Iron release in erythrocytes from patients with β-thalassemia

References

• Beppu M., Ando K., Kikugawa K. 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 1996; 42: 1007–1024
   PubMed Web of Science ®Google Scholar
• Waugh S.M., Low P.S. Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocytes membrane. Biochemistry 1985; 24: 34–39
   PubMed Web of Science ®Google Scholar
• Ando K., Beppu M., Kikugawa K. Evidence for accumulation of lipid hydroperoxides during the aging of human red blood cells in the circulation. Biology and Pharmacology Bulletin 1995; 18: 659–663
   PubMedGoogle Scholar
• Hochstein P., Jain S.K. Association of lipid peroxidation and polymerization of membrane proteins with erythrocyte aging. Federation Proceedings 1981; 40: 183–188
   PubMedGoogle Scholar
• Bartosz G., Soszynski M., Wasilewski A. Aging of the erythrocyte. XII. Protein composition of the membrane. Mechanisms Ageing Development 1982; 19: 45–52
   PubMedGoogle Scholar
• Caseyand J.R., Reithmeier R.A.F. 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 1991; 266: 15726–15737
   PubMedGoogle Scholar
• Beppu M., Murakami K., Kikugawa K. Detection of oxidized lipid-modified erythrocyte membrane proteins by radiolabeling with tritiated borohydride. Biochimica and Biophysical Acta 1987a; 897: 169–179
   PubMedGoogle Scholar
• Beppu M., Inoue M., Ishikawa T., Kikugawa K. Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense. Biochimica and Biophysical Acta 1994b; 1196: 81–87
   PubMed Web of Science ®Google Scholar
• Jain S.K., Shohet S.B. A novel phospholipid in irreversibly sickled cells: evidence for in vivo peroxidative membrane damage in sickle cell disease. Blood 1984; 63: 362–367
   PubMed Web of Science ®Google Scholar
• Schwartz R.S., Rybicki A.C., Heath R.H., Lubin B.H. Protein 4.1 in sickle erythrocytes: evidence for oxidative damage. Journal of Biological Chemistry 1987; 262: 15666–15672
   PubMed Web of Science ®Google Scholar
• Kahane I. Cross-linking of red blood cell membrane proteins induced by oxidative stress in β-thalassemia. FEBS Letters 1978; 85: 267–270
   PubMed Web of Science ®Google Scholar
• Flynn T.P., Allen D.W., Johnson G.J., White J.G. 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 1983; 71: 1215–1223
   PubMed Web of Science ®Google Scholar
• Johnson G.J., Allen D.W., Cadman S., Fairbanks V.F., White J.G., Lampkin B.C., Kaplan M.E. Red-cell-membrane polypeptide aggregates in glucose-6-phosphate dehydrogenase mutants with chronic hemolytic disease. New England Journal of Medicine 1979; 301: 522–527
   PubMedGoogle Scholar
• Vigi V., Volpato S., Gaburro D., Conconi F., Bargellesi A., Pontremoli S. The correlation between red-cell survival and excess of α-globin synthesis in β-thalassemia. British Journal of Haematology 1969; 16: 25–30
   PubMed Web of Science ®Google Scholar
• Wickramasinghe S.N., Letsky E., Moffat B. Effect of α-chain precipitates on bone marrow function in homozygous β-thalassemia. British Journal of Haematology 1973; 25: 123–129
   Web of Science ®Google Scholar
• Scott M.D., van den Berg J.J.M., Repka T., Rouyer-Fessard P., Hebbel R.P., Beuzard P., Lubin B.H. Effect of excess α-hemoglobin chains on cellular and membrane oxidation in model β-thalassemic erythrocytes. Journal of Clinical Investigation 1993; 91: 1706–1712
   PubMed Web of Science ®Google Scholar
• Bunn H.F., Jandl J.H. Exchange of heme among hemoglobins and between hemoglobin and albumin. Journal of Biological Chemistry 1967; 243: 465–475
   Web of Science ®Google Scholar
• Brunori M., Falcioni G., Fioretti E., Giardina B., Rotilio G. 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 1975; 53: 99–104
   Google Scholar
• Sadrzadeh S.M.H., Graf E., Panter S.S., Hallaway P.E., Eaton J.W. Hemoglobin: a biologic Fenton reagent. Journal of Biological Chemistry 1984; 259: 14354–14356
   PubMed Web of Science ®Google Scholar
• Kuross S.A., Hebbel R.P. Nonheme iron in sickle erythrocyte membranes: association with phospholipids and potential role in lipid peroxidation. Blood 1988; 72: 1278–1285
   PubMed Web of Science ®Google Scholar
• Joshi W., Leb L., Piotrowski J., Fortier N., Snyder L.M. Increased sensitivity of isolated alpha subunits of normal human hemoglobin to oxidative damage and crosslinkage with spectrin. Journal of Laboratory and Clinical Medicine 1983; 102: 46–52
   PubMed Web of Science ®Google Scholar
• Scott M.D., Repka T., Hebbel R.P., van den Berg J.J.M., Wagner T.C., Lubin B.H. Membrane deposition of heme and non-heme iron in model thalassemic erythrocytes. Blood 1991; 78(1)771–771
   Google Scholar
• Rachmilewitz E.A., Lubin B.H., Shohet S.B. Lipid membrane peroxidation in beta-thalassemia. Blood 1976; 47: 495–505
   PubMed Web of Science ®Google Scholar
• Gerli G.C., Beretta L., Bianchi M. Erythrocyte superoxide dismutase, catalase and giutathione peroxidase activities in beta-thalassemia (major and minor). Scandinavian Journal of Haematology 1980; 25: 87–92
   PubMedGoogle Scholar
• Grinberg L.N., Rachmilewitz E.A., Kitrossky N., Chevion M. Hydroxyl radical generation in β-thalassemic red blood cells. Free Radical Biology and Medicine 1995; 18: 611–615
   PubMed Web of Science ®Google Scholar
• Ferrali M., Ciccoli L., Comporti M. Allyl alcohol-induced hemolysis and its relation to iron release and lipid peroxidation. Biochemical Pharmacology 1989; 38: 1819–1825
   PubMed Web of Science ®Google Scholar
• Ferrali M., Signorini C., Ciccoli L., Comporti M. Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil. Biochemical Journal 1992; 285: 295–301
   PubMed Web of Science ®Google Scholar
• Ferrali M., Ciccoli L., Signorini C., Comporti M. Iron release and erythrocyte damage in allyl alcohol intoxication in mice. Biochemical Pharmacology 1990; 40: 1485–1490
   PubMed Web of Science ®Google Scholar
• Signorini C., Ferrali M., Ciccoli L., Sugherini L., Magnani A., Comporti M. Iron release, membrane protein oxidation and erythrocyte ageing. FEBS Letters 1995; 362: 165–170
   PubMed Web of Science ®Google Scholar
• 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. Proceedings of the National Academy of Sciences of the USA 1986; 83: 6137–6141
   PubMed Web of Science ®Google Scholar
• Yuan J., Kannan R., Shinar E., Rachmilewitz E.A., Low P.S. Isolation, characterization and immunoprecipitation studies of immune complexes from membranes of β-thalassemic erythrocytes. Blood 1992; 79: 3007–3013
   PubMed Web of Science ®Google Scholar
• Schrier S.L., Mohandas N. Globin-chain specificity of oxidation-induced changes in red blood cell membrane properties. Blood 1938; 79: 1586–1592
   Google Scholar
• Evelyn K.A., Malloy H.T. Microdetermination of oxyhemoglobin, methemoglobin and sulfhemoglobin in a single sample of blood. Journal of Biological Chemistry 1938; 126: 655–662
   Google Scholar
• Beutler E., Duron O., Kelly B.M. Improved method for the determination of blood glutathione. Journal of Laboratory and Clinical Medicine 1963; 61: 882–888
   PubMed Web of Science ®Google Scholar
• Bucci E., Fronticelli C. A new method for the preparation of α and β subunits of human hemoglobin. Journal of Biological Chemistry 1965; 240: 551–552
   Google Scholar
• Lubin B.H., van den Berg J.J.M., Lewis R.A., Scott M.D., Kuypers F.A. Unique properties of the neonatal red cell. Neonatal Immunology and Haematology II, M. Xanthou, R. Bracci, G. Prindull. Elsevier Science Publishers. 1993; 79–89, In
   Google Scholar
• Shinar E., Shalev O., Rachmilewitz E.A., Schrier S.L. Erythrocytes membrane skeleton abnormalities in severe β-thalassemia. Blood 1987; 70: 158–164
   PubMed Web of Science ®Google Scholar
• Shinar E., Rachmilewitz E.A., Lux S.E. Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia. Journal of Clinical Investigation 1989; 83: 404–410
   PubMed Web of Science ®Google Scholar
• Olivieri O., De Franceschi L., Capellini M.D., Girelli D., Corrocher R., Brugnara C. Oxidative damage and erythrocytes membrane transport abnormalities in thalassemias. Blood 1994; 84: 315–320
   PubMed Web of Science ®Google Scholar
• Repka T., Shalev O., Reddy R., Yuan J., Abrahamov A., Rachmilewitz E.A., Low P.S., Hebbel R.P. Nonrandom association of free iron with membranes of sickle and β-thalassemic erythrocytes. Blood 1993; 82: 3204–3210
   PubMed Web of Science ®Google Scholar
• Shalev O., Hebbel R.P. Catalysis of soluble hemoglobin oxidation by free iron on sickle red cell membranes. Blood 1996; 87: 3948–3952
   PubMed Web of Science ®Google Scholar