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Volumn 87, Issue 9, 1996, Pages 3948-3952

Catalysis of soluble hemoglobin oxidation by free iron on sickle red cell membranes

Author keywords

[No Author keywords available]

Indexed keywords

CHELATING AGENT; DEFERIPRONE; FERRIC ION; HEME; HEMOGLOBIN; HEMOGLOBIN S; HEMOPROTEIN; IRON; METHEMOGLOBIN; OXYHEMOGLOBIN;

EID: 0029913286     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v87.9.3948.bloodjournal8793948     Document Type: Article
Times cited : (27)

References (24)
  • 1
    • 0002426265 scopus 로고
    • Membrane associated iron
    • Embury SH, Hebbel RP, Mohandas N, Steinberg MH (eds): New York, Raven Press
    • Hebbel RP: Membrane associated iron, in Embury SH, Hebbel RP, Mohandas N, Steinberg MH (eds): Sickle Cell Disease: Basic Principles and Clinical Practice. New York, Raven Press, 1994, p 163
    • (1994) Sickle Cell Disease: Basic Principles and Clinical Practice , pp. 163
    • Hebbel, R.P.1
  • 2
    • 0022549289 scopus 로고
    • Regulation of erythrocyte cation and water content in sickle cell anemia
    • Brugnara C, Bunn HF, Tosteson DC: Regulation of erythrocyte cation and water content in sickle cell anemia. Science 232:388, 1986
    • (1986) Science , vol.232 , pp. 388
    • Brugnara, C.1    Bunn, H.F.2    Tosteson, D.C.3
  • 3
    • 0026795491 scopus 로고
    • Exaggerated cation leak from oxygenated sickle red blood cells during deformation: Evidence for a unique leak pathway
    • Sugihara T, Hebbel RP: Exaggerated cation leak from oxygenated sickle red blood cells during deformation: Evidence for a unique leak pathway. Blood 80:2374, 1992
    • (1992) Blood , vol.80 , pp. 2374
    • Sugihara, T.1    Hebbel, R.P.2
  • 4
    • 0023718258 scopus 로고
    • Vesiculation of sickle erythrocytes during thermal stress
    • Rank BH, Moyer NL, Hebbel RP: Vesiculation of sickle erythrocytes during thermal stress. Blood 72:1060, 1988
    • (1988) Blood , vol.72 , pp. 1060
    • Rank, B.H.1    Moyer, N.L.2    Hebbel, R.P.3
  • 5
    • 0024989557 scopus 로고
    • Oxidation-induced changes in microrheologic properties of the red blood cell membrane
    • Hebbel RP, Leung A, Mohandas N: Oxidation-induced changes in microrheologic properties of the red blood cell membrane. Blood 76:1015, 1990
    • (1990) Blood , vol.76 , pp. 1015
    • Hebbel, R.P.1    Leung, A.2    Mohandas, N.3
  • 6
    • 0021969804 scopus 로고
    • The role of hemoglobin denaturation and band 3 clustering in red blood cell aging
    • Low PS, Waugh SM, Zinke K, Drenckhahn D: The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227:531, 1985
    • (1985) Science , vol.227 , pp. 531
    • Low, P.S.1    Waugh, S.M.2    Zinke, K.3    Drenckhahn, D.4
  • 7
    • 0022993811 scopus 로고
    • Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes
    • Waugh SM, Willardson BM, Kannan R, Labotka RJ, Low PS: Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes. J Clin Invest 78:1155, 1986
    • (1986) J Clin Invest , vol.78 , pp. 1155
    • Waugh, S.M.1    Willardson, B.M.2    Kannan, R.3    Labotka, R.J.4    Low, P.S.5
  • 8
    • 0041524601 scopus 로고
    • Co-clustering of denatured hemoglobin with band 3: Its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes
    • Schlüter K, Drenckhahn D: Co-clustering of denatured hemoglobin with band 3: Its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proc Natl Acad Sci USA 83:6137, 1986
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6137
    • Schlüter, K.1    Drenckhahn, D.2
  • 9
    • 0026343738 scopus 로고
    • Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis
    • Turrini F, Arese P, Yuan J, Low PS: Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis. J Biol Chem 266:23611, 1991
    • (1991) J Biol Chem , vol.266 , pp. 23611
    • Turrini, F.1    Arese, P.2    Yuan, J.3    Low, P.S.4
  • 10
    • 4244087400 scopus 로고
    • Pathogenesis of hemolytic anemia
    • Embury SH, Hebbel RP, Mohandas N, Steinberg MH (eds): New York, Raven Press
    • Mohandas N, Hebbel RP: Pathogenesis of hemolytic anemia, in Embury SH, Hebbel RP, Mohandas N, Steinberg MH (eds): Sickle Cell Disease: Basic Principles and Clinical Practice. New York, Raven Press, 1994, p 327
    • (1994) Sickle Cell Disease: Basic Principles and Clinical Practice , pp. 327
    • Mohandas, N.1    Hebbel, R.P.2
  • 11
