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Volumn 1620, Issue 1-3, 2003, Pages 211-217

Hydrogen-peroxide-induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase

Author keywords

Catalase; Fluorescence; Glutathione peroxidase; Heme degradation; Hydrogen peroxide; Red blood cell

Indexed keywords

CATALASE; GLUTATHIONE PEROXIDASE; HEME; HEMOGLOBIN; HYDROGEN PEROXIDE; IODOACETAMIDE;

EID: 3242735024     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00537-8     Document Type: Article
Times cited : (168)

References (39)
  • 2
    • 0023943252 scopus 로고
    • Senescence of red blood cells: Progress and problems
    • Clark M.R. Senescence of red blood cells: progress and problems. Physiol. Rev. 68:1988;503-554.
    • (1988) Physiol. Rev. , vol.68 , pp. 503-554
    • Clark, M.R.1
  • 3
    • 0027566866 scopus 로고
    • Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen
    • Kay K.M. Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen. Cell. Mol. Biol. 39:1993;131-153.
    • (1993) Cell. Mol. Biol. , vol.39 , pp. 131-153
    • Kay, K.M.1
  • 4
    • 0026036015 scopus 로고
    • Erythrocyte aging: Physical and chemical membrane changes
    • Bartosz G. Erythrocyte aging: physical and chemical membrane changes. Gerontology. 37:1991;33-67.
    • (1991) Gerontology , vol.37 , pp. 33-67
    • Bartosz, G.1
  • 5
    • 0025060810 scopus 로고
    • Oxidative denaturation of red blood cells in thalassemia
    • Shinar E., Rachmilewitz E.A. Oxidative denaturation of red blood cells in thalassemia. Semin. Hematol. 27:1990;70-82.
    • (1990) Semin. Hematol. , vol.27 , pp. 70-82
    • Shinar, E.1    Rachmilewitz, E.A.2
  • 6
    • 0015502066 scopus 로고
    • The generation of superoxide radical during autoxidation of hemoglobin
    • Misra H.P., Fridovich I. The generation of superoxide radical during autoxidation of hemoglobin. J. Biol. Chem. 247:1972;6960-6962.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 7
    • 33947476438 scopus 로고
    • Glutathione peroxidase: The primary agent for the elimination of hydrogen peroxide in erythrocytes
    • Cohen G., Hochstein P. Glutathione peroxidase: the primary agent for the elimination of hydrogen peroxide in erythrocytes. Biochemistry. 2:1963;1420-1428.
    • (1963) Biochemistry , vol.2 , pp. 1420-1428
    • Cohen, G.1    Hochstein, P.2
  • 9
    • 0030022388 scopus 로고    scopus 로고
    • Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
    • Gaetani G.F., Ferraris A.M., Rolfo M., Mangerini R., Arena S., Kirkman H.N. Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood. 87:1996;1595-1599.
    • (1996) Blood , vol.87 , pp. 1595-1599
    • Gaetani, G.F.1    Ferraris, A.M.2    Rolfo, M.3    Mangerini, R.4    Arena, S.5    Kirkman, H.N.6
  • 10
    • 0031441273 scopus 로고    scopus 로고
    • Direct evidence for catalase as the predominant hydrogen peroxide removing enzyme in human erythrocytes
    • Mueller S., Riedal H.D., Stremmel W. Direct evidence for catalase as the predominant hydrogen peroxide removing enzyme in human erythrocytes. Blood. 90:1997;4973-4978.
    • (1997) Blood , vol.90 , pp. 4973-4978
    • Mueller, S.1    Riedal, H.D.2    Stremmel, W.3
  • 11
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during oxidation of hemoglobin by hydrogen peroxide
    • Nagababu E., Rifkind J.M. Formation of fluorescent heme degradation products during oxidation of hemoglobin by hydrogen peroxide. Biochem. Biophys. Res. Commun. 247:1998;592-596.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 12
    • 0034647775 scopus 로고    scopus 로고
    • Heme degradation during autoxidation of oxyhemoglobin
    • Nagababu E., Rifkind J.M. Heme degradation during autoxidation of oxyhemoglobin. Biochem. Biophys. Res. Commun. 273:2000;839-845.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 839-845
    • Nagababu, E.1    Rifkind, J.M.2
  • 13
    • 0033797642 scopus 로고    scopus 로고
