메뉴 건너뛰기




Volumn 418, Issue 2, 2009, Pages 359-367

Oxidized and poorly glycosylated band 3 is selectively phosphorylated by Syk kinase to form large membrane clusters in normal and G6PD-deficient red blood cells

Author keywords

Band 3; Diamide; p72 Syk; Src family kinase; Tyrosine phosphorylation

Indexed keywords

BAND 3; DIAMIDE; P72 SYK; SRC FAMILY KINASE; TYROSINE PHOSPHORYLATION;

EID: 61449112071     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081557     Document Type: Article
Times cited : (92)

References (44)
  • 1
    • 0345767281 scopus 로고    scopus 로고
    • Haemoglobinopathies and resistance to malaria
    • Roberts, D. J. and Williams, T. N. (2003) Haemoglobinopathies and resistance to malaria. Redox Rep. 8, 304-310
    • (2003) Redox Rep , vol.8 , pp. 304-310
    • Roberts, D.J.1    Williams, T.N.2
  • 2
    • 37549026846 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency
    • Cappellini, M. D. and Fiorelli, G. (2008) Glucose-6-phosphate dehydrogenase deficiency. Lancet 371, 64-74
    • (2008) Lancet , vol.371 , pp. 64-74
    • Cappellini, M.D.1    Fiorelli, G.2
  • 3
    • 0032513245 scopus 로고    scopus 로고
    • Plasmodium falciparum glutathione metabolism and growth are independent of glutathione system of host erythrocyte
    • Ayi, K., Cappadoro, M., Branca, M., Turrini, F. and Arese, P. (1998) Plasmodium falciparum glutathione metabolism and growth are independent of glutathione system of host erythrocyte. FEBS Lett. 424, 257-261
    • (1998) FEBS Lett , vol.424 , pp. 257-261
    • Ayi, K.1    Cappadoro, M.2    Branca, M.3    Turrini, F.4    Arese, P.5
  • 4
    • 51749087913 scopus 로고    scopus 로고
    • Naturally occurring anti-band 3 antibodies and red blood cell removal under physiological and pathological conditions
    • Pantaleo, A., Giribaldi, G., Mannu, F., Arese, P. and Turrini, F. (2008) Naturally occurring anti-band 3 antibodies and red blood cell removal under physiological and pathological conditions. Autoimmun. Rev. 7, 457-462
    • (2008) Autoimmun. Rev , vol.7 , pp. 457-462
    • Pantaleo, A.1    Giribaldi, G.2    Mannu, F.3    Arese, P.4    Turrini, F.5
  • 5
    • 0029165258 scopus 로고
    • Role of hemichrome binding to erythrocyte membrane in the generation of band-3 alterations in β-thalassemia intermedia erythrocytes
    • Mannu, F., Arese, P., Cappellini, M. D., Fiorelli, G., Cappadoro, M., Giribaldi, G. and Turrini, F. (1995) Role of hemichrome binding to erythrocyte membrane in the generation of band-3 alterations in β-thalassemia intermedia erythrocytes. Blood 86, 2014-2020
    • (1995) Blood , vol.86 , pp. 2014-2020
    • Mannu, F.1    Arese, P.2    Cappellini, M.D.3    Fiorelli, G.4    Cappadoro, M.5    Giribaldi, G.6    Turrini, F.7
  • 6
    • 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 β-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 β-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
  • 7
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger (AE1)
    • Tanner, M. J. (1993) Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Semin. Hematol. 30, 34-57
    • (1993) Semin. Hematol , vol.30 , pp. 34-57
    • Tanner, M.J.1
  • 8
    • 0025896582 scopus 로고
    • Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability
    • Low, P. S., Willardson, B. M., Mohandas, N., Rossi, M. and Shohet, S. (1991) Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability. Blood 77, 1581-1586
    • (1991) Blood , vol.77 , pp. 1581-1586