    • 0008239743 scopus 로고
    • Accelerated auto-oxidation and heme loss due to instability of sickle hemoglobin
    • Hebbel RP, Morgan WT, Eaton JW, Hedlund BE: Accelerated auto-oxidation and heme loss due to instability of sickle hemoglobin. Proc Natl Acad Sci USA 85:237, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 237
    • Hebbel, R.P.1    Morgan, W.T.2    Eaton, J.W.3    Hedlund, B.E.4
  • 12
    • 0028031991 scopus 로고
    • Denaturing interaction between sickle hemoglobin and phosphatidylserine liposomes
    • Marva E, Hebbel RP: Denaturing interaction between sickle hemoglobin and phosphatidylserine liposomes. Blood 83:242, 1994
    • (1994) Blood , vol.83 , pp. 242
    • Marva, E.1    Hebbel, R.P.2
  • 13
    • 0021702455 scopus 로고
    • The aerobic reduction of Fe(III) complexes by hemoglobin and myoglobin
    • Eguchi LA, Saltman P: The aerobic reduction of Fe(III) complexes by hemoglobin and myoglobin. J Biol Chem 259:14337, 1984
    • (1984) J Biol Chem , vol.259 , pp. 14337
    • Eguchi, L.A.1    Saltman, P.2
  • 14
    • 0005664743 scopus 로고
    • Kinetics and mechanisms of metal reduction by hemoglobin. 1. Reduction of iron(in) complexes
    • Eguchi LA, Saltman P: Kinetics and mechanisms of metal reduction by hemoglobin. 1. Reduction of iron(in) complexes. Inorg Chem 26:3665, 1987
    • (1987) Inorg Chem , vol.26 , pp. 3665
    • Eguchi, L.A.1    Saltman, P.2
  • 15
    • 0023781675 scopus 로고
    • Nonheme iron in sickle erythrocyte membranes: Association with phospholipids and potential role in lipid peroxidation
    • Kuross SA, Hebbel RP: Nonheme iron in sickle erythrocyte membranes: Association with phospholipids and potential role in lipid peroxidation Blood 72:1278, 1988
    • (1988) Blood , vol.72 , pp. 1278
    • Kuross, S.A.1    Hebbel, R.P.2
  • 17
    • 15844385361 scopus 로고
    • The nature of membrane-bound iron-species involved in radical-mediated damage to sickle erythrocytes
    • Hartley A, Rice-Evans C: The nature of membrane-bound iron-species involved in radical-mediated damage to sickle erythrocytes. Biochem Soc Trans 17:488, 1989
    • (1989) Biochem Soc Trans , vol.17 , pp. 488
    • Hartley, A.1    Rice-Evans, C.2
  • 19
    • 0025749683 scopus 로고
    • Hydroxyl radical formation by sickle erythrocyte membranes: Role of pathologic iron deposits and cytoplasmic reducing agents
    • Repka T, Hebbel RP: Hydroxyl radical formation by sickle erythrocyte membranes: Role of pathologic iron deposits and cytoplasmic reducing agents. Blood 78:2753, 1991
    • (1991) Blood , vol.78 , pp. 2753
    • Repka, T.1    Hebbel, R.P.2
  • 20
    • 0029097965 scopus 로고
    • Deferiprone (L1) chelates pathologic iron deposits from membranes of intact thalassemic and sickle RBC both in vitro and in vivo
    • Shalev O, Repka T, Goldfarb A, Grinberg L, Abrahamov A, Olivieri NF, Rachmilewitz EA, Hebbel RP: Deferiprone (L1) chelates pathologic iron deposits from membranes of intact thalassemic and sickle RBC both in vitro and in vivo. Blood 86:2008, 1995
    • (1995) Blood , vol.86 , pp. 2008
    • Shalev, O.1    Repka, T.2    Goldfarb, A.3    Grinberg, L.4    Abrahamov, A.5    Olivieri, N.F.6    Rachmilewitz, E.A.7    Hebbel, R.P.8
  • 21
    • 85052776694 scopus 로고
    • Reactions of superoxide with hemoglobin
    • Greenwald RA (ed): Boca Raton, CRC Press
    • Winterboum CC: Reactions of superoxide with hemoglobin, in Greenwald RA (ed): CRC Handbook of Methods for Oxygen Radical Research. Boca Raton, CRC Press, 1985, p 137
    • (1985) CRC Handbook of Methods for Oxygen Radical Research , pp. 137
    • Winterboum, C.C.1
  • 22
    • 0023937376 scopus 로고
    • Excess heme in sickle erythrocyte inside-out membranes: Possible role in thiol oxidation
    • Kuross SA, Rank BH, Hebbel RP: Excess heme in sickle erythrocyte inside-out membranes: Possible role in thiol oxidation. Blood 71:876, 1988
    • (1988) Blood , vol.71 , pp. 876
    • Kuross, S.A.1    Rank, B.H.2    Hebbel, R.P.3
  • 23
    • 0029982812 scopus 로고    scopus 로고
    • Extremely high avidity association of fe(III) with the sickle red cell membrane
    • in press
    • Shalev O, Hebbel RP: Extremely high avidity association of fe(III) with the sickle red cell membrane. Blood 1996 (in press)
    • (1996) Blood
    • Shalev, O.1    Hebbel, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.