    • The origin of red cell fluorescence caused by hydrogen peroxide treatment
    • Nagababu E., Chrest F.J., Rifkind J.M. The origin of red cell fluorescence caused by hydrogen peroxide treatment. Free Radic. Biol. Med. 29:2000;659-663.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 659-663
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 14
    • 0003946353 scopus 로고
    • Red cell metabolism
    • New York: Grune and Stratton Inc.
    • Beutler E. Red cell metabolism. A Manual of Biochemical Methods. 3rd ed. 1984;103-105 Grune and Stratton Inc. New York.
    • (1984) A Manual of Biochemical Methods 3rd ed. , pp. 103-105
    • Beutler, E.1
  • 15
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Methods Enzymol. 105:1984;121-126.
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 16
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin oxidative break down
    • Mills G.C. Hemoglobin catabolism. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin oxidative break down. J. Biol. Chem. 229:1957;189-197.
    • (1957) J. Biol. Chem. , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 17
    • 0028261076 scopus 로고
    • Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes
    • Gaetani G.F., Kirkman H.N., Mangerini R., Ferraris A.M. Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood. 84:1994;325-330.
    • (1994) Blood , vol.84 , pp. 325-330
    • Gaetani, G.F.1    Kirkman, H.N.2    Mangerini, R.3    Ferraris, A.M.4
  • 18
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Ho Y.S., Magnenat J., Bronson R.T., Cao J., Gargano M., Sugawara N., Funk C.D. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem. 272:1997;16644-16651.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16644-16651
    • Ho, Y.S.1    Magnenat, J.2    Bronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, N.6    Funk, C.D.7
  • 19
    • 0034284002 scopus 로고    scopus 로고
    • Red cells from glutathione peroxidase-1 deficient mice have nearly normal defenses against exogenous peroxides
    • Johnson R.M., Goyette G. Jr., Ravindranath Y., Ho Y.S. Red cells from glutathione peroxidase-1 deficient mice have nearly normal defenses against exogenous peroxides. Blood. 96:2000;1985-1988.
    • (2000) Blood , vol.96 , pp. 1985-1988
    • Johnson, R.M.1    Goyette G., Jr.2    Ravindranath, Y.3    Ho, Y.S.4
  • 21
    • 0025761870 scopus 로고
    • Glutathione peroxidase deficiency and childhood seizures
    • Weber G.F., Maertens P., Meng X.Z., Pippenger C.E. Glutathione peroxidase deficiency and childhood seizures. Lancet. 337:1991;1443-1444.
    • (1991) Lancet , vol.337 , pp. 1443-1444
    • Weber, G.F.1    Maertens, P.2    Meng, X.Z.3    Pippenger, C.E.4
  • 23
    • 0028833848 scopus 로고
    • Hungarian hereditary acatalasemia and hypocatalasemia are not associated with chronic hemolysis
    • Goth L., Vitai M. Hungarian hereditary acatalasemia and hypocatalasemia are not associated with chronic hemolysis. Clin. Chim. Acta. 233:1995;75-79.
    • (1995) Clin. Chim. Acta , vol.233 , pp. 75-79
    • Goth, L.1    Vitai, M.2
  • 24
    • 0037103291 scopus 로고    scopus 로고
    • Oxidation of glutathione peroxidase-deficient red cells by organic peroxides
    • Johnson R.M., Goyette G. Jr., Ravindranath Y., Ho Y.S. Oxidation of glutathione peroxidase-deficient red cells by organic peroxides. Blood. 100:2002;1515-1516.
    • (2002) Blood , vol.100 , pp. 1515-1516
    • Johnson, R.M.1    Goyette G., Jr.2    Ravindranath, Y.3    Ho, Y.S.4
  • 25
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: Superoxide production and heme degradation
    • Nagababu E., Rifkind J.M. Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry. 39:2000;12503-12511.
    • (2000) Biochemistry , vol.39 , pp. 12503-12511
    • Nagababu, E.1    Rifkind, J.M.2
  • 26
    • 0028828562 scopus 로고
    • Heme degradation in the presence of glutathione