    • Low, P.S.1    Willardson, B.M.2    Mohandas, N.3    Rossi, M.4    Shohet, S.5
  • 9
    • 0024418244 scopus 로고
    • The redox state of cysteines 201 and 317 of the erythrocyte anion exchanger is critical for ankyrin binding
    • Thevenin, B. J., Willardson, B. M. and Low, P. S. (1989) The redox state of cysteines 201 and 317 of the erythrocyte anion exchanger is critical for ankyrin binding. J. Biol. Chem. 264, 15886-15892
    • (1989) J. Biol. Chem , vol.264 , pp. 15886-15892
    • Thevenin, B.J.1    Willardson, B.M.2    Low, P.S.3
  • 10
    • 0028258990 scopus 로고
    • Binding of naturally occurring antibodies to oxidatively and nonoxidatively modified erythrocyte band 3
    • Turrini, F., Mannu, F., Cappadoro, M., Ulliers, D., Giribaldi, G. and Arese, P. (1994) Binding of naturally occurring antibodies to oxidatively and nonoxidatively modified erythrocyte band 3. Biochim. Biophys. Acta 1190, 297-303
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 297-303
    • Turrini, F.1    Mannu, F.2    Cappadoro, M.3    Ulliers, D.4    Giribaldi, G.5    Arese, P.6
  • 11
    • 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., Fasler, S., Stammler, P., Kazatchkine, M. D. and Arese, P. (1987) Naturally occurring anti-band-3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes. Proc. Natl. Acad. Sci. U.S.A. 84, 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    Fasler, S.4    Stammler, P.5    Kazatchkine, M.D.6    Arese, P.7
  • 12
    • 0346398291 scopus 로고    scopus 로고
    • Mechanisms of band 3 oxidation and clustering in the phagocytosis of Plasmodium falciparum-infected erythrocytes
    • Turrini, F., Giribaldi, G., Carta, F., Mannu, F. and Arese, P. (2003) Mechanisms of band 3 oxidation and clustering in the phagocytosis of Plasmodium falciparum-infected erythrocytes. Redox Rep. 8, 300-303
    • (2003) Redox Rep , vol.8 , pp. 300-303
    • Turrini, F.1    Giribaldi, G.2    Carta, F.3    Mannu, F.4    Arese, P.5
  • 13
    • 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, F., 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, F.3    Arese, P.4    Turrini, F.5
  • 14
    • 0027288165 scopus 로고
    • Characterization of the autologous antibodies that opsonize erythrocytes with clustered integral membrane proteins
    • Turrini, F., Mannu, F., Arese, P., Yuan, J. and Low, P. S. (1993) Characterization of the autologous antibodies that opsonize erythrocytes with clustered integral membrane proteins. Blood 81, 3146-3152
    • (1993) Blood , vol.81 , pp. 3146-3152
    • Turrini, F.1    Mannu, F.2    Arese, P.3    Yuan, J.4    Low, P.S.5
  • 15
    • 0023814970 scopus 로고    scopus 로고
    • Kannan, R., Labotka, R. and Low, P. S. (1988) Isolation and characterization of the hemichrome-stabilized membrane protein aggregates from sickle erythrocytes. Major site of autologous antibody binding. J. Biol. Chem. 263, 13766-13773
    • Kannan, R., Labotka, R. and Low, P. S. (1988) Isolation and characterization of the hemichrome-stabilized membrane protein aggregates from sickle erythrocytes. Major site of autologous antibody binding. J. Biol. Chem. 263, 13766-13773
  • 16
    • 0026704541 scopus 로고
    • Isolation, characterization, and immunoprecipitation studies of immune complexes from membranes of β-thalassemic erythrocytes
    • Yuan, J., Kannan, R., Shinar, E., Rachmilewitz, E. A. and Low, P. S. (1992) Isolation, characterization, and immunoprecipitation studies of immune complexes from membranes of β-thalassemic erythrocytes. Blood 79, 3007-3013
