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Volumn 38, Issue 3, 2007, Pages 210-220

Physiologically important secondary modifications of red cell membrane in hereditary spherocytosis-evidence for in vivo oxidation and lipid rafts protein variations

Author keywords

Carbonylation; Hemoglobin oxidation; Hereditary spherocytosis; Lipid rafts; Opsonization

Indexed keywords

ANKYRIN; ERYTHROCYTE BAND 3 PROTEIN; ERYTHROCYTE BAND 4.2 PROTEIN; HEMOGLOBIN; IMMUNOGLOBULIN G; PROTEIN ANTIBODY; SPECTRIN;

EID: 34047191022     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2006.10.163     Document Type: Article
Times cited : (29)

References (48)
  • 2
    • 15844377239 scopus 로고    scopus 로고
    • Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation
    • Inaba M., Yawata A., Koshino I., et al. Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation. J. Clin. Invest. 97 (1996) 1804-1817
    • (1996) J. Clin. Invest. , vol.97 , pp. 1804-1817
    • Inaba, M.1    Yawata, A.2    Koshino, I.3
  • 3
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • Handin R.I., Lux S.E., and Stossel T.P. (Eds), JB Lippincott Co., Philadelphia
    • Lux S.E., and Palek J. Disorders of the red cell membrane. In: Handin R.I., Lux S.E., and Stossel T.P. (Eds). Blood: Principles and Practice of Hematology (1995), JB Lippincott Co., Philadelphia 1701-1818
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1818
    • Lux, S.E.1    Palek, J.2
  • 4
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes
    • Sheetz M.P., Schindler M., and Koppel D.E. Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes. Nature 285 (1980) 510-511
    • (1980) Nature , vol.285 , pp. 510-511
    • Sheetz, M.P.1    Schindler, M.2    Koppel, D.E.3
  • 5
    • 16044367177 scopus 로고    scopus 로고
    • Anion exchanger 1 (band 3) is required to prevent erythrocyte membrane surface loss and not to form the membrane skeleton
    • Peters L.L., Shivdasani R.A., Liu S.-C., et al. Anion exchanger 1 (band 3) is required to prevent erythrocyte membrane surface loss and not to form the membrane skeleton. Cell 86 (1996) 917-927
    • (1996) Cell , vol.86 , pp. 917-927
    • Peters, L.L.1    Shivdasani, R.A.2    Liu, S.-C.3
  • 6
    • 0032939337 scopus 로고    scopus 로고
    • Evaluation of biochemical changes during in vivo erythrocyte senescence in the dog
    • Rettig M.P., Low P.S., Gimm J.A., et al. Evaluation of biochemical changes during in vivo erythrocyte senescence in the dog. Blood 93 (1999) 376-384
    • (1999) Blood , vol.93 , pp. 376-384
    • Rettig, M.P.1    Low, P.S.2    Gimm, J.A.3
  • 7
    • 0033057033 scopus 로고    scopus 로고
    • Metabolic indicators of oxidative stress correlate with haemichrome attachment to membrane, band 3 aggregation and erythrophagocytosis in beta-thalassaemia intermedia
    • Cappellini M.D., Tavazzi D., Duca L., et al. Metabolic indicators of oxidative stress correlate with haemichrome attachment to membrane, band 3 aggregation and erythrophagocytosis in beta-thalassaemia intermedia. Br. J. Haematol. 104 3 (1999) 504-512
    • (1999) Br. J. Haematol. , vol.104 , Issue.3 , pp. 504-512
    • Cappellini, M.D.1    Tavazzi, D.2    Duca, L.3
  • 8
    • 0034975571 scopus 로고    scopus 로고
    • Increase in band 3 density and aggregation in hereditary spherocytosis
    • Reinhardt D., Witt O., Miosge N., et al. Increase in band 3 density and aggregation in hereditary spherocytosis. Blood Cells Mol. Dis. 27 (2001) 399-406
    • (2001) Blood Cells Mol. Dis. , vol.27 , pp. 399-406
    • Reinhardt, D.1    Witt, O.2    Miosge, N.3
  • 9
    • 20244368825 scopus 로고    scopus 로고
    • Protein deficiency balance as a predictor of clinical outcome in hereditary spherocytosis
    • Rocha S., Rebelo I., Costa E., et al. Protein deficiency balance as a predictor of clinical outcome in hereditary spherocytosis. Eur. J. Haematol. 74 (2005) 374-380
    • (2005) Eur. J. Haematol. , vol.74 , pp. 374-380
    • Rocha, S.1    Rebelo, I.2    Costa, E.3
  • 10
    • 0026589919 scopus 로고
    • Oxidative erythrocyte membrane damage in hereditary spherocytosis
    • Caprari P., Bozzi A., Ferroni L., et al. Oxidative erythrocyte membrane damage in hereditary spherocytosis. Biochem. Int. 26 (1992) 265-274
    • (1992) Biochem. Int. , vol.26 , pp. 265-274
    • Caprari, P.1    Bozzi, A.2    Ferroni, L.3
  • 11
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • Salzer U., and Prohaska R. Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 97 (2001) 1141-1143
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salzer, U.1    Prohaska, R.2
  • 12
    • 0036530302 scopus 로고    scopus 로고
    • ++-dependent vesicle release from erythrocytes involves stomatin-specific lipid rafts, synexin (annexin VII), and sorcin
    • ++-dependent vesicle release from erythrocytes involves stomatin-specific lipid rafts, synexin (annexin VII), and sorcin. Blood 99 (2002) 2569-2577
    • (2002) Blood , vol.99 , pp. 2569-2577
    • Salzer, U.1    Hinterdorfer, P.2    Hunger, U.3
  • 13
    • 0032880488 scopus 로고    scopus 로고
    • LELY, a low expression allele of the gene encoding erythroid spectrin α-chain, in the Greek population
    • LELY, a low expression allele of the gene encoding erythroid spectrin α-chain, in the Greek population. Haematologica 84 (1999) 754-755
    • (1999) Haematologica , vol.84 , pp. 754-755
    • Papassideri, I.1    Antonelou, M.2    Karababa, F.3
  • 14
    • 0033377235 scopus 로고    scopus 로고
    • Erythropoiesis: hereditary spherocytosis in Greece: collective data on a large number of patients
    • Premetis E., Stamoulakatou A., and Loukopoulos D. Erythropoiesis: hereditary spherocytosis in Greece: collective data on a large number of patients. Hematology 4 (1999) 361-366
    • (1999) Hematology , vol.4 , pp. 361-366
    • Premetis, E.1    Stamoulakatou, A.2    Loukopoulos, D.3
  • 15
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • Dodge J.T., Mitchell C., and Hanahan D.J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 100 (1963) 119-130
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 16
    • 0023093149 scopus 로고
    • Membrane skeletal alterations during in vivo mouse red cell aging. Increase in the band 4.1a:4.1b ratio
    • Mueller T.J., Jackson C.W., Dockter M.E., and Morrison M. Membrane skeletal alterations during in vivo mouse red cell aging. Increase in the band 4.1a:4.1b ratio. J. Clin. Invest. 79 (1987) 492-499
    • (1987) J. Clin. Invest. , vol.79 , pp. 492-499
    • Mueller, T.J.1    Jackson, C.W.2    Dockter, M.E.3    Morrison, M.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.N. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.N.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G., Steck T.L., and Wallach D.F.H. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10 (1971) 2606-2617
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 20
    • 33645325682 scopus 로고    scopus 로고
    • Membrane protein carbonylation in non-leukodepleted CPDA-preserved red blood cells
    • Kriebardis A.G., Antonelou M.H., Stamoulis K.E., et al. Membrane protein carbonylation in non-leukodepleted CPDA-preserved red blood cells. Blood Cells Mol. Dis. 36 (2006) 279-282
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 279-282
    • Kriebardis, A.G.1    Antonelou, M.H.2    Stamoulis, K.E.3
  • 21
    • 17844394438 scopus 로고    scopus 로고
    • Skeletal muscle myofibrillar protein oxidation in heart failure and the protective effect of Carvedilol
    • Dalla Libera L., Ravara B., Gobbo V., et al. Skeletal muscle myofibrillar protein oxidation in heart failure and the protective effect of Carvedilol. J. Mol. Cell. Cardiol. 38 (2005) 803-807
    • (2005) J. Mol. Cell. Cardiol. , vol.38 , pp. 803-807
    • Dalla Libera, L.1    Ravara, B.2    Gobbo, V.3
  • 22
    • 0023681418 scopus 로고
    • Correlation between protein 4.1a/4.1b ratio and erythrocyte life span
    • Inaba M., and Maede Y. Correlation between protein 4.1a/4.1b ratio and erythrocyte life span. Biochim. Biophys. Acta 944 (1988) 256-264
    • (1988) Biochim. Biophys. Acta , vol.944 , pp. 256-264
    • Inaba, M.1    Maede, Y.2
  • 23
    • 0037232537 scopus 로고    scopus 로고
    • Defective organization of the erythroid cell membrane in a novel case of congenital anemia
    • Antonelou M.H., Papassideri I.S., Karababa F.J., et al. Defective organization of the erythroid cell membrane in a novel case of congenital anemia. Blood Cells Mol. Dis. 30 (2003) 43-54
    • (2003) Blood Cells Mol. Dis. , vol.30 , pp. 43-54
    • Antonelou, M.H.1    Papassideri, I.S.2    Karababa, F.J.3
  • 24
    • 0018952931 scopus 로고
    • The isolation and characterization of 60 nm vesicles ("nanovesicles") produced during ionophore A23187-induced budding of human erythrocytes
    • Allan D., Thomas P., and Limbrick A.R. The isolation and characterization of 60 nm vesicles ("nanovesicles") produced during ionophore A23187-induced budding of human erythrocytes. Biochem. J. 188 (1980) 881-887
    • (1980) Biochem. J. , vol.188 , pp. 881-887
    • Allan, D.1    Thomas, P.2    Limbrick, A.R.3
  • 25
    • 0027989483 scopus 로고
    • Hereditary spherocytosis: diagnostic and anemia-associated aberrations of ghost proteins
    • Orntoft T.F., and Clausen N. Hereditary spherocytosis: diagnostic and anemia-associated aberrations of ghost proteins. Scand. J. Clin. Lab. Invest. 54 (1994) 95-103
    • (1994) Scand. J. Clin. Lab. Invest. , vol.54 , pp. 95-103
    • Orntoft, T.F.1    Clausen, N.2
  • 26
    • 0023867132 scopus 로고
    • Deficiency of protein 4.2 in erythrocytes from a patient with a Coombs negative hemolytic anemia. Evidence for a role of protein 4.2 in stabilizing ankyrin on the membrane
    • Rybicki A.C., Heath R., Wolf J.L., et al. Deficiency of protein 4.2 in erythrocytes from a patient with a Coombs negative hemolytic anemia. Evidence for a role of protein 4.2 in stabilizing ankyrin on the membrane. J. Clin. Invest. 81 3 (1988) 893-901
    • (1988) J. Clin. Invest. , vol.81 , Issue.3 , pp. 893-901
    • Rybicki, A.C.1    Heath, R.2    Wolf, J.L.3
  • 27
    • 0026512776 scopus 로고
    • Characterization and comparison of the red blood cell membrane damage in severe human α- and β-thalassemia
    • Advani R., Sorenson S., Shinar E., et al. Characterization and comparison of the red blood cell membrane damage in severe human α- and β-thalassemia. Blood 79 (1992) 1058-1563
    • (1992) Blood , vol.79 , pp. 1058-1563
    • Advani, R.1    Sorenson, S.2    Shinar, E.3
  • 28
    • 0017353871 scopus 로고
    • Increased membrane binding of erythrocyte catalase in hereditary spherocytosis and in metabolically stressed normal cells
    • Allen D.W., Cadman S., McCann S.R., and Finkel B. Increased membrane binding of erythrocyte catalase in hereditary spherocytosis and in metabolically stressed normal cells. Blood 49 (1977) 113-123
    • (1977) Blood , vol.49 , pp. 113-123
    • Allen, D.W.1    Cadman, S.2    McCann, S.R.3    Finkel, B.4
  • 29
    • 27644592041 scopus 로고    scopus 로고
    • Lipids versus proteins as major targets of pro-oxidant, direct-acting hemolytic agents