    • Atamna H., Ginsburg H. 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    Ginsburg, H.2
  • 27
    • 0023176273 scopus 로고
    • Lipid peroxidation and mechanism of toxicity
    • Horton A.A., Fairhurst S. Lipid peroxidation and mechanism of toxicity. Crit. Rev. Toxicol. 18:1987;27-79.
    • (1987) Crit. Rev. Toxicol. , vol.18 , pp. 27-79
    • Horton, A.A.1    Fairhurst, S.2
  • 28
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn H.F., Jandl J.H. Exchange of heme among hemoglobins and between hemoglobin and albumin. J. Biol. Chem. 243:1968;465-475.
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 29
    • 0037047013 scopus 로고    scopus 로고
    • Binding of hemoglobin to red cell membranes with eosin-5-maleimide labeled band-3: Analysis of centrifugation and fluorescence data
    • Demehin A.A., Abugo O.O., Jayakumar R., Lakowicz J.R., Rifkind J.M. Binding of hemoglobin to red cell membranes with eosin-5-maleimide labeled band-3: analysis of centrifugation and fluorescence data. Biochemistry. 41:2002;8630-8637.
    • (2002) Biochemistry , vol.41 , pp. 8630-8637
    • Demehin, A.A.1    Abugo, O.O.2    Jayakumar, R.3    Lakowicz, J.R.4    Rifkind, J.M.5
  • 30
    • 84907037913 scopus 로고
    • The hypoxic stress on erythrocytes associated with superoxide formation
    • Rifkind J.M., Zhang L., Levy A., Manoharan P.T. The hypoxic stress on erythrocytes associated with superoxide formation. Free Radic. Res. Commun. 12-13:1991;645-652.
    • (1991) Free Radic. Res. Commun. , vol.12-13 , pp. 645-652
    • Rifkind, J.M.1    Zhang, L.2    Levy, A.3    Manoharan, P.T.4
  • 31
    • 0034926240 scopus 로고    scopus 로고
    • The reduction of nitroblue tetrazolium by red blood cells: A measure of red blood cell membrane antioxidant capacity and hemoglobin-membrane binding sites
    • Demehin A.A., Abugo O.O., Rifkind J.M. The reduction of nitroblue tetrazolium by red blood cells: a measure of red blood cell membrane antioxidant capacity and hemoglobin-membrane binding sites. Free Radic. Res. 34:2001;605-620.
    • (2001) Free Radic. Res. , vol.34 , pp. 605-620
    • Demehin, A.A.1    Abugo, O.O.2    Rifkind, J.M.3
  • 32
    • 0001488065 scopus 로고
    • Formation of free radicals under hypoxia
    • P.W. Hochachka, P.L. Lutz, T. Sick, M. Rosenthal, & G. van den Thillart. Boca Raton, FL: CRC Press
    • Rifkind J.M., Abugo O.O., Levy A., Monticone R., Heim J. Formation of free radicals under hypoxia. Hochachka P.W., Lutz P.L., Sick T., Rosenthal M., van den Thillart G. Surviving Hypoxia: Mechanism of Control and Adaptation. 1993;509-525 CRC Press, Boca Raton, FL.
    • (1993) Surviving Hypoxia: Mechanism of Control and Adaptation , pp. 509-525
    • Rifkind, J.M.1    Abugo, O.O.2    Levy, A.3    Monticone, R.4    Heim, J.5
  • 35
    • 0028796836 scopus 로고
    • Oxidation state of glutathione and membrane proteins in human red cells of different age
    • Piccinini G., Minetti G., Baluini C., Brovelli A. Oxidation state of glutathione and membrane proteins in human red cells of different age. Mech. Ageing Dev. 78:1995;15-26.
    • (1995) Mech. Ageing Dev. , vol.78 , pp. 15-26
    • Piccinini, G.1    Minetti, G.2    Baluini, C.3    Brovelli, A.4
  • 36
    • 0035114063 scopus 로고    scopus 로고
    • Alterations of antioxidant enzymes and oxidative stress markers in aging
    • Kasapoglu M., Ozben T. Alterations of antioxidant enzymes and oxidative stress markers in aging. Exp. Gerontol. 36:2001;209-220.
    • (2001) Exp. Gerontol. , vol.36 , pp. 209-220
    • Kasapoglu, M.1    Ozben, T.2
  • 38
    • 0025061081 scopus 로고
    • The sickle erythrocyte in double jeopardy: Autoxidation and iron decompartmentalization
    • Hebbel R.P. The sickle erythrocyte in double jeopardy: autoxidation and iron decompartmentalization. Semin. Hematol. 27:1990;51-69.
    • (1990) Semin. Hematol. , vol.27 , pp. 51-69
    • Hebbel, R.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.