    • (1992) Blood , vol.79 , pp. 3007-3013
    • Yuan, J.1    Kannan, R.2    Shinar, E.3    Rachmilewitz, E.A.4    Low, P.S.5
  • 17
    • 16844378031 scopus 로고    scopus 로고
    • Band 3 modifications in Plasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots
    • Tokumasu, F., Fairhurst, R. M., Ostera, G. R., Brittain, N. J., Hwang, J., Wellems, T. E. and Dvorak, J. A. (2005) Band 3 modifications in Plasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots. J. Cell Sci. 118, 1091-1098
    • (2005) J. Cell Sci , vol.118 , pp. 1091-1098
    • Tokumasu, F.1    Fairhurst, R.M.2    Ostera, G.R.3    Brittain, N.J.4    Hwang, J.5    Wellems, T.E.6    Dvorak, J.A.7
  • 18
    • 5444239857 scopus 로고    scopus 로고
    • Innate immune and non-immune mediators of erythrocyte clearance
    • Lutz, H. U. (2004) Innate immune and non-immune mediators of erythrocyte clearance. Cell. Mol. Biol. 50, 107-116
    • (2004) Cell. Mol. Biol , vol.50 , pp. 107-116
    • Lutz, H.U.1
  • 19
    • 32244435726 scopus 로고    scopus 로고
    • Immunoregulation of cellular life span
    • Kay, M. (2005) Immunoregulation of cellular life span. Ann. N. Y. Acad. Sci. 1057, 85-111
    • (2005) Ann. N. Y. Acad. Sci , vol.1057 , pp. 85-111
    • Kay, M.1
  • 20
    • 0036659906 scopus 로고    scopus 로고
    • Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes
    • Bordin, L., Brunati, A. M., Donella-Deana, A., Baggio, B., Toninello, A. and Clari, G. (2002) Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes. Blood 100, 276-282
    • (2002) Blood , vol.100 , pp. 276-282
    • Bordin, L.1    Brunati, A.M.2    Donella-Deana, A.3    Baggio, B.4    Toninello, A.5    Clari, G.6
  • 22
    • 0029833733 scopus 로고    scopus 로고
    • The Lyn-catalyzed Tyr phosphorylation of the transmembrane band-3 protein of human erythrocytes
    • Brunati, A. M., Bordin, L., Clari, G. and Moret, V. (1996) The Lyn-catalyzed Tyr phosphorylation of the transmembrane band-3 protein of human erythrocytes. Eur. J. Biochem. 240, 394-399
    • (1996) Eur. J. Biochem , vol.240 , pp. 394-399
    • Brunati, A.M.1    Bordin, L.2    Clari, G.3    Moret, V.4
  • 23
    • 0034663190 scopus 로고    scopus 로고
    • Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: Identification of primary and secondary phosphorylation sites
    • Brunati, A. M., Bordin, L., Clari, G., James, P., Quadroni, M., Baritono, E., Pinna, L. A. and Donella-Deana, A. (2000) Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites. Blood 96, 1550-1557
    • (2000) Blood , vol.96 , pp. 1550-1557
    • Brunati, A.M.1    Bordin, L.2    Clari, G.3    James, P.4    Quadroni, M.5    Baritono, E.6    Pinna, L.A.7    Donella-Deana, A.8
  • 24
    • 0032554648 scopus 로고    scopus 로고
    • Differential regulation of oxidative and osmotic stress induced Syk activation by both autophosphorylation and SH2 domains
    • Qin, S., Kurosaki, T. and Yamamura, H. (1998) Differential regulation of oxidative and osmotic stress induced Syk activation by both autophosphorylation and SH2 domains. Biochemistry 37, 5481-5486
    • (1998) Biochemistry , vol.37 , pp. 5481-5486
    • Qin, S.1    Kurosaki, T.2    Yamamura, H.3
  • 26
    • 0035892138 scopus 로고    scopus 로고
    • Deoxygenation of sickle cells stimulates Syk tyrosine kinase and inhibits a membrane tyrosine phosphatase
    • Merciris, P., Hardy-Dessources, M. D. and Giraud, F. (2001) Deoxygenation of sickle cells stimulates Syk tyrosine kinase and inhibits a membrane tyrosine phosphatase. Blood 98, 3121-3127
