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Volumn 30, Issue 5, 1999, Pages 407-413

Iron release in erythrocytes from patients with β-thalassemia

Author keywords

thalassemia; Erythrocytes; Foetal hemoglobin (HbF); Iron release; Oxidative stress

Indexed keywords

HEMOGLOBIN F; IRON; MEMBRANE PROTEIN; METHEMOGLOBIN;

EID: 0033040939     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715769900300441     Document Type: Article
Times cited : (14)

References (41)
  • 1
    • 0030280772 scopus 로고    scopus 로고
    • Poly-N-acetyllactosaminyl saccharide chains of band 3 as determinants for anti-band 3 autoantibody binding to senescent and oxidized erythrocytes
    • M. Beppu, K. Ando and K. Kikugawa (1996) Poly-N-acetyllactosaminyl saccharide chains of band 3 as determinants for anti-band 3 autoantibody binding to senescent and oxidized erythrocytes. Cellular and Molecular Biology, 42, 1007-1024.
    • (1996) Cellular and Molecular Biology , vol.42 , pp. 1007-1024
    • Beppu, M.1    Ando, K.2    Kikugawa, K.3
  • 2
    • 0021914417 scopus 로고
    • Hemichrome binding to band 3: Nucleation of Heinz bodies on the erythrocytes membrane
    • S.M. Waugh and P.S. Low (1985) Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocytes membrane. Biochemistry, 24, 34-39.
    • (1985) Biochemistry , vol.24 , pp. 34-39
    • Waugh, S.M.1    Low, P.S.2
  • 3
    • 0029040462 scopus 로고
    • Evidence for accumulation of lipid hydroperoxides during the aging of human red blood cells in the circulation
    • K. Ando, M. Beppu and K. Kikugawa (1995) Evidence for accumulation of lipid hydroperoxides during the aging of human red blood cells in the circulation. Biology and Pharmacology Bulletin, 18, 659-663.
    • (1995) Biology and Pharmacology Bulletin , vol.18 , pp. 659-663
    • Ando, K.1    Beppu, M.2    Kikugawa, K.3
  • 4
    • 0019474177 scopus 로고
    • Association of lipid peroxidation and polymerization of membrane proteins with erythrocyte aging
    • P. Hochstein and S.K. Jain (1981) Association of lipid peroxidation and polymerization of membrane proteins with erythrocyte aging. Federation Proceedings, 40, 183-188.
    • (1981) Federation Proceedings , vol.40 , pp. 183-188
    • Hochstein, P.1    Jain, S.K.2
  • 6
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography: Oligomeric stability and origin of heterogeneity
    • J.R. Caseyand and R.A.F. Reithmeier (1991) Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography: Oligomeric stability and origin of heterogeneity. Journal of Biological Chemistry, 266, 15726-15737.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 15726-15737
    • Caseyand, J.R.1    Reithmeier, R.A.F.2
  • 7
    • 0023107937 scopus 로고
    • Detection of oxidized lipid-modified erythrocyte membrane proteins by radiolabeling with tritiated borohydride
    • M. Beppu, K. Murakami and K. Kikugawa (1987a) Detection of oxidized lipid-modified erythrocyte membrane proteins by radiolabeling with tritiated borohydride. Biochimica and Biophysical Acta, 897, 169-179.
    • (1987) Biochimica and Biophysical Acta , vol.897 , pp. 169-179
    • Beppu, M.1    Murakami, K.2    Kikugawa, K.3
  • 8
    • 0028109433 scopus 로고
    • Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense
    • M. Beppu, M. Inoue, T. Ishikawa and K. Kikugawa (1994b) Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense. Biochimica and Biophysical Acta, 1196, 81-87.
    • (1994) Biochimica and Biophysical Acta , vol.1196 , pp. 81-87
    • Beppu, M.1    Inoue, M.2    Ishikawa, T.3    Kikugawa, K.4
  • 9
    • 0021367031 scopus 로고
    • A novel phospholipid in irreversibly sickled cells: Evidence for in vivo peroxidative membrane damage in sickle cell disease
    • S.K. Jain and S.B. Shohet (1984) A novel phospholipid in irreversibly sickled cells: evidence for in vivo peroxidative membrane damage in sickle cell disease. Blood, 63, 362-367.
    • (1984) Blood , vol.63 , pp. 362-367
    • Jain, S.K.1    Shohet, S.B.2
  • 11
    • 0017811290 scopus 로고
    • Cross-linking of red blood cell membrane proteins induced by oxidative stress in β-thalassemia
