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Volumn 118, Issue 5, 2005, Pages 1091-1098

Band 3 modifications in Plasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots

Author keywords

Autocorrelation; Band 3 clustering; Hemoglobin C; Malaria; Membrane modification; Power spectrum; Quantum dots

Indexed keywords

AUTOANTIBODY; ERYTHROCYTE BAND 3 PROTEIN; HEMOGLOBIN C; QUANTUM DOT;

EID: 16844378031     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01662     Document Type: Article
Times cited : (82)

References (42)
  • 1
    • 0034307363 scopus 로고    scopus 로고
    • Hemoglobin C associated with protection from severe malaria in the Dogon of Mali, a West African population with a low prevalence of hemoglobin S
    • Agarwal, A., Guindo, A., Cissoko, Y., Taylor, J. G., Coulibaly, D., Kone, A., Kayentao, K., Djimde, A., Plowe, C. V., Doumbo, O. et al. (2000). Hemoglobin C associated with protection from severe malaria in the Dogon of Mali, a West African population with a low prevalence of hemoglobin S. Blood 96, 2358-2363.
    • (2000) Blood , vol.96 , pp. 2358-2363
    • Agarwal, A.1    Guindo, A.2    Cissoko, Y.3    Taylor, J.G.4    Coulibaly, D.5    Kone, A.6    Kayentao, K.7    Djimde, A.8    Plowe, C.V.9    Doumbo, O.10
  • 2
    • 0031106036 scopus 로고    scopus 로고
    • Induction of band 3 aggregation in erythrocytes results in anti-band 3 autoantibody binding to the carbohydrate epitopes of band 3
    • Ando, K., Kikugawa, K. and Beppu, M. (1997). Induction of band 3 aggregation in erythrocytes results in anti-band 3 autoantibody binding to the carbohydrate epitopes of band 3. Arch. Biochem. Biophys. 339, 250-257.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 250-257
    • Ando, K.1    Kikugawa, K.2    Beppu, M.3
  • 3
    • 16844368076 scopus 로고    scopus 로고
    • Hemoglobin C modulates the surface topography of Plasmodium falciparum-infected erythrocytes
    • (in press)
    • Arie, T., Fairhurst, R. M., Brittain, N. J., Wellems, T. E. and Dvorak, J. A. (2005). Hemoglobin C modulates the surface topography of Plasmodium falciparum-infected erythrocytes. J. Struct. Biol. (in press).
    • (2005) J. Struct. Biol.
    • Arie, T.1    Fairhurst, R.M.2    Brittain, N.J.3    Wellems, T.E.4    Dvorak, J.A.5
  • 4
    • 8644226200 scopus 로고    scopus 로고
    • Enhanced phagocytosis of ring-parasitized mutant erythrocytes. A common mechanism that may explain protection against falciparum-malaria in sickle-trait and beta-thalassemia-trait
    • Ayi, K., Turrini, F., Piga, A. and Arese, P. (2004). Enhanced phagocytosis of ring-parasitized mutant erythrocytes. A common mechanism that may explain protection against falciparum-malaria in sickle-trait and beta-thalassemia-trait. Blood 104, 3364-3371.
    • (2004) Blood , vol.104 , pp. 3364-3371
    • Ayi, K.1    Turrini, F.2    Piga, A.3    Arese, P.4
  • 5
    • 5144228243 scopus 로고    scopus 로고
    • Erythrocyte aging in sickle cell disease
    • Bosman, G. J. (2004). Erythrocyte aging in sickle cell disease. Cell. Mol. Biol. 50, 81-86.
    • (2004) Cell. Mol. Biol. , vol.50 , pp. 81-86
    • Bosman, G.J.1
  • 6
    • 0032189018 scopus 로고    scopus 로고
    • Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency
    • Cappadoro, M., Giribaldi, G., O'Brien, E., Turrini, F., Mannu, F., Ulliers, D., Simula, G., Luzzatto, L. and Arese, P. (1998). Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency. Blood 92, 2527-2534.