    • McMillan D.C., Powell C.L., Bowman Z.S., et al. Lipids versus proteins as major targets of pro-oxidant, direct-acting hemolytic agents. Toxicol. Sci. 88 (2005) 74-83
    • (2005) Toxicol. Sci. , vol.88 , pp. 74-83
    • McMillan, D.C.1    Powell, C.L.2    Bowman, Z.S.3
  • 30
    • 0022408547 scopus 로고
    • Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics and spectrin-hemoglobin cross-linking
    • Snyder L.M., Fortier N.L., Trainor J., et al. Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics and spectrin-hemoglobin cross-linking. J. Clin. Invest. 76 (1985) 1971-1977
    • (1985) J. Clin. Invest. , vol.76 , pp. 1971-1977
    • Snyder, L.M.1    Fortier, N.L.2    Trainor, J.3
  • 31
    • 0017802807 scopus 로고
    • Metabolic dependence of protein arrangement in human erythrocyte membranes. I. Analysis of spectrin-rich complexes in ATP-depleted red cells
    • Palek J., Liu S.-C., and Snyder L.M. Metabolic dependence of protein arrangement in human erythrocyte membranes. I. Analysis of spectrin-rich complexes in ATP-depleted red cells. Blood 51 3 (1978) 385-395
    • (1978) Blood , vol.51 , Issue.3 , pp. 385-395
    • Palek, J.1    Liu, S.-C.2    Snyder, L.M.3
  • 32
    • 0018761655 scopus 로고
    • Calcium-induced erythrocyte membrane changes
    • Allen D.W., and Cadman S. Calcium-induced erythrocyte membrane changes. Biochim. Biophys. Acta 551 1 (1979) 1-9
    • (1979) Biochim. Biophys. Acta , vol.551 , Issue.1 , pp. 1-9
    • Allen, D.W.1    Cadman, S.2
  • 33
    • 0035674616 scopus 로고    scopus 로고
    • Programmed cell death in mature erythrocytes: a model for investigating death effector pathways operating in the absence of mitochondria
    • Bratosin D., Estaquier J., Petit F., et al. Programmed cell death in mature erythrocytes: a model for investigating death effector pathways operating in the absence of mitochondria. Cell Death Differ. 8 (2001) 1143-1156
    • (2001) Cell Death Differ. , vol.8 , pp. 1143-1156
    • Bratosin, D.1    Estaquier, J.2    Petit, F.3
  • 34
    • 32844459256 scopus 로고    scopus 로고
    • Regulation of protein 4.1R interactions with membrane proteins by Ca2+ and calmodulin
    • Nunomura W., and Takakuwa Y. Regulation of protein 4.1R interactions with membrane proteins by Ca2+ and calmodulin. Front. Biosci. 11 (2006) 1522-1539
    • (2006) Front. Biosci. , vol.11 , pp. 1522-1539
    • Nunomura, W.1    Takakuwa, Y.2
  • 35
    • 0028221176 scopus 로고
    • Effects of calcium permeabilization on RBC rheologic behaviour
    • Friederichs E., and Meiselman H.J. Effects of calcium permeabilization on RBC rheologic behaviour. Biorheology 31 (1994) 207-215
    • (1994) Biorheology , vol.31 , pp. 207-215
    • Friederichs, E.1    Meiselman, H.J.2
  • 36
    • 0023821177 scopus 로고
    • 2+ influx in normal and spherocytic red cells
    • 2+ influx in normal and spherocytic red cells. Clin. Chim. Acta 174 (1988) 141-148
    • (1988) Clin. Chim. Acta , vol.174 , pp. 141-148
    • Johnsson, R.1    Saris, N.-E.2
  • 37
    • 0030713087 scopus 로고    scopus 로고
    • Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting
    • Knowles D.W., Tilley L., Mohandas N., and Chasis JA. Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting. Proc. Natl. Acad. Sci. 94 (1997) 12969-12974
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 12969-12974
    • Knowles, D.W.1    Tilley, L.2    Mohandas, N.3    Chasis, JA.4
  • 38
    • 0023909278 scopus 로고
    • The relationship between in vivo generated hemoglobin skeletal protein complex and increased red cell membrane rigidity
    • Fortier N., Snyder L.M., Garver F., et al. The relationship between in vivo generated hemoglobin skeletal protein complex and increased red cell membrane rigidity. Blood 71 (1988) 1427-1431