    • I. Kahane (1978) Cross-linking of red blood cell membrane proteins induced by oxidative stress in β-thalassemia. FEBS Letters, 85, 267-270.
    • (1978) FEBS Letters , vol.85 , pp. 267-270
    • Kahane, I.1
  • 12
    • 0020608050 scopus 로고
    • Oxidant damage of the lipids and proteins of the erythrocyte membranes in unstable hemoglobin disease: Evidence for the role of lipid peroxidation
    • T.P. Flynn, D.W. Allen, G.J. Johnson and J.G. White (1983) Oxidant damage of the lipids and proteins of the erythrocyte membranes in unstable hemoglobin disease: Evidence for the role of lipid peroxidation. Journal of Clinical Investigation, 71, 1215-1223.
    • (1983) Journal of Clinical Investigation , vol.71 , pp. 1215-1223
    • Flynn, T.P.1    Allen, D.W.2    Johnson, G.J.3    White, J.G.4
  • 15
    • 0015882983 scopus 로고
    • Effect of α-chain precipitates on bone marrow function in homozygous β-thalassemia
    • S.N. Wickramasinghe, E. Letsky and B. Moffat (1973) Effect of α-chain precipitates on bone marrow function in homozygous β-thalassemia. British Journal of Haematology, 25, 123-129.
    • (1973) British Journal of Haematology , vol.25 , pp. 123-129
    • Wickramasinghe, S.N.1    Letsky, E.2    Moffat, B.3
  • 17
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • H.F. Bunn and J.H. Jandl (1967) Exchange of heme among hemoglobins and between hemoglobin and albumin. Journal of Biological Chemistry, 243, 465-475.
    • (1967) Journal of Biological Chemistry , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 18
    • 0016660866 scopus 로고
    • Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation
    • M. Brunori, G. Falcioni, E. Fioretti, B. Giardina and G. Rotilio (1975) Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation. European Journal of Biochemistry, 53, 99-104.
    • (1975) European Journal of Biochemistry , vol.53 , pp. 99-104
    • Brunori, M.1    Falcioni, G.2    Fioretti, E.3    Giardina, B.4    Rotilio, G.5
  • 20
    • 0023781675 scopus 로고
    • Nonheme iron in sickle erythrocyte membranes: Association with phospholipids and potential role in lipid peroxidation
    • S.A. Kuross 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
  • 21
    • 0020577135 scopus 로고
    • Increased sensitivity of isolated alpha subunits of normal human hemoglobin to oxidative damage and crosslinkage with spectrin
    • W. Joshi, L. Leb, J. Piotrowski, N. Fortier and L.M. Snyder (1983) Increased sensitivity of isolated alpha subunits of normal human hemoglobin to oxidative damage and crosslinkage with spectrin. Journal of Laboratory and Clinical Medicine, 102, 46-52.
    • (1983) Journal of Laboratory and Clinical Medicine , vol.102 , pp. 46-52
    • Joshi, W.1    Leb, L.2    Piotrowski, J.3    Fortier, N.4    Snyder, L.M.5
  • 22
    • 0344879576 scopus 로고
    • Membrane deposition of heme and non-heme iron in model thalassemic erythrocytes
    • M.D. Scott, T. Repka, R.P. Hebbel, J.J.M. van den Berg, T.C. Wagner and B.H. Lubin (1991) Membrane deposition of heme and non-heme iron in model thalassemic erythrocytes. Blood, 78 (Suppl. 1), 771.
    • (1991) Blood , vol.78 , Issue.SUPPL. 1 , pp. 771
    • Scott, M.D.1    Repka, T.2    Hebbel, R.P.3    Van Den Berg, J.J.M.4    Wagner, T.C.5    Lubin, B.H.6
  • 23
    • 0017253603 scopus 로고
    • Lipid membrane peroxidation in beta-thalassemia
    • E.A. Rachmilewitz, B.H. Lubin and S.B. Shohet (1976) Lipid membrane peroxidation in beta-thalassemia. Blood, 47, 495-505.
    • (1976) Blood , vol.47 , pp. 495-505
    • Rachmilewitz, E.A.1    Lubin, B.H.2    Shohet, S.B.3
  • 24
    • 0018942275 scopus 로고
    • Erythrocyte superoxide dismutase, catalase and giutathione peroxidase activities in beta-thalassemia (major and minor)
    • G.C. Gerli, L. Beretta and M. Bianchi (1980) Erythrocyte superoxide dismutase, catalase and giutathione peroxidase activities in beta-thalassemia (major and minor). Scandinavian Journal of Haematology, 25, 87-92.
    • (1980) Scandinavian Journal of Haematology , vol.25 , pp. 87-92
    • Gerli, G.C.1    Beretta, L.2    Bianchi, M.3
  • 26
    • 0024364270 scopus 로고