    • (1998) Blood , vol.92 , pp. 2527-2534
    • Cappadoro, M.1    Giribaldi, G.2    O'Brien, E.3    Turrini, F.4    Mannu, F.5    Ulliers, D.6    Simula, G.7    Luzzatto, L.8    Arese, P.9
  • 9
    • 0038281390 scopus 로고    scopus 로고
    • Aberrant development of Plasmodium falciparum in hemoglobin CC red cells: Implications for the malaria protective effect of the homozygous state
    • Fairhurst, R. M., Fujioka, H., Hayton, K., Collins, K. F. and Wellems, T. E. (2003). Aberrant development of Plasmodium falciparum in hemoglobin CC red cells: implications for the malaria protective effect of the homozygous state. Blood 101, 3309-3315.
    • (2003) Blood , vol.101 , pp. 3309-3315
    • Fairhurst, R.M.1    Fujioka, H.2    Hayton, K.3    Collins, K.F.4    Wellems, T.E.5
  • 10
    • 0028954970 scopus 로고
    • Naturally occurring human anti-band 3 autoantibodies accelerate clearance of erythrocytes in guinea pigs
    • Giger, U., Sticher, B., Naef, R., Burger, R. and Lutz, H. U. (1995). Naturally occurring human anti-band 3 autoantibodies accelerate clearance of erythrocytes in guinea pigs. Blood 85 1920-1928.
    • (1995) Blood , vol.85 , pp. 1920-1928
    • Giger, U.1    Sticher, B.2    Naef, R.3    Burger, R.4    Lutz, H.U.5
  • 11
    • 0035016684 scopus 로고    scopus 로고
    • Growth of Plasmodium falciparum induces stage-dependent haemichrome formation, oxidative aggregation of band 3, membrane deposition of complement and antibodies, and phagocytosis of parasitized erythrocytes
    • Giribaldi, G., Ulliers, D., Mannu, E, Arese, P. and Turrini, F. (2001). Growth of Plasmodium falciparum induces stage-dependent haemichrome formation, oxidative aggregation of band 3, membrane deposition of complement and antibodies, and phagocytosis of parasitized erythrocytes. Br. J. Haematol. 113, 492-499.
    • (2001) Br. J. Haematol. , vol.113 , pp. 492-499
    • Giribaldi, G.1    Ulliers, D.2    Mannu, E.3    Arese, P.4    Turrini, F.5
  • 12
    • 0028924481 scopus 로고
    • Monoclonal antibodies that react with human band 3 residues 542-555 recognize different conformations of this protein in uninfected and Plasmodium falciparum infected erythrocytes
    • Guthrie, N., Crandall, I. E., Marini, S., Fasciglione, G. F. and Sherman, I. W. (1995). Monoclonal antibodies that react with human band 3 residues 542-555 recognize different conformations of this protein in uninfected and Plasmodium falciparum infected erythrocytes. Mol. Cell. Biochem. 144, 117-123.
    • (1995) Mol. Cell. Biochem. , vol.144 , pp. 117-123
    • Guthrie, N.1    Crandall, I.E.2    Marini, S.3    Fasciglione, G.F.4    Sherman, I.W.5
  • 13
    • 0036682503 scopus 로고    scopus 로고
    • Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development
    • Hanspal, M., Dua, M., Takakuwa, Y., Chishti, A. H. and Mizuno, A. (2002). Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development. Blood 100, 1048-1054.
    • (2002) Blood , vol.100 , pp. 1048-1054
    • Hanspal, M.1    Dua, M.2    Takakuwa, Y.3    Chishti, A.H.4    Mizuno, A.5
  • 14
    • 0025061081 scopus 로고
    • The sickle erythrocyte in double jeopardy: Autoxidation and iron decompartmentalization
    • Hebbel, R. P. (1990). The sickle erythrocyte in double jeopardy: autoxidation and iron decompartmentalization. Semin. Hematol. 27, 51-69.
    • (1990) Semin. Hematol. , vol.27 , pp. 51-69
    • Hebbel, R.P.1
  • 15
    • 0021996069 scopus 로고
    • Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients
    • Hirsch, R. E., Raventos-Suarez, C., Olson, J. A. and Nagel, R. L. (1985). Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients. Blood 66, 775-777.
    • (1985) Blood , vol.66 , pp. 775-777
    • Hirsch, R.E.1    Raventos-Suarez, C.2    Olson, J.A.3    Nagel, R.L.4
  • 16
    • 0027953906 scopus 로고
    • Immune responses to band 3 neoantigens on Plasmodium falciparum-infected erythrocytes in subjects living in an area of intense malaria transmission are associated with low parasite density and high hematocrit value
    • Hogh, B., Petersen, E., Crandall, I., Gottschau, A. and Sherman, I. W. (1994). Immune responses to band 3 neoantigens on Plasmodium falciparum-infected erythrocytes in subjects living in an area of intense malaria transmission are associated with low parasite density and high hematocrit value. Infect. Immun. 62, 4362-4366.
    • (1994) Infect. Immun. , vol.62 , pp. 4362-4366
    • Hogh, B.1    Petersen, E.2    Crandall, I.3    Gottschau, A.4    Sherman, I.W.5
  • 17
    • 0031956655 scopus 로고    scopus 로고
    • Domains in cell plasma membranes investigated by near-field scanning optical microscopy
    • Hwang, J., Gheber, L. A., Margolis, L. and Edidin, M. (1998). Domains in cell plasma membranes investigated by near-field scanning optical microscopy. Biophys. J. 74, 2184-2190.
    • (1998) Biophys. J. , vol.74 , pp. 2184-2190
    • Hwang, J.1    Gheber, L.A.2    Margolis, L.3    Edidin, M.4
  • 18
    • 0014882126 scopus 로고
    • The role of hemoglobin heme loss in Heinz body formation: Studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins
    • Jacob, H. S. and Winterhalter, K. H. (1970). The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins. J. Clin. Invest. 49, 2008-2016.
    • (1970) J. Clin. Invest. , vol.49 , pp. 2008-2016
    • Jacob, H.S.1    Winterhalter, K.H.2
  • 19
    • 0019872977 scopus 로고
    • Isolation of the phagocytosis-inducing IgG-binding antigen on senescent somatic cells
    • Kay, M. M. (1981). Isolation of the phagocytosis-inducing IgG-binding antigen on senescent somatic cells. Nature 289, 491-494.
    • (1981) Nature , vol.289 , pp. 491-494
    • Kay, M.M.1
  • 20
    • 0021297603 scopus 로고
    • Band 3, the predominant transmembrane polypeptide, undergoes proteolytic degradation as cells age
    • Kay, M. M. (1984). Band 3, the predominant transmembrane polypeptide, undergoes proteolytic degradation as cells age. Monogr. Dev. Biol. 17, 245-253.
    • (1984) Monogr. Dev. Biol. , vol.17 , pp. 245-253
    • Kay, M.M.1
  • 21
    • 0034881976 scopus 로고    scopus 로고
    • Malaria: A vaccine concept based on sickle haemoglobin's augmentation of an innate autoimmune process to band 3
    • Kennedy, J. R. (2001). Malaria: a vaccine concept based on sickle haemoglobin's augmentation of an innate autoimmune process to band 3. Int. J. Parasitol. 31, 1275-1277.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1275-1277
    • Kennedy, J.R.1
  • 22
    • 0025856071 scopus 로고
    • Uncoupling of the spectrin-based skeleton from the lipid bilayer in sickled red cells
    • Liu, S. C., Derick, L. H., Zhai, S. and Palek, J. (1991). Uncoupling of the spectrin-based skeleton from the lipid bilayer in sickled red cells. Science 252, 574-576.
    • (1991) Science , vol.252 , pp. 574-576
    • Liu, S.C.1    Derick, L.H.2    Zhai, S.3    Palek, J.4
  • 23
    • 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. (1985). The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227, 531-533.
    • (1985) Science , vol.227 , pp. 531-533
    • Low, P.S.1    Waugh, S.M.2    Zinke, K.3    Drenckhahn, D.4
  • 24
    • 0021680934 scopus 로고
    • Naturally occurring autoantibodies to exoplasmic and cryptic regions of band 3 protein, the major integral membrane protein of human red blood cells
    • Lutz, H. U., Flepp, R. and Stringaro-Wipf, G. (1984). Naturally occurring autoantibodies to exoplasmic and cryptic regions of band 3 protein, the major integral membrane protein of human red blood cells. J. Immunol. 133, 2610-2618.
    • (1984) J. Immunol. , vol.133 , pp. 2610-2618
    • Lutz, H.U.1    Flepp, R.2    Stringaro-Wipf, G.3
  • 25
    • 0023730842 scopus 로고
    • Naturally occurring anti-band 3 antibodies and complement in phagocytosis of oxidatively-stressed and in clearance of senescent red cells
    • Lutz, H. U., Fasler, S., Stammler, P., Bussolino, F. and Arese, P. (1988). Naturally occurring anti-band 3 antibodies and complement in phagocytosis of oxidatively-stressed and in clearance of senescent red cells. Blood Cells 14, 175-203.
    • (1988) Blood Cells , vol.14 , pp. 175-203
    • Lutz, H.U.1    Fasler, S.2    Stammler, P.3    Bussolino, F.4    Arese, P.5
  • 27
    • 0014685779 scopus 로고
    • Formation of hemichromes from oxidized hemoglobin subunits
    • Rachmilewitz, E. A. (1969). Formation of hemichromes from oxidized hemoglobin subunits. Ann. N. Y. Acad. Sci. 165, 171-184.
    • (1969) Ann. N. Y. Acad. Sci. , vol.165 , pp. 171-184
    • Rachmilewitz, E.A.1
  • 28
    • 0016235720 scopus 로고
    • Denaturation of the normal and abnormal hemoglobin molecule
    • Rachmilewitz, E. A. (1974). Denaturation of the normal and abnormal hemoglobin molecule. Semin. Hematol. 11, 441-462.
    • (1974) Semin. Hematol. , vol.11 , pp. 441-462
    • Rachmilewitz, E.A.1
  • 30
    • 0028364885 scopus 로고
    • Detection, formation, and relevance of hemichromes and hemochromes
    • Rifkind, J. M., Abugo, O., Levy, A. and Heim, J. (1994). Detection, formation, and relevance of hemichromes and hemochromes. Methods Enzymol. 231, 449-480.
    • (1994) Methods Enzymol. , vol.231 , pp. 449-480
    • Rifkind, J.M.1    Abugo, O.2    Levy, A.3    Heim, J.4
  • 31
    • 0030581703 scopus 로고    scopus 로고
    • A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum
    • Roggwiller, E., Betoulle, M. E., Blisnick, T. and Braun Breton, C. (1996). A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum. Mol. Biochem. Parasitol. 82, 13-24.
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 13-24
    • Roggwiller, E.1    Betoulle, M.E.2    Blisnick, T.3    Braun Breton, C.4
  • 32
    • 0347814858 scopus 로고
    • 1st International workshop on monoclonal-antibodies against human red blood-cell and related antigens
    • Rouger, P. and Anstee, D. (1988). 1st International workshop on monoclonal-antibodies against human red blood-cell and related antigens. Vox Sang. 55, 57-61.
    • (1988) Vox Sang , vol.55 , pp. 57-61
    • Rouger, P.1    Anstee, D.2
  • 33
    • 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
    • Schluter, K. and Drenckhahn, D. (1986). Co-clustering of denatured hemoglobin with band 3, its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proc. Natl. Acad. Sci. USA 83, 6137-6141.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6137-6141
    • Schluter, K.1    Drenckhahn, D.2
  • 35
    • 0002375258 scopus 로고
    • Clinical manifestations of hemoglobin C disorders
    • Smith, E. W. and Krevans, J. R. (1959). Clinical manifestations of hemoglobin C disorders. Bull. Johns Hopkins Hosp. 104, 17-43.
    • (1959) Bull. Johns Hopkins Hosp. , vol.104 , pp. 17-43
    • Smith, E.W.1    Krevans, J.R.2
  • 36
    • 0042913276 scopus 로고    scopus 로고
    • Development and application of quantum dots for immunocytochemistry of human erythrocytes
    • Tokumasu, F. and Dvorak, J. (2003). Development and application of quantum dots for immunocytochemistry of human erythrocytes. J. Microsc. 211, 256-261.
    • (2003) J. Microsc. , vol.211 , pp. 256-261
    • Tokumasu, F.1    Dvorak, J.2
  • 37
    • 1242310570 scopus 로고    scopus 로고
    • Heterogeneous molecular distribution in supported multicomponent lipid bilayers
    • Tokumasu, F., Hwang, J. and Dvorak, J. A. (2004). Heterogeneous molecular distribution in supported multicomponent lipid bilayers. Langmuir 20, 614-618.
    • (2004) Langmuir , vol.20 , pp. 614-618
    • Tokumasu, F.1    Hwang, J.2    Dvorak, J.A.3
  • 38
    • 0026343738 scopus 로고
    • Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis
    • Turrini, F., Arese, P., Yuan, J. and Low, P. S. (1991). Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis. J. Biol. Chem. 266, 23611-23617.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23611-23617
    • Turrini, F.1    Arese, P.2    Yuan, J.3    Low, P.S.4
  • 39
    • 0021914417 scopus 로고
    • Hemichrome binding to band 3, nucleation of Heinz bodies on the erythrocyte membrane
    • Waugh, S. M. and Low, P. S. (1985). Hemichrome binding to band 3, nucleation of Heinz bodies on the erythrocyte membrane. Biochemistry 24, 34-39.
    • (1985) Biochemistry , vol.24 , pp. 34-39
    • Waugh, S.M.1    Low, P.S.2
  • 40
    • 0022993811 scopus 로고
    • Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes
    • Waugh, S. M., Willardson, B. M., Kannan, R., Labotka, R. J. and Low, P. S. (1986). Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes. J. Clin. Invest. 78, 1155-1160.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1155-1160
    • Waugh, S.M.1    Willardson, B.M.2    Kannan, R.3    Labotka, R.J.4    Low, P.S.5
  • 41
    • 0016283763 scopus 로고
    • Studies of hemoglobin denaturation and Heinz body formation in the unstable hemoglobins
    • Winterbourn, C. C. and Carrell, R. W. (1974). Studies of hemoglobin denaturation and Heinz body formation in the unstable hemoglobins. J. Clin. Invest. 54, 678-689.
    • (1974) J. Clin. Invest. , vol.54 , pp. 678-689
    • Winterbourn, C.C.1    Carrell, R.W.2
  • 42
    • 0037225979 scopus 로고    scopus 로고
    • Immunofluorescent labeling of cancer marker Her2 and other cellular targets with semiconductor quantum dots
    • Wu, X., Liu, H., Liu, J., Haley, K. N., Treadway, J. A., Larson, J. P., Ge, N., Peale, F. and Bruchez, M. P. (2003). Immunofluorescent labeling of cancer marker Her2 and other cellular targets with semiconductor quantum dots. Nat. Biotechnol. 21, 41-46.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 41-46
    • Wu, X.1    Liu, H.2    Liu, J.3    Haley, K.N.4    Treadway, J.A.5    Larson, J.P.6    Ge, N.7    Peale, F.8    Bruchez, M.P.9


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