메뉴 건너뛰기




Volumn 99, Issue 1, 1997, Pages 29-36

Flow cytometric analysis of band 3 protein of human erythrocytes

Author keywords

anion exchanger; band 3 protein; eosin 5 maleimide; erythrocytes; flow cytometry; hereditary spherocytosis

Indexed keywords

ERYTHROCYTE BAND 3 PROTEIN;

EID: 0030889034     PISSN: 00651281     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0065-1281(97)80005-0     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0019832231 scopus 로고
    • Microvesicles from sickle erythrocytes and their relation to irreversible sickling
    • Allan D, Limbrick AR, Thomas P, and Westerman MP (1981) Microvesicles from sickle erythrocytes and their relation to irreversible sickling. Br J Haematol 47: 350-383
    • (1981) Br J Haematol , vol.47 , pp. 350-383
    • Allan, D.1    Limbrick, A.R.2    Thomas, P.3    Westerman, M.P.4
  • 2
    • 0018952931 scopus 로고
    • The isolation and characterization of 60 nm vesicles produced during ionophore A23 187-induced budding of human erythrocytes
    • Allan D, Thomas P, and Limbrick AR (1980) The isolation and characterization of 60 nm vesicles produced during ionophore A23 187-induced budding of human erythrocytes. Biochem J 188: 881-887
    • (1980) Biochem J , vol.188 , pp. 881-887
    • Allan, D.1    Thomas, P.2    Limbrick, A.R.3
  • 3
    • 0029641158 scopus 로고
    • Abnormal changes in erythrocyte membrane proteins in hereditary spherocytosis and their relation to clinical and biological aspects of the disease
    • Ayala S, Besson I, Aymerich M, Berga L, and Vives-Corrons JL (1995) Abnormal changes in erythrocyte membrane proteins in hereditary spherocytosis and their relation to clinical and biological aspects of the disease. Med Clin Barc 105: 45-49
    • (1995) Med Clin Barc , vol.105 , pp. 45-49
    • Ayala, S.1    Besson, I.2    Aymerich, M.3    Berga, L.4    Vives-Corrons, J.L.5
  • 4
    • 0024445677 scopus 로고
    • Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human red blood cells
    • Bütikofer P, Kuypers FA, Xu CM, Chiu DTY, and Lubin B (1989) Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human red blood cells. Blood 74: 1481-1485
    • (1989) Blood , vol.74 , pp. 1481-1485
    • Bütikofer, P.1    Kuypers, F.A.2    Xu, C.M.3    Chiu, D.T.Y.4    Lubin, B.5
  • 5
    • 0023772780 scopus 로고
    • Asymmetric distribution of phospholipids in spectrin-poor erythrocyte vesicles
    • Calvez JY, Zachowski A, Herrmann A, Morrot G, and Devaux PF (1988) Asymmetric distribution of phospholipids in spectrin-poor erythrocyte vesicles. Biochemistry 27: 5666-5670
    • (1988) Biochemistry , vol.27 , pp. 5666-5670
    • Calvez, J.Y.1    Zachowski, A.2    Herrmann, A.3    Morrot, G.4    Devaux, P.F.5
  • 6
    • 0023726325 scopus 로고
    • Decreased membrane mechanical stability and in vivo loss of surface area reflect spectrin deficiency in hereditary spherocytosis
    • Chasis JA, Agre P, and Mohandas N (1988) Decreased membrane mechanical stability and in vivo loss of surface area reflect spectrin deficiency in hereditary spherocytosis. J Clin Invest 82: 617-623
    • (1988) J Clin Invest , vol.82 , pp. 617-623
    • Chasis, J.A.1    Agre, P.2    Mohandas, N.3
  • 8
    • 0025118699 scopus 로고
    • Identification of the eosinyl-5-maleimide reaction site on the human erythrocyte anion-exchange protein: Overlap with the reaction sites of other chemical probes
    • Cobb CE, and Beth AH (1990) Identification of the eosinyl-5-maleimide reaction site on the human erythrocyte anion-exchange protein: overlap with the reaction sites of other chemical probes. Biochem 29: 8223-8290
    • (1990) Biochem , vol.29 , pp. 8223-8290
    • Cobb, C.E.1    Beth, A.H.2
  • 9
    • 0028947308 scopus 로고
    • Genetic disorders of the red cell membrane
    • Delaunay J (1995) Genetic disorders of the red cell membrane. Crit Rev Oncol Hematol 19: 79-110
    • (1995) Crit Rev Oncol Hematol , vol.19 , pp. 79-110
    • Delaunay, J.1
  • 10
    • 0022621367 scopus 로고
    • Paroxysmal nocturnal hemoglobinuria erythrocytes are of two distinct types: Positive or negative for acetylcholinesterase
    • Dockter ME, and Morrison M (1986) Paroxysmal nocturnal hemoglobinuria erythrocytes are of two distinct types: positive or negative for acetylcholinesterase. Blood 67: 540-543
    • (1986) Blood , vol.67 , pp. 540-543
    • Dockter, M.E.1    Morrison, M.2
  • 11
    • 0028351203 scopus 로고
    • Changes in ABH antigen expression on red cells during in vivo aging - A flow cytometric analysis
    • Fibach E, and Sharon R (1994) Changes in ABH antigen expression on red cells during in vivo aging - A flow cytometric analysis. Transfusion 34: 328-332
    • (1994) Transfusion , vol.34 , pp. 328-332
    • Fibach, E.1    Sharon, R.2
  • 12
    • 0028902501 scopus 로고
    • Study of the vesicles released during conservation of red cells
    • Ghailani N, Guillemin C, and Vigneron C (1995) Study of the vesicles released during conservation of red cells. Nouv Rev Fr Hematol 37: 141-147
    • (1995) Nouv Rev Fr Hematol , vol.37 , pp. 141-147
    • Ghailani, N.1    Guillemin, C.2    Vigneron, C.3
  • 13
    • 0023950643 scopus 로고
    • Effect of red cell age on vesiculation in vitro
    • Greenwalt TJ, and Dumaswala UJ (1988) Effect of red cell age on vesiculation in vitro. Br J Haematol 68: 465-167
    • (1988) Br J Haematol , vol.68 , pp. 465-1167
    • Greenwalt, T.J.1    Dumaswala, U.J.2
  • 14
    • 0026619972 scopus 로고
    • Quantification of red cell fragmentation: Usefulness of heating cells and of automatic counting devices
    • Guetarni D, Zerhouni F, Beldjord K, Henni T, Godet J, and Colonna P (1992) Quantification of red cell fragmentation: usefulness of heating cells and of automatic counting devices. Ann Biol Clin 50: 649-651
    • (1992) Ann Biol Clin , vol.50 , pp. 649-651
    • Guetarni, D.1    Zerhouni, F.2    Beldjord, K.3    Henni, T.4    Godet, J.5    Colonna, P.6
  • 15
    • 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, Sato K, Takeuchi M, Takakuwa Y, Manno S, Yawata Y, Kanzaki A, Sakai J, Ban A, Ono K, and Maede Y (1996) 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: 1804-1817
    • (1996) J Clin Invest , vol.97 , pp. 1804-1817
    • Inaba, M.1    Yawata, A.2    Koshino, I.3    Sato, K.4    Takeuchi, M.5    Takakuwa, Y.6    Manno, S.7    Yawata, Y.8    Kanzaki, A.9    Sakai, J.10    Ban, A.11    Ono, K.12    Maede, Y.13
  • 16
    • 0028569538 scopus 로고
    • Uniquely higher incidence of isolated or combined deficiency of band 3/or band 4.2 in the pathogenesis of autosomal dominantly inherited hereditary spherocytosis in the Japanese population
    • Inoue T, Kanzaki A, Yawata A, Wada H, Okamoto N, Takahashi M, Sugihara T, Yamada O, and Yawata Y (1994) Uniquely higher incidence of isolated or combined deficiency of band 3/or band 4.2 in the pathogenesis of autosomal dominantly inherited hereditary spherocytosis in the Japanese population. Int J Hematol 60: 227-238
    • (1994) Int J Hematol , vol.60 , pp. 227-238
    • Inoue, T.1    Kanzaki, A.2    Yawata, A.3    Wada, H.4    Okamoto, N.5    Takahashi, M.6    Sugihara, T.7    Yamada, O.8    Yawata, Y.9
  • 18
    • 0028939295 scopus 로고
    • Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis
    • Jarolim P, Rubin HL, Brabec V, Chrobak L, Zolotarev AS, Alper SL, Brugnara C, Wichterle H, and Palek J (1995a) Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis. Blood 85: 634-640
    • (1995) Blood , vol.85 , pp. 634-640
    • Jarolim, P.1    Rubin, H.L.2    Brabec, V.3    Chrobak, L.4    Zolotarev, A.S.5    Alper, S.L.6    Brugnara, C.7    Wichterle, H.8    Palek, J.9
  • 19
    • 0028925242 scopus 로고
    • A nonsense mutation 1 669 Glu → Ter within the regulatory domain of human erythroid ankyrin leads to a selective deficiency of the major ankyrin isoform (band 2.1) and a phenotype of autosomal dominant hereditary spherocytosis
    • Jarolim P, Rubin HL, Brabec V, and Palek J (1995b) A nonsense mutation 1 669 Glu → Ter within the regulatory domain of human erythroid ankyrin leads to a selective deficiency of the major ankyrin isoform (band 2.1) and a phenotype of autosomal dominant hereditary spherocytosis. J Clin Invest 95: 941-947
    • (1995) J Clin Invest , vol.95 , pp. 941-947
    • Jarolim, P.1    Rubin, H.L.2    Brabec, V.3    Palek, J.4
  • 21
    • 0342430428 scopus 로고
    • A subset of patients with dominantly inherited hereditary spherocytosis has a marked deficiency of the band 3 protein
    • Jarolim P, Ruff P, Coetzer TL, Prchal JT, Ballas SK, Poon M, Brabec V, and Palek J (1990) A subset of patients with dominantly inherited hereditary spherocytosis has a marked deficiency of the band 3 protein. Blood 76: 37 a
    • (1990) Blood , vol.76
    • Jarolim, P.1    Ruff, P.2    Coetzer, T.L.3    Prchal, J.T.4    Ballas, S.K.5    Poon, M.6    Brabec, V.7    Palek, J.8
  • 22
    • 0021914710 scopus 로고
    • Quantitation of protein 3 content of circulating erythrocytes at the single cell level
    • Jennings LK, Brown LK, and Dockter ME (1985) Quantitation of protein 3 content of circulating erythrocytes at the single cell level. Blood 65: 1256-1262
    • (1985) Blood , vol.65 , pp. 1256-1262
    • Jennings, L.K.1    Brown, L.K.2    Dockter, M.E.3
  • 24
    • 0342864950 scopus 로고
    • Destruction of erythrocytes
    • Williams WJ, Beutler E, Erslev AJ, Lichtman MA (Eds) New York. McGraw-Hill
    • LaCelle PL (1990) Destruction of erythrocytes. In: Williams WJ, Beutler E, Erslev AJ, Lichtman MA (Eds) Hematology. New York. McGraw-Hill. pp 398-407
    • (1990) Hematology , pp. 398-407
    • LaCelle, P.L.1
  • 25
    • 0025759938 scopus 로고
    • Formation of large, membrane skeleton-free erythrocyte vesicles as a function of intracellular pH and temperature
    • Lelkes G, and Fodor I (1991) