Oxidative crosslinking, spectrin and membrane interactions of hemoglobin mixtures in HbEβ-thalassemia

References

• Weatherall DJ, Clegg JB. Thalassaemia-a global public health problem. Nature Med 1996; 2: 847–849.
   PubMed Web of Science ®Google Scholar
• Traeger J, Wood WG, Clegg JB, Weatherall DJ. Defective synthesis of HbE is due to reduced levels of beta E mRNA. Nature 1980; 288: 497–499.
   PubMed Web of Science ®Google Scholar
• Orkin SH, Kazazian HH Jr, Antonarakis SE, Ostrer H, Goff SC, Sexton JP. Abnormal RNA processing due to the exon mutation of beta E-globin gene. Nature 1982; 300: 768–769.
   PubMed Web of Science ®Google Scholar
• Fucharoen S, Winichagoon P, Pootrakul P, Piankijagum A, Wasi P. Variable severity of Southeast Asian beta-thalassaemia/HbE disease. Birth Defects Orig Artie Ser 1987; 23: 241–248.
   PubMedGoogle Scholar
• Delaunay J, Dhermy D. Mutations involving the spectrin hetero-dimer contact site: clinical expression and alterations in specific function. Semin Hematol 1993; 30: 21–33.
   PubMed Web of Science ®Google Scholar
• Wichterle H, Hanspal M, Palek J, Jarolim P. Combination of twomutant alpha spectrin alleles underlies a severe spherocytic haemolytic anemia. J Clin Invest 1996; 98: 2300–2307.
   PubMed Web of Science ®Google Scholar
• Gallagher PG, Petruzzi MJ, Weed SA et al. Mutation of a highlyconserved residue of beta I spectrin associated with fatal and near-fatal neonatal haemolytic anemia. J Clin Invest 1997; 99: 267–277.
   PubMed Web of Science ®Google Scholar
• Schrier SL, Rachmilewitz E, Mohandas N. Cellular and membraneproperties of alpha and beta thalassemic erythrocytes are different: implication for differences in clinical manifestations. Blood 1989; 74: 2194–2202.
   PubMed Web of Science ®Google Scholar
• Schrier SL. Thalassaemia: pathophysiology of red cell changes. Annu Rev Med 1994; 45: 211–218.
   PubMed Web of Science ®Google Scholar
• Knyszynski A, Danon D, Kahane I, Rachmilewitz EA. Phagocytosis of nucleated and mature beta thalassaemic red blood cells by mouse macrophages in vitro. Br J Haematol 1979; 43: 251–255.
   PubMed Web of Science ®Google Scholar
• Wiener E, Wickramasinghe SN. The in vitro interaction between red cells from patients with homozygous )3-thalassaemia and normal human macrophages. Exp Hematol 1985; 13: 401a.
   Web of Science ®Google Scholar
• Schindler M, Koppel DE, Sheetz MP. Modulation of membrane protein lateral mobility by polyphosphates and polyamines. Proc Natl Acad Sci USA 1980; 77: 1457–1461.
   PubMed Web of Science ®Google Scholar
• Sheetz MP, Casaly J. 2,3-Diphosphoglycerate and ATP dissociate erythrocyte membrane skeletons. J Biol Chem 1980; 255: 9955–9960.
   PubMed Web of Science ®Google Scholar
• Lo HH, Schimmel PR. Interaction of human hemoglobin with adenine nucleotides. J Biol Chem 1969; 244: 5084–5086.
   PubMed Web of Science ®Google Scholar
• Vincentelli J, Fraboni A, Paul C, Schnek AG. The influence of experimental conditions on the spectrin-hemoglobin interaction. Biol Chem Hoppe Seyler 1989; 370: 63–66.
   PubMed Web of Science ®Google Scholar
• Snyder LM, Garver F, Liu SC, Leb L, Trainor J, Fortier NL. Demonstration of Hemoglobin associated with isolated, purified spectrin from senescent human red cells. Br J Haematol 1985; 61: 415–419.
