonatal plasma
    • V. Gopinathan, N.J. Miller, A.D. Milner, and C.A. Rice-Evans Bilirubin and ascorbate antioxidant activity in neonatal plasma FEBS Lett. 349 1994 197 200
    • (1994) FEBS Lett. , vol.349 , pp. 197-200
    • Gopinathan, V.1    Miller, N.J.2    Milner, A.D.3    Rice-Evans, C.A.4
  • 35
    • 0032800507 scopus 로고    scopus 로고
    • The effects of heme-binding proteins on the peroxidative and catalytic activities of hemin
    • L.N. Grinberg, P.J. O'Brien, and Z. Hrkal The effects of heme-binding proteins on the peroxidative and catalytic activities of hemin Free Radic. Biol. Med. 26 1999 214 219
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 214-219
    • Grinberg, L.N.1    O'Brien, P.J.2    Hrkal, Z.3
  • 36
    • 0018095311 scopus 로고
    • Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase
    • F.P. Guengerich Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase Biochemistry 17 1978 3633 3639
    • (1978) Biochemistry , vol.17 , pp. 3633-3639
    • Guengerich, F.P.1
  • 37
    • 0024241523 scopus 로고
    • Antioxidant protection by hemopexin of heme stimulated lipid peroxidation
    • J.M.C. Gutteridge, and A. Smith Antioxidant protection by hemopexin of heme stimulated lipid peroxidation Biochem. J. 256 1988 861 865
    • (1988) Biochem. J. , vol.256 , pp. 861-865
    • Gutteridge, J.M.C.1    Smith, A.2
  • 39
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • P.M. Harrison, and P. Arosio The ferritins: molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta 1275 1996 161 203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 41
    • 0034022619 scopus 로고    scopus 로고
    • Pathogenesis of renal failure in rhabdomyolysis: The role of myoglobin
    • S. Holt, and K. Moore Pathogenesis of renal failure in rhabdomyolysis: the role of myoglobin Exp. Nephrol. 8 2000 72 76
    • (2000) Exp. Nephrol. , vol.8 , pp. 72-76
    • Holt, S.1    Moore, K.2
  • 43
    • 0028818098 scopus 로고
    • Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase and heavy metal in primary rat hepatocytes and hepatoma cells
    • S. Immenschuh, S.-I. Iwahara, H. Satoh, C. Nell, N. Katz, and U. Muller-Eberhard Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase and heavy metal in primary rat hepatocytes and hepatoma cells Biochemistry 34 1995 13407 13411
    • (1995) Biochemistry , vol.34 , pp. 13407-13411
    • Immenschuh, S.1    Iwahara, S.-I.2    Satoh, H.3    Nell, C.4    Katz, N.5    Muller-Eberhard, U.6
  • 44
    • 0034668216 scopus 로고    scopus 로고
    • Gene regulation of heme oxygenase-1 as a therapeutic target
    • S. Immenschuh, and G. Ramadori Gene regulation of heme oxygenase-1 as a therapeutic target Biochem. Pharmacol. 60 2000 1121 1128
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1121-1128
    • Immenschuh, S.1    Ramadori, G.2
  • 45
    • 0021955120 scopus 로고
    • A two-molecule mechanism of heme degradation
    • H.A. Itano, and T.A. Hirota A two-molecule mechanism of heme degradation Biochem. J. 226 1985 767 771
    • (1985) Biochem. J. , vol.226 , pp. 767-771
    • Itano, H.A.1    Hirota, T.A.2
  • 48
    • 0035366598 scopus 로고    scopus 로고
    • Repression of the heavy ferritin chain increases the labile iron pool of human K562 cells
    • O. Kakhlon, Y. Gruenbaum, and Z.L. Cabantchik Repression of the heavy ferritin chain increases the labile iron pool of human K562 cells Biochem. J. 356 2001 311 316
    • (2001) Biochem. J. , vol.356 , pp. 311-316
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.L.3
  • 49
    • 0022553242 scopus 로고
    • Control of heme metabolism with synthetic metalloporphyrins
    • A. Kappas, and G.S. Drummond Control of heme metabolism with synthetic metalloporphyrins J. Clin. Investig. 77 1986 335 339
    • (1986) J. Clin. Investig. , vol.77 , pp. 335-339
    • Kappas, A.1    Drummond, G.S.2
  • 50
    • 4644329141 scopus 로고    scopus 로고
    • Non-specific inhibition of human cytochrome P450-catalyzed reactions by hemin
    • E.Y. Kim, M.Y. Kim, W.S. Koh, F.P. Guengerich, and C.H. Yun Non-specific inhibition of human cytochrome P450-catalyzed reactions by hemin Toxicol. Lett. 153 2004 239 246
    • (2004) Toxicol. Lett. , vol.153 , pp. 239-246
    • Kim, E.Y.1    Kim, M.Y.2    Koh, W.S.3    Guengerich, F.P.4    Yun, C.H.5
  • 51
    • 0020382669 scopus 로고
    • The interaction of hemin and bilirubin with the human red cell membrane
    • I. Kirschner-Zilber, E. Rabizadeh, and N. Shaklai The interaction of hemin and bilirubin with the human red cell membrane Biochem. Biophys. Acta 690 1982 20 30
    • (1982) Biochem. Biophys. Acta , vol.690 , pp. 20-30
    • Kirschner-Zilber, I.1    Rabizadeh, E.2    Shaklai, N.3
  • 52
    • 0023835962 scopus 로고
    • Rat liver cytochrome P-450b, P-420b, and P-420c are degraded to biliverdin by heme oxygenase
    • R.K. Kutty, R.F. Daniel, D.E. Ryan, W. Levine, and M.D. Maines Rat liver cytochrome P-450b, P-420b, and P-420c are degraded to biliverdin by heme oxygenase Arch. Biochem. Biophys. 260 1988 638 644
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 638-644
    • Kutty, R.K.1    Daniel, R.F.2    Ryan, D.E.3    Levine, W.4    Maines, M.D.5
  • 53
    • 0020479556 scopus 로고
    • Oxidation of heme c derivatives by purified heme oxygenase: Evidence for the presence of one molecule species of heme oxygenase in the rat liver
    • R.K. Kutty, and M.D. Maines Oxidation of heme c derivatives by purified heme oxygenase: evidence for the presence of one molecule species of heme oxygenase in the rat liver J. Biol. Chem. 257 1982 9944 9952
    • (1982) J. Biol. Chem. , vol.257 , pp. 9944-9952
    • Kutty, R.K.1    Maines, M.D.2
  • 54
    • 0023404188 scopus 로고
    • Characterization of an NADH-dependent heme degrading ststem in the heart mitochondria
    • R.K. Kutty, and M.D. Maines Characterization of an NADH-dependent heme degrading ststem in the heart mitochondria Biochem. J. 246 1987 467 474
    • (1987) Biochem. J. , vol.246 , pp. 467-474
    • Kutty, R.K.1    Maines, M.D.2
  • 55
    • 7944227387 scopus 로고    scopus 로고
    • The lipocalin alpha (1)-microglobulin binds heme in different species
    • J. Larsson, M. Allhorn, and B. Kerstrom The lipocalin alpha (1)-microglobulin binds heme in different species Arch. Biochem. Biophys. 432 2004 196 204
    • (2004) Arch. Biochem. Biophys. , vol.432 , pp. 196-204
    • Larsson, J.1    Allhorn, M.2    Kerstrom, B.3
  • 56
    • 0034701113 scopus 로고    scopus 로고
    • Age-dependent increase of heme oxygenase-1 gene expression in the liver mediated by NF kappa B
    • Y. Lavrovsky, C.S. Sog, B. Chatterjee, and A.K. Roy Age-dependent increase of heme oxygenase-1 gene expression in the liver mediated by NF kappa B Mech. Ageing Dev. 114 2000 49 60
    • (2000) Mech. Ageing Dev. , vol.114 , pp. 49-60
    • Lavrovsky, Y.1    Sog, C.S.2    Chatterjee, B.3    Roy, A.K.4
  • 57
    • 0028307310 scopus 로고
    • Identification of binding sites for transcription factors NF-kappa B and AP-2 in the promoter region of the human heme oxygenase1 gene
    • Y. Lavrovsky, M.L. Schwartzman, R.D. Levere, and N.G. Abraham Identification of binding sites for transcription factors NF-kappa B and AP-2 in the promoter region of the human heme oxygenase1 gene Proc. Natl. Acad. Sci. U.S.A. 91 1994 5987 5991
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5987-5991
    • Lavrovsky, Y.1    Schwartzman, M.L.2    Levere, R.D.3    Abraham, N.G.4
  • 58
    • 0019331875 scopus 로고
    • Role of superoxide in DNA strand scission
    • S.A. Lesko, R.J. Lorentzen, and O.P. Paul Role of superoxide in DNA strand scission Biochemistry 19 1980 3023 3028
    • (1980) Biochemistry , vol.19 , pp. 3023-3028
    • Lesko, S.A.1    Lorentzen, R.J.2    Paul, O.P.3
  • 59
    • 0027234437 scopus 로고
    • Hemin: Levels in experimental subarachnoid hematoma and effects on dissociated vascular smooth muscle cells
    • P.B. Letarte, K. Lieberman, K. Nagatani, R.A. Haworth, G.B. Odell, and T.A. Duff Hemin: levels in experimental subarachnoid hematoma and effects on dissociated vascular smooth muscle cells J. Neurosurg. 79 1993 252 255
    • (1993) J. Neurosurg. , vol.79 , pp. 252-255
    • Letarte, P.B.1    Lieberman, K.2    Nagatani, K.3    Haworth, R.A.4    Odell, G.B.5    Duff, T.A.6
  • 60
    • 0022413423 scopus 로고
    • Hemin mediated dissociation of erythrocyte membrane skeletal proteins
    • S.C. Liu, S. Zhai, J. Lawler, and J. Palek Hemin mediated dissociation of erythrocyte membrane skeletal proteins J. Biol. Chem. 260 1985 12234 12239
    • (1985) J. Biol. Chem. , vol.260 , pp. 12234-12239
    • Liu, S.C.1    Zhai, S.2    Lawler, J.3    Palek, J.4
  • 62
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • M.D. Maines Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications FASEB J. 2 1988 2557 2568
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 63
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • M.D. Maines The heme oxygenase system: a regulator of second messenger gases Ann. Rev. Pharmacol. Toxicol. 37 1997 517 554
    • (1997) Ann. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 64
    • 0008881566 scopus 로고    scopus 로고
    • The heme oxygenase system and its functions in brain
    • M.D. Maines The heme oxygenase system and its functions in brain Cell. Mol. Biol. 46 2000 573 585
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 573-585
    • Maines, M.D.1
  • 67
    • 0028574776 scopus 로고
    • Oxidative crosslinking of LDL protein induced by hemin: Involvement of tyrosines
    • Y.I. Miller, and N. Shaklai Oxidative crosslinking of LDL protein induced by hemin: involvement of tyrosines Biochem. Mol. Biol. Int. 34 1994 1121 1129
    • (1994) Biochem. Mol. Biol. Int. , vol.34 , pp. 1121-1129
    • Miller, Y.I.1    Shaklai, N.2
  • 68
    • 4544246612 scopus 로고    scopus 로고
    • CD163: A regulated hemoglobin scavenger receptor with a role in the anti-inflammatory response
    • S.K. Moestrup, and H.J. Moller CD163: a regulated hemoglobin scavenger receptor with a role in the anti-inflammatory response Ann. Med. 36 2004 347 354
    • (2004) Ann. Med. , vol.36 , pp. 347-354
    • Moestrup, S.K.1    Moller, H.J.2
  • 69
  • 70
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • G.C. Mueller, and R.L. Aft Hemin-mediated oxidative degradation of proteins J. Biol. Chem. 259 1984 301 305
    • (1984) J. Biol. Chem. , vol.259 , pp. 301-305
    • Mueller, G.C.1    Aft, R.L.2
  • 71
    • 0027498438 scopus 로고
    • Bioactivity of heme and its containments
    • U. Muller-Eberhard, and M. Fraig Bioactivity of heme and its containments Am. J. Hematol. 42 1993 59 62
    • (1993) Am. J. Hematol. , vol.42 , pp. 59-62
    • Muller-Eberhard, U.1    Fraig, M.2
  • 72
    • 0014360531 scopus 로고
    • Plasma concentration of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • U. Muller-Eberhard, J. Javid, H.H. Liem, A. Hanstein, and M. Hanna Plasma concentration of hemopexin, haptoglobin and heme in patients with various hemolytic diseases Blood 32 1968 811 815
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Liem, H.H.3    Hanstein, A.4    Hanna, M.5
  • 73
    • 0021908520 scopus 로고
    • Concepts of heme dissociation within hepatocytes
    • U. Muller-Eberhard, and S.H. Vincent Concepts of heme dissociation within hepatocytes Biochem. Pharm. 34 1985 719 725
    • (1985) Biochem. Pharm. , vol.34 , pp. 719-725
    • Muller-Eberhard, U.1    Vincent, S.H.2
  • 75
    • 0028900182 scopus 로고
    • Heme protein-mediated renal injury: A protective role for 21-aminosteroids in vitro and in vivo
    • K.A. Nath, J. Balla, A.J. Croatt, and G.M. Vercellotti Heme protein-mediated renal injury: a protective role for 21-aminosteroids in vitro and in vivo Kidney Int. 47 1995 592 602
    • (1995) Kidney Int. , vol.47 , pp. 592-602
    • Nath, K.A.1    Balla, J.2    Croatt, A.J.3    Vercellotti, G.M.4
  • 76
    • 0023689975 scopus 로고
    • Intra-hepatocellular site of the catabolism of heme and globin moiety of hemoglobin-haptoglobin after intravenous administration to rats
    • S. Oshiro, and H. Nakajima Intra-hepatocellular site of the catabolism of heme and globin moiety of hemoglobin-haptoglobin after intravenous administration to rats J. Biol. Chem. 63 1988 16032 16038
    • (1988) J. Biol. Chem. , vol.63 , pp. 16032-16038
    • Oshiro, S.1    Nakajima, H.2
  • 78
    • 0032972686 scopus 로고    scopus 로고
    • Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice
    • N. Panahian, M. Yoshiura, and M.D. Maines Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice J. Neurochem. 72 1999 1187 1203
    • (1999) J. Neurochem. , vol.72 , pp. 1187-1203
    • Panahian, N.1    Yoshiura, M.2    Maines, M.D.3
  • 79
    • 0347951196 scopus 로고    scopus 로고
    • Hemoglobin scavenger receptor CD163 mediates interleukin-10 release and heme oxygenase-1 synthesis: Anti-inflammatory monocyte-macrophase responses in vitro, in resolving skin blisters in vivo, and after cardiopulmonary bypass surgery
    • P. Philippidis, J.C. Mason, B.J. Evans, I. Nadra, K.M. Taylor, D.O. Haskard, and R.C. Landis Hemoglobin scavenger receptor CD163 mediates interleukin-10 release and heme oxygenase-1 synthesis: anti-inflammatory monocyte-macrophase responses in vitro, in resolving skin blisters in vivo, and after cardiopulmonary bypass surgery Circ. Res. 94 2004 119 126
    • (2004) Circ. Res. , vol.94 , pp. 119-126
    • Philippidis, P.1    Mason, J.C.2    Evans, B.J.3    Nadra, I.4    Taylor, K.M.5    Haskard, D.O.6    Landis, R.C.7
  • 80
    • 0142185379 scopus 로고    scopus 로고
    • Meat and cancer: Hemeoglobin and heme in a low-calcium diet promote colorectal carcinogenesis at the aberrant crypt stage in rats
    • F. Pierre, S. Tache, C.R. Petit, R. Van der Meer, and Corpet S D.E. Meat and cancer: hemeoglobin and heme in a low-calcium diet promote colorectal carcinogenesis at the aberrant crypt stage in rats Carcinogenesis 24 2003 1683 1690
    • (2003) Carcinogenesis , vol.24 , pp. 1683-1690
    • Pierre, F.1    Tache, S.2    Petit, C.R.3    Van Der Meer, R.4    Corpet, S.D.E.5
  • 81
    • 0032546922 scopus 로고    scopus 로고
    • Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells
    • V. Picard, S. Epsztejn, P. Santambrogio, Z.L. Cabantchik, and C. Beaumont Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells J. Biol. Chem. 273 1998 15382 15386
    • (1998) J. Biol. Chem. , vol.273 , pp. 15382-15386
    • Picard, V.1    Epsztejn, S.2    Santambrogio, P.3    Cabantchik, Z.L.4    Beaumont, C.5
  • 82
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • P. Ponka Cell biology of heme Am. J. Med. Sci. 318 1999 241 256
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 241-256
    • Ponka, P.1
  • 84
    • 0037055997 scopus 로고    scopus 로고
    • Ferritin induction protects cortical astrocytes from heme-mediated oxidative injury
    • R.F. Regan, N. Kumar, F. Gao, and Y. Guo Ferritin induction protects cortical astrocytes from heme-mediated oxidative injury Neuroscience 113 2002 985 994
    • (2002) Neuroscience , vol.113 , pp. 985-994
    • Regan, R.F.1    Kumar, N.2    Gao, F.3    Guo, Y.4
  • 86
    • 0141928185 scopus 로고    scopus 로고
    • Effects of exogenous heme on renal function: Role of heme oxygenase and cyclooxygenase
    • F. Rodriguez, R. Kemp, M. Balazy, and A. Nasjletti Effects of exogenous heme on renal function: role of heme oxygenase and cyclooxygenase Hypertension 42 2003 680 684
    • (2003) Hypertension , vol.42 , pp. 680-684
    • Rodriguez, F.1    Kemp, R.2    Balazy, M.3    Nasjletti, A.4
  • 87
    • 0000512791 scopus 로고
    • Methemalbumin, interaction between human serum albumin and ferriprotoporphyrin IX
    • M. Rosenfeld, and D.M. Surgenor Methemalbumin, interaction between human serum albumin and ferriprotoporphyrin IX J. Biol. Chem. 183 1950 663 677
    • (1950) J. Biol. Chem. , vol.183 , pp. 663-677
    • Rosenfeld, M.1    Surgenor, D.M.2
  • 88
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity: Heme oxygenase has both pro- and antioxidant properties
    • S.W. Ryter, and R.M. Tyrrell The heme synthesis and degradation pathways: role in oxidant sensitivity: heme oxygenase has both pro- and antioxidant properties Free Radic. Biol. Med. 28 2000 289 309
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 89
    • 0017289492 scopus 로고
    • Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells
    • S. Sassa Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells J. Exp. Med. 143 1976 305 315
    • (1976) J. Exp. Med. , vol.143 , pp. 305-315
    • Sassa, S.1
  • 90
    • 0027359301 scopus 로고
    • Hemin-induced lipid membrane disorder and increased permeability: A molecular model for the mechanism of cell lysis
    • T.H. Schmitt, A. Wilson, Frezzatti Jr., and S. Schreier Hemin-induced lipid membrane disorder and increased permeability: a molecular model for the mechanism of cell lysis Arch. Biochem. Biophys. 207 1993 96 103
    • (1993) Arch. Biochem. Biophys. , vol.207 , pp. 96-103
    • Schmitt, T.H.1    Wilson, A.2    Frezzatti, Jr.3    Schreier, S.4
  • 91
    • 0014713324 scopus 로고
    • Disposal of plasma heme in normal man and patients with intravascular hemolysis
    • D.A. Sears Disposal of plasma heme in normal man and patients with intravascular hemolysis J. Clin. Invest. 49 1970 5 14
    • (1970) J. Clin. Invest. , vol.49 , pp. 5-14
    • Sears, D.A.1
  • 92
    • 0030754401 scopus 로고    scopus 로고
    • COX-2, HO NO! Cyclooxygenase-2, heme oxygenase and nitric oxide synthase: Their role and interactions in inflammation
    • BIRAs Symposium, Saint Bartholomew's Hospital, London, April 26, 1996
    • Seed, M.P., Willoughby, D.A., 1997. COX-2, HO NO! Cyclooxygenase-2, heme oxygenase and nitric oxide synthase: their role and interactions in inflammation. BIRAs Symposium, Saint Bartholomew's Hospital, London, April 26, 1996, Inflamm. Res. 46, 279-281.
    • (1997) Inflamm. Res. , vol.46 , pp. 279-281
    • Seed, M.P.1    Willoughby, D.A.2
  • 94
    • 0030014964 scopus 로고    scopus 로고
    • Involvement of the transcription factor NF-kappa B in tubular morphogenesis of human microvascular endothelial cells by oxidative stress
    • T. Shono, M. Ono, H. Izumi, S.I. Jimi, K. Matsushima, T. Okamoto, K. Kohno, and M. Kuwano Involvement of the transcription factor NF-kappa B in tubular morphogenesis of human microvascular endothelial cells by oxidative stress Mol. Cell. Biol. 16 1996 4231 4239
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4231-4239
    • Shono, T.1    Ono, M.2    Izumi, H.3    Jimi, S.I.4    Matsushima, K.5    Okamoto, T.6    Kohno, K.7    Kuwano, M.8
  • 95
    • 0019877615 scopus 로고
    • Hemopexin-mediated transport of heme into isolated rat hepatocytes
    • A. Smith, and W.T. Morgan Hemopexin-mediated transport of heme into isolated rat hepatocytes J. Biol. Chem. 256 1981 10902 10909
    • (1981) J. Biol. Chem. , vol.256 , pp. 10902-10909
    • Smith, A.1    Morgan, W.T.2
  • 96
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • R. Stocker, Y. Yamamoto, A.F. McDonagh, A.N. Glazer, and B.N. Ames Bilirubin is an antioxidant of possible physiological importance Science 235 1987 1043 1046
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 97
    • 0025043651 scopus 로고
    • Hemin-promoted peroxidation of red cell cytoskeletal proteins
    • I. Solar, J. Dulitzky, and N. Shaklai Hemin-promoted peroxidation of red cell cytoskeletal proteins Arch. Biochem. Biophys. 283 1990 81 89
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 81-89
    • Solar, I.1    Dulitzky, J.2    Shaklai, N.3
  • 99
    • 0023221126 scopus 로고
    • Cell surface receptor for hemopexin in human leukemia HL60 cells
    • S. Taketani, H. Kohno, and R. Tokunaga Cell surface receptor for hemopexin in human leukemia HL60 cells J. Biol. Chem. 262 1987 4639 4643
    • (1987) J. Biol. Chem. , vol.262 , pp. 4639-4643
    • Taketani, S.1    Kohno, H.2    Tokunaga, R.3
  • 100
    • 0036670753 scopus 로고    scopus 로고
    • Making light of it: The role of plant haem oxygenases in phytochrome chromophore synthesis
    • M.J. Terry, P.J. Linley, and T. Kohchi Making light of it: the role of plant haem oxygenases in phytochrome chromophore synthesis Biochem. Soc. Trans. 30 2002 604 609
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 604-609
    • Terry, M.J.1    Linley, P.J.2    Kohchi, T.3
  • 101
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase characterization of the enzyme
    • R. Tenhunen, H.S. Marver, and R. Schmid Microsomal heme oxygenase characterization of the enzyme J. Biol. Chem. 244 1969 6388 6394
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 102
  • 104
    • 0036182512 scopus 로고    scopus 로고
    • Potential involvement of hemoglobin and heme in the pathogenesis of peritoneal endometriosis
    • A.V. Van Langendonckt, F. Casanas-Roux, M.M. Dolmans, and J. Donnez Potential involvement of hemoglobin and heme in the pathogenesis of peritoneal endometriosis Fertil. Steril. 77 2002 561 570
    • (2002) Fertil. Steril. , vol.77 , pp. 561-570
    • Van Langendonckt, A.V.1    Casanas-Roux, F.2    Dolmans, M.M.3    Donnez, J.4
  • 105
    • 0020509898 scopus 로고
    • Growth-promoting effects of iron- and cobalt-protoporphyrins on cultured embryonic cells
    • C. Verger, S. Sassa, and A. Kappas Growth-promoting effects of iron- and cobalt-protoporphyrins on cultured embryonic cells J. Cell. Phys. 116 1983 135 141
    • (1983) J. Cell. Phys. , vol.116 , pp. 135-141
    • Verger, C.1    Sassa, S.2    Kappas, A.3
  • 106
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • G.F. Vile, S. Basu-Modak, C. Waltner, and R.M. Tyrrel Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts Proc. Natl. Acad. Sci. U.S.A. 91 1994 2607 2610
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrel, R.M.4
  • 108
    • 0024574001 scopus 로고
    • Oxidative effects of heme and porphyrins on proteins and lipids
    • S.H. Vincent Oxidative effects of heme and porphyrins on proteins and lipids Semin. Hematol. 26 1989 105 113
    • (1989) Semin. Hematol. , vol.26 , pp. 105-113
    • Vincent, S.H.1
  • 109
    • 2942542718 scopus 로고    scopus 로고
    • Haptoglobin polymorphisms and iron homeostasis in health and in disease
    • H.V. Vlierberghe, M. Langlois, and J. Delanghe Haptoglobin polymorphisms and iron homeostasis in health and in disease Clin. Chim. 345 2004 35 42
    • (2004) Clin. Chim. , vol.345 , pp. 35-42
    • Vlierberghe, H.V.1    Langlois, M.2    Delanghe, J.3
  • 111
    • 0030734872 scopus 로고    scopus 로고
    • Heme induces the expression of adhesion molecules ICAM-1: VCAM-1 and E-selectin in vascular endothelial cells
    • F.A.D.T.G. Wagener, E. Feldman, T. de Witte, and N.G. Abraham Heme induces the expression of adhesion molecules ICAM-1: VCAM-1 and E-selectin in vascular endothelial cells Proc. Soc. Exp. Biol. Med. 216 1997 456 463
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.216 , pp. 456-463
    • Wagener, F.A.D.T.G.1    Feldman, E.2    De Witte, T.3    Abraham, N.G.4
  • 114
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • D. Willis, A.R. Moore, R. Frederick, and D.A. Willoughby Heme oxygenase: a novel target for the modulation of the inflammatory response Nat. Med. 2 1996 87 90
    • (1996) Nat. Med. , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4
  • 115
    • 0021132163 scopus 로고
    • Features of intermediary steps around the 688 nm substances in the heme oxygenase reaction
    • T. Yoshida, and M. Noguchi Features of intermediary steps around the 688 nm substances in the heme oxygenase reaction J. Biochem. (Tokyo) 96 1984 563 570
    • (1984) J. Biochem. (Tokyo) , vol.96 , pp. 563-570
    • Yoshida, T.1    Noguchi, M.2


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