    • (2001) Blood , vol.98 , pp. 3121-3127
    • Merciris, P.1    Hardy-Dessources, M.D.2    Giraud, F.3
  • 27
    • 28544447372 scopus 로고    scopus 로고
    • Band 3 Tyr-phosphorylation in normal and glucose-6-phospate dehydrogenase-deficient human erythrocytes
    • Bordin, L., Zen, F., Ion-Popa, F., Barbetta, M., Baggio, B. and Clari, G. (2005) Band 3 Tyr-phosphorylation in normal and glucose-6-phospate dehydrogenase-deficient human erythrocytes. Mol. Membr. Biol. 22, 411-420
    • (2005) Mol. Membr. Biol , vol.22 , pp. 411-420
    • Bordin, L.1    Zen, F.2    Ion-Popa, F.3    Barbetta, M.4    Baggio, B.5    Clari, G.6
  • 28
    • 0031005935 scopus 로고    scopus 로고
    • Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3-associated phosphotyrosine phosphatase
    • Zipser, Y., Piade, A. and Kosower, N. S. (1997) Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3-associated phosphotyrosine phosphatase. FEBS Lett. 406, 126-130
    • (1997) FEBS Lett , vol.406 , pp. 126-130
    • Zipser, Y.1    Piade, A.2    Kosower, N.S.3
  • 29
    • 0942268718 scopus 로고    scopus 로고
    • Differential sorting of tyrosine kinases and phosphotyrosine phosphatases acting on band 3 during vesiculation of human erythrocytes
    • Minetti, G., Ciana, A. and Balduini, C. (2004) Differential sorting of tyrosine kinases and phosphotyrosine phosphatases acting on band 3 during vesiculation of human erythrocytes. Biochem. J. 377, 489-497
    • (2004) Biochem. J , vol.377 , pp. 489-497
    • Minetti, G.1    Ciana, A.2    Balduini, C.3
  • 30
    • 1642300555 scopus 로고    scopus 로고
    • Phosphotyrosine phosphatases acting on band 3 in human erythrocytes of different age: PTP1B processing during cell ageing
    • Ciana, A., Minetti, G. and Balduini, C. (2004) Phosphotyrosine phosphatases acting on band 3 in human erythrocytes of different age: PTP1B processing during cell ageing. Bioelectrochemistry 62, 169-173
    • (2004) Bioelectrochemistry , vol.62 , pp. 169-173
    • Ciana, A.1    Minetti, G.2    Balduini, C.3
  • 31
    • 0025862306 scopus 로고
    • Isolation and partial characterization of antibody- and globin-enriched complexes from membranes of dense human erythrocytes
    • Kannan, R., Yuan, J. and Low, P. S. (1991) Isolation and partial characterization of antibody- and globin-enriched complexes from membranes of dense human erythrocytes. Biochem. J. 278, 57-62
    • (1991) Biochem. J , vol.278 , pp. 57-62
    • Kannan, R.1    Yuan, J.2    Low, P.S.3
  • 32
    • 15844386537 scopus 로고    scopus 로고
    • Multiple G6PD mutations are associated with a clinical and biochemical phenotype similar to that of G6PD Mediterranean
    • Cappellini, M. D., Martinez di Montemuros, F., De Bellis, G., Debernardi, S., Dotti, C. and Fiorelli, G. (1996) Multiple G6PD mutations are associated with a clinical and biochemical phenotype similar to that of G6PD Mediterranean. Blood 87, 3953-3958
    • (1996) Blood , vol.87 , pp. 3953-3958
    • Cappellini, M.D.1    Martinez di Montemuros, F.2    De Bellis, G.3    Debernardi, S.4    Dotti, C.5    Fiorelli, G.6
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 31144465975 scopus 로고    scopus 로고
    • Protein/RNA coextraction and small two-dimensional polyacrylamide gel electrophoresis for proteomic/gene expression analysis of renal cancer biopsies
