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Volumn 41, Issue 1, 2008, Pages 5-9

Presence of cytosolic peroxiredoxin 2 in the erythrocyte membrane of patients with hereditary spherocytosis

Author keywords

Erythrocyte membrane proteins; Hereditary spherocytosis; Mass spectroscopy; Oxidative stress; Peroxiredoxin 2

Indexed keywords

HEMOGLOBIN; PEROXIREDOXIN; PEROXIREDOXIN 2;

EID: 44449117859     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2008.02.008     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 33846274937 scopus 로고    scopus 로고
    • The molecular basis of hereditary red cell membrane disorders
    • Delaunay J. The molecular basis of hereditary red cell membrane disorders. Blood Rev. 21 1 (2007) 1-20
    • (2007) Blood Rev. , vol.21 , Issue.1 , pp. 1-20
    • Delaunay, J.1
  • 2
    • 4143053494 scopus 로고    scopus 로고
    • Guidelines for the diagnosis and management of hereditary spherocytosis
    • Bolton-Maggs P.H.B., Stevens R.F., Dodd N.J., et al. Guidelines for the diagnosis and management of hereditary spherocytosis. Br. J. Haematol. 126 (2004) 455-474
    • (2004) Br. J. Haematol. , vol.126 , pp. 455-474
    • Bolton-Maggs, P.H.B.1    Stevens, R.F.2    Dodd, N.J.3
  • 3
    • 0025996014 scopus 로고
    • + transport in erythrocyte membrane vesicles requires a cytoplasmic protein
    • + transport in erythrocyte membrane vesicles requires a cytoplasmic protein. J. Biol. Chem. 266 (1991) 18964-18968
    • (1991) J. Biol. Chem. , vol.266 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3
  • 4
    • 0029560827 scopus 로고
    • Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B)
    • Rabilloud T., Berthier R., Vinçon M., et al. Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B). Biochem. J. 312 (1995) 699-705
    • (1995) Biochem. J. , vol.312 , pp. 699-705
    • Rabilloud, T.1    Berthier, R.2    Vinçon, M.3
  • 5
    • 0343953384 scopus 로고    scopus 로고
    • Crystal structure of decameric 2-cys peroxiredoxinfrom human erythrocytes at 1.7 A° resolution
    • Schröder E., Littlechild J.A., Lebedev A.A., et al. Crystal structure of decameric 2-cys peroxiredoxinfrom human erythrocytes at 1.7 A° resolution. Structure 8 (2000) 605-615
    • (2000) Structure , vol.8 , pp. 605-615
    • Schröder, E.1    Littlechild, J.A.2    Lebedev, A.A.3
  • 7
    • 0029591899 scopus 로고
    • Thioredoxin-linked peroxidade from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell
    • Cha M.K., and Kim I.H. Thioredoxin-linked peroxidade from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. Biochem. Biophys. Res. Commun. 217 3 (1995) 900-907
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , Issue.3 , pp. 900-907
    • Cha, M.K.1    Kim, I.H.2
  • 8
    • 0035844694 scopus 로고    scopus 로고
    • Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography
    • Harris J.R., Schröder E., Isupov M.N., et al. Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. Biochim. Biophys. Acta 1547 (2001) 221-234
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 221-234
    • Harris, J.R.1    Schröder, E.2    Isupov, M.N.3
  • 10
    • 0032473915 scopus 로고    scopus 로고
    • Porcine natural-killer enhancing factor-B: oligomerization and identification as a calpain substrate in vitro
    • Schröder E., Willis A.C., and Ponting C.P. Porcine natural-killer enhancing factor-B: oligomerization and identification as a calpain substrate in vitro. Biochim. Biophys. Acta 1384 (1998) 279-291
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 279-291
    • Schröder, E.1    Willis, A.C.2    Ponting, C.P.3
  • 11
    • 0034643923 scopus 로고    scopus 로고
    • Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane
    • Cha M.K., Yun C.H., and Kim I.H. Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane. Biochemistry 39 (2000) 6944-6950
    • (2000) Biochemistry , vol.39 , pp. 6944-6950
    • Cha, M.K.1    Yun, C.H.2    Kim, I.H.3
  • 12
    • 0030761062 scopus 로고    scopus 로고
    • Calpromotin, a cytoplasmic protein, is associated with the formation of dense cells in sickle cell anemia
    • Moore R.B., Shriver S.K., Jenkins L.D., et al. Calpromotin, a cytoplasmic protein, is associated with the formation of dense cells in sickle cell anemia. Am. J. Hematol. 56 (1997) 100-106
    • (1997) Am. J. Hematol. , vol.56 , pp. 100-106
    • Moore, R.B.1    Shriver, S.K.2    Jenkins, L.D.3
  • 13
    • 0026795940 scopus 로고
    • Calcium activated potassium transport and high molecular weight forms of calpromotin
    • Plishker G.A., Chevalier D., Seinsoth L., and Moore R.B. Calcium activated potassium transport and high molecular weight forms of calpromotin. J. Biol. Chem. 267 (1992) 21839-21843