   PubMed Web of Science ®Google Scholar
• Shaklai N, Frayman B, Fortier N, Snyder M. Crosslinking of isolated cytoskeletal proteins with hemoglobin: a possible damage inflicted to the red cell membrane. Biochim Biophys Acta 1987; 915: 406–414.
   PubMed Web of Science ®Google Scholar
• Snyder LM, Leb L, Piotrowski J, Sauberman N, Liu SC, Fortier NL. Irreversible spectrin-Hemoglobin crosslinking in vivo: a marker for red cell senescence. Br J Haematol 1983; 53: 379–384.
   PubMed Web of Science ®Google Scholar
• Fortier N, Snyder LM, Garver F, Kiefer C, McKenney J, Mohandas N. The relationship between in vivo generated hemoglobin skeletal protein complex and increased red cell membrane rigidity. Blood 1988; 71: 1427–1431.
   PubMed Web of Science ®Google Scholar
• Rouyer-Fessard P, Garel MC, Domenget C et al. A study of membrane protein defects and alpha hemoglobin chains of red blood cells in human beta thalassaemia. J Biol Chem 1989; 264: 19092–19098.
   PubMed Web of Science ®Google Scholar
• Aljurf M, Ma L, Angelucci E et al. Abnormal assembly of membrane proteins in erythroid progenitors of patients with beta-thalassaemia major. Blood 1996; 87: 2049–2056.
   PubMed Web of Science ®Google Scholar
• Chaimanee P, Yuthavong Y. Binding of Hemoglobin to spectrin of human erythrocytes. FEBS Lett 1977; 78: 119–123.
   PubMed Web of Science ®Google Scholar
• Cassoly R. Evidence against the binding of native hemoglobin to spectrin of human erythrocytes. FEBS Lett 1978; 85: 357–360.
   PubMed Web of Science ®Google Scholar
• Datta P, Chakrabarty SB, Chakrabarty A, Chakrabarti A. Interaction of erythroid spectrin with hemoglobin variants: implications in beta-thalassaemia. Blood Cells Mol Dis 2003; 30: 248–453.
   PubMed Web of Science ®Google Scholar
• Datta P, Basu S, Chakrabarty SB et al. Enhanced oxidative cross-linking of hemoglobin E with spectrin and loss of erythrocyte membrane asymmetry in hemoglobin Efl-Thalassaemia. Blood Cells Mol Dis 2006; 37: 77–81.
   PubMed Web of Science ®Google Scholar
• Bhattacharyya M, Ray S, Bhattacharya S, Chakrabarti A. Chaperone activity and prodan binding at the self-associating domain of erythroid spectrin. J Biol Chem 2004; 279: 55080–55088.
   PubMed Web of Science ®Google Scholar
• Chakrabarti A, Bhattacharya S, Ray S, Bhattacharyya M. Binding of a denatured haeme protein and ATP to erythroid spectrin. Biochem Biophys Res Commun 2001; 282: 1189–1193.
   PubMed Web of Science ®Google Scholar
• Chakrabarti A, Kelkar DA, Chattopadhyay A. Spectrin organiza-tion and dynamics: new insights. BioSci Rep 2006; 26: 369–386.
   PubMed Web of Science ®Google Scholar
• Gordon-Smith EC, White JM. Oxidative hemolysis and Heinz body haemolytic anemia. Br J Haematol 1974; 26: 513–517.
   PubMed Web of Science ®Google Scholar
• Waters HM, Howarth JE, Hyde K et al. An evaluation of the bio-rad variant hemoglobin testing system for the detection of hemoglobinopathies. Clin Lab Haematol 1998; 20: 31–40.
   PubMedGoogle Scholar
• Riggs A. Preparation of blood hemoglobins of vertebrates. Methods Enzymol 1981; 76: 5–29.