    • Barbero, G., Carta, F., Giribaldi, G., Mandili, G., Crobu, S., Ceruti, C., Fontana, D., Destefanis, P. and Turrini, F. (2006) Protein/RNA coextraction and small two-dimensional polyacrylamide gel electrophoresis for proteomic/gene expression analysis of renal cancer biopsies. Anal. Biochem. 349, 62-71
    • (2006) Anal. Biochem , vol.349 , pp. 62-71
    • Barbero, G.1    Carta, F.2    Giribaldi, G.3    Mandili, G.4    Crobu, S.5    Ceruti, C.6    Fontana, D.7    Destefanis, P.8    Turrini, F.9
  • 36
    • 26844468117 scopus 로고    scopus 로고
    • Phosphatase-directed phosphorylation-site determination: A synthesis of methods for the detection and identification of phosphopeptides
    • Torres, M. P., Thapar, R., Marzluff, W. F. and Borchers, C. H. (2005) Phosphatase-directed phosphorylation-site determination: a synthesis of methods for the detection and identification of phosphopeptides. J. Proteome Res. 4, 1628-1635
    • (2005) J. Proteome Res , vol.4 , pp. 1628-1635
    • Torres, M.P.1    Thapar, R.2    Marzluff, W.F.3    Borchers, C.H.4
  • 37
    • 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
  • 38
    • 0033740226 scopus 로고    scopus 로고
    • Band 3 protein clustering on human erythrocytes promotes binding of naturally occurring anti-band 3 and anti-spectrin antibodies
    • Hornig, R. and Lutz, H. U. (2000) Band 3 protein clustering on human erythrocytes promotes binding of naturally occurring anti-band 3 and anti-spectrin antibodies. Exp. Gerontol. 35, 1025-1044
    • (2000) Exp. Gerontol , vol.35 , pp. 1025-1044
    • Hornig, R.1    Lutz, H.U.2
  • 39
    • 0027453622 scopus 로고
    • Naturally occurring anti-band 3 antibodies have a unique affinity for C3
    • Lutz, H. U., Nater, M. and Stammler, P. (1993) Naturally occurring anti-band 3 antibodies have a unique affinity for C3. Immunology 80, 191-196
    • (1993) Immunology , vol.80 , pp. 191-196
    • Lutz, H.U.1    Nater, M.2    Stammler, P.3
  • 40
    • 0037470168 scopus 로고    scopus 로고
    • Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis
    • Chang, S. H. and Low, P. S. (2003) Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis. J. Biol. Chem. 278, 6879-6884
    • (2003) J. Biol. Chem , vol.278 , pp. 6879-6884
    • Chang, S.H.1    Low, P.S.2
  • 41
    • 33745242864 scopus 로고    scopus 로고
    • Band 3 Tyr-phosphorylation in human erythrocytes from non-pregnant and pregnant women
    • Bordin, L., Quartesan, S., Zen, F., Vianello, F. and Clari, G. (2006) Band 3 Tyr-phosphorylation in human erythrocytes from non-pregnant and pregnant women. Biochim. Biophys. Acta 1758, 611-619
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 611-619
    • Bordin, L.1    Quartesan, S.2    Zen, F.3    Vianello, F.4    Clari, G.5
  • 42
    • 0032532004 scopus 로고    scopus 로고
    • Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3
    • Minetti, G., Seppi, C., Ciana, A., Balduini, C., Low, P. S. and Brovelli, A. (1998) Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3. Biochem. J. 335, 305-311
    • (1998) Biochem. J , vol.335 , pp. 305-311
    • Minetti, G.1    Seppi, C.2    Ciana, A.3    Balduini, C.4    Low, P.S.5    Brovelli, A.6
  • 43
    • 0023227217 scopus 로고
    • Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II
    • Fukuda, M. N., Dell, A. and Scartezzini, P. (1987) Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II. J. Biol. Chem. 262, 7195-7206
    • (1987) J. Biol. Chem , vol.262 , pp. 7195-7206
    • Fukuda, M.N.1    Dell, A.2    Scartezzini, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.