    • (1992) J. Biol. Chem. , vol.267 , pp. 21839-21843
    • Plishker, G.A.1    Chevalier, D.2    Seinsoth, L.3    Moore, R.B.4
  • 14
    • 10744227416 scopus 로고    scopus 로고
    • Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection
    • Murphy S.C., Samuel B.U., Harrison T., et al. Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection. Blood 103 5 (2004) 1920-1928
    • (2004) Blood , vol.103 , Issue.5 , pp. 1920-1928
    • Murphy, S.C.1    Samuel, B.U.2    Harrison, T.3
  • 15
    • 0018247024 scopus 로고
    • Role of physiologic autoantibody in the removal of senescent human red cells
    • Kay M.M.B. Role of physiologic autoantibody in the removal of senescent human red cells. J. Supramol. Struct. 9 (1978) 555-567
    • (1978) J. Supramol. Struct. , vol.9 , pp. 555-567
    • Kay, M.M.B.1
  • 17
    • 0008631054 scopus 로고
    • Localization of senescent cell antigen on band 3
    • Kay M.M.B. Localization of senescent cell antigen on band 3. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 5753-5757
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 5753-5757
    • Kay, M.M.B.1
  • 18
    • 0346079412 scopus 로고
    • Naturally occurring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes
    • Lutz H.U., Bussolino F., Flepp R., et al. Naturally occurring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 7368-7372
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7368-7372
    • Lutz, H.U.1    Bussolino, F.2    Flepp, R.3
  • 19
    • 0026886458 scopus 로고
    • Naturally occurring anti-band 3 antibodies
    • Lutz A. Naturally occurring anti-band 3 antibodies. Transfus. Med. Rev. 6 (1992) 201-211
    • (1992) Transfus. Med. Rev. , vol.6 , pp. 201-211
    • Lutz, A.1
  • 20
    • 0021228486 scopus 로고
    • ICSH reference method for staining of blood and bone marrow films by azure B and eosin Y (Romanowsky stain)
    • International Committee for Standardization in Haematology. ICSH reference method for staining of blood and bone marrow films by azure B and eosin Y (Romanowsky stain). Br. J. Haematol. 57 (1984) 707-710
    • (1984) Br. J. Haematol. , vol.57 , pp. 707-710
    • International Committee for Standardization in Haematology1
  • 21
    • 0012189450 scopus 로고    scopus 로고
    • Investigation of the hereditary hemolytic anemias: membrane and enzyme abnormalities
    • Lewis S.M., Bain B.J., and Bates I. (Eds), Churchill Livingstone, London
    • Roper D., Layton M., and Lewis S.M. Investigation of the hereditary hemolytic anemias: membrane and enzyme abnormalities. In: Lewis S.M., Bain B.J., and Bates I. (Eds). Dacie and Lewis Practical Haematology (2001), Churchill Livingstone, London 167-198
    • (2001) Dacie and Lewis Practical Haematology , pp. 167-198
    • Roper, D.1    Layton, M.2    Lewis, S.M.3
  • 22
    • 17444428972 scopus 로고    scopus 로고
    • Acquired haemolytic anaemias
    • Lewis S.M., Bain B.J., and Bates I. (Eds), Churchill Livingstone, London
    • Regan F., Newlands M., and Bain B.J. Acquired haemolytic anaemias. In: Lewis S.M., Bain B.J., and Bates I. (Eds). Dacie and Lewis Practical Haematology (2001), Churchill Livingstone, London 199-229
    • (2001) Dacie and Lewis Practical Haematology , pp. 199-229
    • Regan, F.1    Newlands, M.2    Bain, B.J.3
  • 23
    • 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
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of the protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of the protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0015236352 scopus 로고
    • Electrophoresis of the major polypeptides of the human erythocyte membrane
    • Fairbanks G., Steck T.L., and Wallach D.F.H. Electrophoresis of the major polypeptides of the human erythocyte membrane. Biochemistry 10 (1971) 2606-2616
    • (1971) Biochemistry , vol.10 , pp. 2606-2616
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 27
    • 0025644237 scopus 로고
    • Clinical and molecular aspects of disorders of the erythrocyte membrane skeleton
    • Gallagher P.G., Tse W.T., and Forget B.G. Clinical and molecular aspects of disorders of the erythrocyte membrane skeleton. Semin. Perinatol. 14 5 (1990) 352-367
    • (1990) Semin. Perinatol. , vol.14 , Issue.5 , pp. 352-367
    • Gallagher, P.G.1    Tse, W.T.2    Forget, B.G.3
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Stahelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 9 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , Issue.9 , pp. 4350-4354
    • Towbin, H.1    Stahelin, T.2    Gordon, J.3
  • 29
    • 0029080207 scopus 로고
    • Altered erythrocyte membrane band 3 profile as a marker in patients at risk for cardiovascular disease
    • Santos-Silva A., Castro E.M.B., Teixeira N.A., et al. Altered erythrocyte membrane band 3 profile as a marker in patients at risk for cardiovascular disease. Atherosclerosis 116 2 (1995) 199-209
    • (1995) Atherosclerosis , vol.116 , Issue.2 , pp. 199-209
    • Santos-Silva, A.1    Castro, E.M.B.2    Teixeira, N.A.3
  • 30
    • 34047191022 scopus 로고    scopus 로고
    • Physiologically important secondary modifications of red cell membrane in hereditary spherocytosis - evidence for in vivo oxidation and lipid raft protein modifications
    • Margetis P., Antonelou M., Karababa F., et al. Physiologically important secondary modifications of red cell membrane in hereditary spherocytosis - evidence for in vivo oxidation and lipid raft protein modifications. Blood Cells Mol. Dis. 38 3 (2007) 210-220
    • (2007) Blood Cells Mol. Dis. , vol.38 , Issue.3 , pp. 210-220
    • Margetis, P.1    Antonelou, M.2    Karababa, F.3
  • 31
    • 10744233389 scopus 로고    scopus 로고
    • Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
    • Lee T.-H., Kim S.-U., Yu S.-L., et al. Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood 101 12 (2003) 5033-5038
    • (2003) Blood , vol.101 , Issue.12 , pp. 5033-5038
    • Lee, T.-H.1    Kim, S.-U.2    Yu, S.-L.3
  • 32
    • 0042568938 scopus 로고    scopus 로고
    • C.A. Neumann, D.S. Krause, C.V. Carman, et al. Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defense and tumor suppression, Nature 424 (2003) 561-565.
    • C.A. Neumann, D.S. Krause, C.V. Carman, et al. Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defense and tumor suppression, Nature 424 (2003) 561-565.
  • 33
    • 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
  • 34
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 function as a non-catalytic scavenger of low level hydrogen peroxide in the erythrocyte
    • Low F.M., Hampton M.B., Peskin A.V., and Winterbourn C.C. Peroxiredoxin 2 function as a non-catalytic scavenger of low level hydrogen peroxide in the erythrocyte. Blood 109 6 (2007) 2611-2617
    • (2007) Blood , vol.109 , Issue.6 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 36
    • 0037238206 scopus 로고    scopus 로고
    • Antioxidant protein 2 prevents methemoglobin formation in erythrocyte hemolysates
    • Stuhlmeier K.M., Kao J.J., Wallbrant P., et al. Antioxidant protein 2 prevents methemoglobin formation in erythrocyte hemolysates. Eur. J. Biochemistry 270 (2003) 334-341
    • (2003) Eur. J. Biochemistry , vol.270 , pp. 334-341
    • Stuhlmeier, K.M.1    Kao, J.J.2    Wallbrant, P.3
  • 37
    • 0021969804 scopus 로고
    • The role of hemoglobin denaturation and band 3 clustering in red blood cell aging
    • Low P.S., Waugh S.M., Zinke K., and Drenckhahn D. The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227 (1985) 531-533
    • (1985) Science , vol.227 , pp. 531-533
    • Low, P.S.1    Waugh, S.M.2    Zinke, K.3    Drenckhahn, D.4
  • 38
    • 0035078544 scopus 로고    scopus 로고
    • Leukocyte activation, erythrocyte damage, lipid profile and oxidative stress imposed by high competition physical exercise in adolescents
    • Santos-Silva A., Rebelo I., Castro E.M.B., et al. Leukocyte activation, erythrocyte damage, lipid profile and oxidative stress imposed by high competition physical exercise in adolescents. Clin. Chim. Acta 306 1-2 (2001) 119-126
    • (2001) Clin. Chim. Acta , vol.306 , Issue.1-2 , pp. 119-126
    • Santos-Silva, A.1    Rebelo, I.2    Castro, E.M.B.3
  • 39
    • 0036242731 scopus 로고    scopus 로고
    • Erythrocyte damage and leukocyte activation in ischemic stroke
    • Santos-Silva A., Rebelo I., Castro E., et al. Erythrocyte damage and leukocyte activation in ischemic stroke. Clin. Chim. Acta 320 (2002) 29-35
    • (2002) Clin. Chim. Acta , vol.320 , pp. 29-35
    • Santos-Silva, A.1    Rebelo, I.2    Castro, E.3
  • 40
    • 0036757735 scopus 로고    scopus 로고
    • Band 3 as a marker of erythrocyte changes in pregnancy
    • Belo L., Rebelo I., Castro E.M.B., et al. Band 3 as a marker of erythrocyte changes in pregnancy. Eur. J. Haematol. 69 3 (2002) 145-151
    • (2002) Eur. J. Haematol. , vol.69 , Issue.3 , pp. 145-151
    • Belo, L.1    Rebelo, I.2    Castro, E.M.B.3
  • 41
  • 42
    • 0032575368 scopus 로고    scopus 로고
    • Erythrocyte membrane band 3 profile imposed by cellular aging, by activated neutrophils and by neutrophilic elastase
    • Santos-Silva A., Castro E.M.B., Teixeira N.A., et al. Erythrocyte membrane band 3 profile imposed by cellular aging, by activated neutrophils and by neutrophilic elastase. Clin. Chim. Acta 275 (1998) 185-196
    • (1998) Clin. Chim. Acta , vol.275 , pp. 185-196
    • Santos-Silva, A.1    Castro, E.M.B.2    Teixeira, N.A.3


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