   PubMedGoogle Scholar
• Di Iorio EE. Preparation of derivatives of ferrous and ferric hemoglobin. Methods Enzymol 1981; 76: 57–72.
   PubMedGoogle Scholar
• Sen U, Dasgupta J, Choudhury D et al. Crystal structures of HbA2and HbE and modeling of hemoglobin delta 4: interpretation of the thermal stability and the antisickling effect of HbA2 and identification of the ferrocyanide binding site in Hb. Biochemistry 2004; 43: 12477–12488.
   PubMed Web of Science ®Google Scholar
• Waugh SM, Low PS. Haemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane. Biochemistry 1985; 24: 34–39.
   PubMed Web of Science ®Google Scholar
• Winterbourn CC. Oxidative reactions of hemoglobin. Methods Enzymol 1990; 186: 265–272.
   PubMed Web of Science ®Google Scholar
• Gratzer WB. Preparation of spectrin. Methods Enzymol 1982; 85: 475–480.
   PubMed Web of Science ®Google Scholar
• Sambrook J, Fritsch EF, Maniatis T. In: Nolan C. (ed) Molecular cloning: a laboratory manual. New York: Cold Spring Harbor Laboratory Press, 1989, C5.
   Google Scholar
• Joshi W, Leb L, Piotrowski J, Fortier N, Snyder LM. Increased sensitivity of isolated alpha subunits of normal human hemoglobin to oxidative damage and crosslinkage with spectrin. J Lab Clin Med 1983; 102: 46–52.
   PubMed Web of Science ®Google Scholar
• Huang C. Studies on phosphatidylcholine vesicles: formation and physical characteristics. Biochemistry 1969; 8: 344–352.
   PubMed Web of Science ®Google Scholar
• Barbet J, Machy P, Truneh A, Leserman LD. Weak acid-induced release of liposome-encapsulated carboxyfluorescein. Biochim Biophys Acta 1984; 772: 347–356.
   PubMed Web of Science ®Google Scholar
• Bhown AS, Hunter F, Bennett JC. Analysis of the spectrin bindingdomains of globin. Biochem Biophys Res Commun 1989; 164: 894–902.
   PubMed Web of Science ®Google Scholar
• Datta P, Chakrabarty S, Chakrabarty A, Chakrabarti A. Spectrin interactions of globin chains in presence of phosphate metabolites and hydrogen peroxide: implications in thalassemia. J Biosci 2007; 32: 1147–1151.
   PubMed Web of Science ®Google Scholar
• Kiefer CR, Trainor JF, McKenney JB, Valeri CR, Snyder LM. Hemoglobin-spectrin complexes: interference with spectrin tetra-mer assembly as a mechanism for compartmentalization of band 1 and band 2 complexes. Blood 1995; 86: 366–371.
   PubMed Web of Science ®Google Scholar
• Frischer H, Bowman J. Hemoglobin E. An oxidatively unstable mutation. J Lab Clin Med 1975; 85: 531–539.
   PubMed Web of Science ®Google Scholar
• Shaeffer JR. Turnover of excess hemoglobin alpha chains in beta-thalassemic cells is ATP-dependent. J Biol Chem 1983; 258: 13172–13177.
   PubMed Web of Science ®Google Scholar
• Shaeffer JR. ATP-dependent proteolysis of hemoglobin alpha chains in beta-thalassemic hemolysates is ubiquitin-dependent. J Biol Chem 1988; 263: 13663–13669.
   PubMed Web of Science ®Google Scholar
• Solar I, Dulitzky J, Shaklai, N. Hemin-promoted peroxidation of red cell cytoskeletal proteins. Arch Biochem Biophys 1990; 283: 81–89.
   PubMed Web of Science ®Google Scholar
• Chiu DT, van den Berg J, Kuypers FA, Hung IJ, Wei JS, Liu TZ. Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: possibly related to the rates of hemin release. Free Radic Biol Med 1996; 21: 89–95.
   PubMed Web of Science ®Google Scholar