메뉴 건너뛰기




Volumn 100, Issue 6, 1997, Pages 1459-1464

Removal of erythrocyte membrane iron in vivo ameliorates the pathobiology of murine thalassemia

Author keywords

Chelation; Iron; Membrane; Red blood cell; Thalassemia

Indexed keywords

DEFERIPRONE; GLOBIN; HEMOGLOBIN; IMMUNOGLOBULIN; IRON; MEMBRANE PROTEIN; POTASSIUM;

EID: 0030822467     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119666     Document Type: Article
Times cited : (38)

References (29)
  • 1
    • 0025060810 scopus 로고
    • Oxidative denaturation of red blood cells in thalassemia
    • Shinar, E., and E.A. Rachmilewitz. 1990. Oxidative denaturation of red blood cells in thalassemia. Semin. Hematol. 27:70-82.
    • (1990) Semin. Hematol. , vol.27 , pp. 70-82
    • Shinar, E.1    Rachmilewitz, E.A.2
  • 4
    • 0026597441 scopus 로고
    • Oxidative red blood cell membrane injury in the pathophysiology of severe mouse β-thalassemia
    • Advani, R., E. Rubin, N. Mohandas, and S.L. Schrier. 1992. Oxidative red blood cell membrane injury in the pathophysiology of severe mouse β-thalassemia. Blood. 79:1064-1067.
    • (1992) Blood , vol.79 , pp. 1064-1067
    • Advani, R.1    Rubin, E.2    Mohandas, N.3    Schrier, S.L.4
  • 6
    • 0023781675 scopus 로고
    • Nonheme iron in sickle erythrocyte membranes: Association with phospholipids and potential role in lipid peroxidation
    • Kuross, S.A., and R.P. Hebbel. 1988. Nonheme iron in sickle erythrocyte membranes: Association with phospholipids and potential role in lipid peroxidation. Blood. 72:1278-1285.
    • (1988) Blood , vol.72 , pp. 1278-1285
    • Kuross, S.A.1    Hebbel, R.P.2
  • 7
    • 0025749683 scopus 로고
    • Hydroxyl radical formation by sickle erythrocyte membranes: Role of pathologic iron deposits and cytoplasmic reducing agents
    • Repka, T., and R.P. Hebbel. 1991. Hydroxyl radical formation by sickle erythrocyte membranes: role of pathologic iron deposits and cytoplasmic reducing agents. Blood. 78:2753-2758.
    • (1991) Blood , vol.78 , pp. 2753-2758
    • Repka, T.1    Hebbel, R.P.2
  • 8
    • 0025061081 scopus 로고
    • The sickle erythrocyte in double jeopardy: Autoxidation and iron decompartmentalization
    • Hebbel, R.P. 1990. The sickle erythrocyte in double jeopardy: autoxidation and iron decompartmentalization. Semin. Hematol. 27:51-69.
    • (1990) Semin. Hematol. , vol.27 , pp. 51-69
    • Hebbel, R.P.1
  • 10
    • 0000234906 scopus 로고
    • Structure/red blood cell permeability, activity of iron(III) chelator complexes
    • Kontoghiorghes, G.J. 1988. Structure/red blood cell permeability, activity of iron(III) chelator complexes. Inorganic Chimica Acta. 151:101-106.
    • (1988) Inorganic Chimica Acta , vol.151 , pp. 101-106
    • Kontoghiorghes, G.J.1
  • 11
    • 0029097965 scopus 로고
    • Deferiprone (L1) chelates pathologic iron deposits from membranes of intact thalassemic and sickle red blood cells both in vitro and in vivo
    • Shalev, O., T. Repka, A. Goldfarb, L. Grinberg, A. Abrahamov, N.F. Olivieri, E.A. Rachmilewitz, and R.P. Hebbel. 1995. Deferiprone (L1) chelates pathologic iron deposits from membranes of intact thalassemic and sickle red blood cells both in vitro and in vivo. Blood. 86:2008-2013.
    • (1995) Blood , vol.86 , pp. 2008-2013
    • 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
  • 14
    • 0028925757 scopus 로고
    • Cation transport in mouse erythrocytes: Role of K+/Cl- cotransport in regulatory volume decrease
    • Armsby, C.C., C. Brugnara, and S.L. Alper. 1995. Cation transport in mouse erythrocytes: Role of K+/Cl-cotransport in regulatory volume decrease. Am. J. Physiol (Cell Physiol. 37) 268:C894-C902.
    • (1995) Am. J. Physiol (Cell Physiol. 37) , vol.268
    • Armsby, C.C.1    Brugnara, C.2    Alper, S.L.3
  • 15
    • 0023937376 scopus 로고
    • Excess heme in sickle erythrocyte inside-out membranes: Possible role in thiol oxidation
    • Kuross, S., B.H. Rank, and R.P. Hebbel. 1988. Excess heme in sickle erythrocyte inside-out membranes: Possible role in thiol oxidation. Blood. 71: 876-882.
    • (1988) Blood , vol.71 , pp. 876-882
    • Kuross, S.1    Rank, B.H.2    Hebbel, R.P.3
  • 16
    • 0021799078 scopus 로고
    • Abnormal redox status of membrane-protein thiols in sickle erythrocytes
    • Rank, B., J. Carlsson, and R.P. Hebbel. 1985. Abnormal redox status of membrane-protein thiols in sickle erythrocytes. J. Clin. Invest. 75:1531-1537.
    • (1985) J. Clin. Invest. , vol.75 , pp. 1531-1537
    • Rank, B.1    Carlsson, J.2    Hebbel, R.P.3
  • 18
    • 0020530019 scopus 로고
    • Osmotic gradient ektacytometry: Comprehensive characterization of red cell volume and surface maintenance