    • Allyl alcohol-induced hemolysis and its relation to iron release and lipid peroxidation
    • M. Ferrali, L. Ciccoli and M. Comporti (1989) Allyl alcohol-induced hemolysis and its relation to iron release and lipid peroxidation. Biochemical Pharmacology, 38, 1819-1825.
    • (1989) Biochemical Pharmacology , vol.38 , pp. 1819-1825
    • Ferrali, M.1    Ciccoli, L.2    Comporti, M.3
  • 27
    • 0026680709 scopus 로고
    • Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil
    • M. Ferrali, C. Signorini, L. Ciccoli and M. Comporti (1992) Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil. Biochemical Journal, 285, 295-301.
    • (1992) Biochemical Journal , vol.285 , pp. 295-301
    • Ferrali, M.1    Signorini, C.2    Ciccoli, L.3    Comporti, M.4
  • 28
    • 0025025540 scopus 로고
    • Iron release and erythrocyte damage in allyl alcohol intoxication in mice
    • M. Ferrali, L. Ciccoli, C. Signorini and M. Comporti (1990) Iron release and erythrocyte damage in allyl alcohol intoxication in mice. Biochemical Pharmacology, 40, 1485-1490.
    • (1990) Biochemical Pharmacology , vol.40 , pp. 1485-1490
    • Ferrali, M.1    Ciccoli, L.2    Signorini, C.3    Comporti, M.4
  • 30
    • 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
    • K. Schlüter and D. Drenckhahn (1986) Co-clustering of denatured hemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proceedings of the National Academy of Sciences of the USA, 83, 6137-6141.
    • (1986) Proceedings of the National Academy of Sciences of the USA , vol.83 , pp. 6137-6141
    • Schlüter, K.1    Drenckhahn, D.2
  • 31
    • 0026704541 scopus 로고
    • Isolation, characterization and immunoprecipitation studies of immune complexes from membranes of β-thalassemic erythrocytes
    • J. Yuan, R. Kannan, E. Shinar, E.A. Rachmilewitz and P.S. Low (1992) Isolation, characterization and immunoprecipitation 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
  • 32
    • 0026563546 scopus 로고
    • Globin-chain specificity of oxidation-induced changes in red blood cell membrane properties
    • S.L. Schrier and N. Mohandas (1938) Globin-chain specificity of oxidation-induced changes in red blood cell membrane properties. Blood, 79, 1586-1592.
    • (1938) Blood , vol.79 , pp. 1586-1592
    • Schrier, S.L.1    Mohandas, N.2
  • 33
    • 0000400174 scopus 로고
    • Microdetermination of oxyhemoglobin, methemoglobin and sulfhemoglobin in a single sample of blood
    • K.A. Evelyn and H.T. Malloy (1938) Microdetermination of oxyhemoglobin, methemoglobin and sulfhemoglobin in a single sample of blood. Journal of Biological Chemistry, 126, 655-662.
    • (1938) Journal of Biological Chemistry , vol.126 , pp. 655-662
    • Evelyn, K.A.1    Malloy, H.T.2
  • 35
    • 0001720527 scopus 로고
    • A new method for the preparation of α and β subunits of human hemoglobin
    • E. Bucci and C. Fronticelli (1965) A new method for the preparation of α and β subunits of human hemoglobin. Journal of Biological Chemistry, 240, 551-552.
    • (1965) Journal of Biological Chemistry , vol.240 , pp. 551-552
    • Bucci, E.1    Fronticelli, C.2
  • 37
    • 0023215591 scopus 로고
    • Erythrocytes membrane skeleton abnormalities in severe β-thalassemia
    • E. Shinar, O. Shalev, E.A. Rachmilewitz and S.L. Schrier (1987) Erythrocytes membrane skeleton abnormalities in severe β-thalassemia. Blood, 70, 158-164.
    • (1987) Blood , vol.70 , pp. 158-164
    • Shinar, E.1    Shalev, O.2    Rachmilewitz, E.A.3    Schrier, S.L.4
  • 38
    • 0024560085 scopus 로고
    • Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia
    • E. Shinar, E.A. Rachmilewitz and S.E. Lux (1989) Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia. Journal of Clinical Investigation, 83, 404-410.
    • (1989) Journal of Clinical Investigation , vol.83 , pp. 404-410
    • Shinar, E.1    Rachmilewitz, E.A.2    Lux, S.E.3
  • 41
    • 0029913286 scopus 로고    scopus 로고
    • Catalysis of soluble hemoglobin oxidation by free iron on sickle red cell membranes
    • O. Shalev 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


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