    • (1988) Blood , vol.71 , pp. 1427-1431
    • Fortier, N.1    Snyder, L.M.2    Garver, F.3
  • 39
    • 0023081353 scopus 로고
    • Hemoglobin autooxidation at physiological concentrations
    • Mansouri A., and Perry C.A. Hemoglobin autooxidation at physiological concentrations. Hemoglobin 11 (1987) 353-371
    • (1987) Hemoglobin , vol.11 , pp. 353-371
    • Mansouri, A.1    Perry, C.A.2
  • 40
    • 0023395676 scopus 로고
    • Abnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding
    • Becker P.S., Morrow J.S., and Lux S.E. Abnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding. J. Clin. Invest. 80 (1987) 557-565
    • (1987) J. Clin. Invest. , vol.80 , pp. 557-565
    • Becker, P.S.1    Morrow, J.S.2    Lux, S.E.3
  • 41
    • 0033957066 scopus 로고    scopus 로고
    • Oxidation and erythrocyte senescence
    • Kiefer C.R., and Snyder L.M. Oxidation and erythrocyte senescence. Curr. Opin. Hematol. 7 (2000) 113-116
    • (2000) Curr. Opin. Hematol. , vol.7 , pp. 113-116
    • Kiefer, C.R.1    Snyder, L.M.2
  • 42
    • 0020701063 scopus 로고
    • Irreversible spectrin-haemoglobin crosslinking in vivo: a marker for red cell senescence
    • Snyder L.M., Leb L., Piotrowski J., et al. Irreversible spectrin-haemoglobin crosslinking in vivo: a marker for red cell senescence. Br. J. Haematol. 53 (1983) 379-384
    • (1983) Br. J. Haematol. , vol.53 , pp. 379-384
    • Snyder, L.M.1    Leb, L.2    Piotrowski, J.3
  • 43
    • 0037363715 scopus 로고    scopus 로고
    • Protein carbonyl groups as biomarkers of oxidative stress
    • Dalle-Donne I., Rossi R., Giustrarini D., et al. Protein carbonyl groups as biomarkers of oxidative stress. Clin. Chem. Acta 329 (2003) 23-38
    • (2003) Clin. Chem. Acta , vol.329 , pp. 23-38
    • Dalle-Donne, I.1    Rossi, R.2    Giustrarini, D.3
  • 44
    • 0023008883 scopus 로고
    • The effect of mild diamide oxidation on the structure and function of human erythrocyte spectrin
    • Becker P.S., Cohen C.M., and Lux S.E. The effect of mild diamide oxidation on the structure and function of human erythrocyte spectrin. J. Biol. Chem. 261 (1986) 4620-4628
    • (1986) J. Biol. Chem. , vol.261 , pp. 4620-4628
    • Becker, P.S.1    Cohen, C.M.2    Lux, S.E.3
  • 45
    • 0022526402 scopus 로고
    • Red cell vesiculation-A common membrane physiological event
    • Wagner G.M., Chiu D.T., Yee M.C., and Lubin B.H. Red cell vesiculation-A common membrane physiological event. J. Lab. Clin. Med. 108 (1986) 315-324
    • (1986) J. Lab. Clin. Med. , vol.108 , pp. 315-324
    • Wagner, G.M.1    Chiu, D.T.2    Yee, M.C.3    Lubin, B.H.4
  • 46
    • 0037105613 scopus 로고    scopus 로고
    • Splenectomy prolongs in vivo survival of erythrocytes differently in spectrin/ankyrin- and band 3-deficient hereditary spherocytosis
    • Reliene R., Mariani M., Zanella A., et al. Splenectomy prolongs in vivo survival of erythrocytes differently in spectrin/ankyrin- and band 3-deficient hereditary spherocytosis. Blood 100 (2002) 2208-2215
    • (2002) Blood , vol.100 , pp. 2208-2215
    • Reliene, R.1    Mariani, M.2    Zanella, A.3
  • 47
    • 0028028173 scopus 로고
    • Interaction of hereditary sperocytosis and alpha thalassaemia: a family study
    • Li C.K., Ng M.H., Cheung K.L., et al. Interaction of hereditary sperocytosis and alpha thalassaemia: a family study. Acta Haematol. 91 4 (1994) 201-205
    • (1994) Acta Haematol. , vol.91 , Issue.4 , pp. 201-205
    • Li, C.K.1    Ng, M.H.2    Cheung, K.L.3
  • 48
    • 33846274937 scopus 로고    scopus 로고
    • J. Delaunay, The molecular basis of hereditary red cell membrane disorders, Blood Rev. Article, (in press). doi:10.1016/j.bire.2006.03.005.


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