    • Clark, M.R., N. Mohandas, and S. Shohet. 1983. Osmotic gradient ektacytometry: comprehensive characterization of red cell volume and surface maintenance. Blood. 61:899-910.
    • (1983) Blood , vol.61 , pp. 899-910
    • Clark, M.R.1    Mohandas, N.2    Shohet, S.3
  • 19
    • 0024560085 scopus 로고
    • Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia
    • Shinar, E., E.A. Rachmilewitz, and S.E. Lux. 1989. Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia. J. Clin. Invest. 83:404-410.
    • (1989) J. Clin. Invest. , vol.83 , pp. 404-410
    • Shinar, E.1    Rachmilewitz, E.A.2    Lux, S.E.3
  • 20
  • 21
    • 0025224874 scopus 로고
    • Mouse β thalassemia, a model for the membrane defects of erythrocytes in the human disease
    • Rouyer-Fessard, P., K. Leroy-Viard, C. Domenget, A. Mrad, and Y. Beuzard. 1990. Mouse β thalassemia, a model for the membrane defects of erythrocytes in the human disease. J. Biol. Chem. 265:20247-20251.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20247-20251
    • Rouyer-Fessard, P.1    Leroy-Viard, K.2    Domenget, C.3    Mrad, A.4    Beuzard, Y.5
  • 22
    • 0026512776 scopus 로고
    • Characterization and comparison of the red blood cell membrane damage in severe human α- and β-thalassemia
    • Advani, R., S. Sorenson, E. Shinar, W. Lande, E. Rachmilewitz, and S.L. Schrier. 1992. Characterization and comparison of the red blood cell membrane damage in severe human α-and β-thalassemia. Blood. 79:1058-1063.
    • (1992) Blood , vol.79 , pp. 1058-1063
    • Advani, R.1    Sorenson, S.2    Shinar, E.3    Lande, W.4    Rachmilewitz, E.5    Schrier, S.L.6
  • 23
    • 0024434530 scopus 로고
    • Cellular and membrane properties of alpha and beta thalassemic erythrocytes are different: Implication for differences in clinical manifestations
    • Schrier, S., E. Rachmilewitz, and N. Mohandas. 1989. Cellular and membrane properties of alpha and beta thalassemic erythrocytes are different: implication for differences in clinical manifestations. Blood. 74:2194-2202.
    • (1989) Blood , vol.74 , pp. 2194-2202
    • Schrier, S.1    Rachmilewitz, E.2    Mohandas, N.3
  • 24
    • 4243714868 scopus 로고    scopus 로고
    • Deferiprone (L1) treatment removes erythrocyte membrane free iron and affects K-Cl cotransport activity in homozygous β thalassemia
    • De Franceschi, L., O. Shalev, A. Piga, M. Collell, O. Olivieri, R. Corrocher, R.P. Hebbel, N. Olivieri, and C. Brugnara. 1996. Deferiprone (L1) treatment removes erythrocyte membrane free iron and affects K-Cl cotransport activity in homozygous β thalassemia. Blood. 88 (Suppl.):24b.
    • (1996) Blood , vol.88 , Issue.SUPPL.
    • De Franceschi, L.1    Shalev, O.2    Piga, A.3    Collell, M.4    Olivieri, O.5    Corrocher, R.6    Hebbel, R.P.7    Olivieri, N.8    Brugnara, C.9
  • 25
    • 0026704541 scopus 로고
    • Isolation, characterization, and immunuprecipitation studies of immune complexes from membranes of β-thalassemic erythrocytes
    • Yuan, J., R. Kannan, E. Shinar, E.A. Rachmilewitz, and P.S. Low. 1992. Isolation, characterization, and immunuprecipitation studies of immune complexes from membranes of β-thalassemic erythrocytes. Blood. 79:3007-3013.
    • (1992) Blood , vol.79 , pp. 3007-3013
    • Yuan, J.1    Kannan, R.2    Shinar, E.3    Rachmilewitz, E.A.4    Low, P.S.5
  • 26
    • 0029913286 scopus 로고    scopus 로고
    • Catalysis of soluble hemoglobin oxidation by free iron on sickle red cell membranes
    • Shalev, O., and R.P. Hebbel. 1996. Catalysis of soluble hemoglobin oxidation by free iron on sickle red cell membranes. Blood. 87:3948-3952.
    • (1996) Blood , vol.87 , pp. 3948-3952
    • Shalev, O.1    Hebbel, R.P.2
  • 27
    • 0024418244 scopus 로고
    • The redox state of cysteines 201 and 317 of the erythrocyte anion exchanger is critical for ankyrin binding
    • Thevenin, B.J.-M., B.M. Willardson, and P.S. Low. 1989. The redox state of cysteines 201 and 317 of the erythrocyte anion exchanger is critical for ankyrin binding. J. Biol. Chem. 264:15886-15892.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15886-15892
    • Thevenin, B.J.-M.1    Willardson, B.M.2    Low, P.S.3
  • 28
    • 0030058376 scopus 로고    scopus 로고
    • Long-term therapy with deferiprone
    • Olivieri, N. 1996. Long-term therapy with deferiprone. Acta Haematologica. 95:37-48.
    • (1996) Acta Haematologica , vol.95 , pp. 37-48
    • Olivieri, N.1
  • 29
    • 0026099699 scopus 로고
    • Beyond hemoglobin polymerization: The red blood cell membrane and sickle disease pathophysiology
    • Hebbel, R.P. 1991. Beyond hemoglobin polymerization: the red blood cell membrane and sickle disease pathophysiology. Blood. 77:214-237.
    • (1991) Blood , vol.77 , pp. 214-237
    • Hebbel, R.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.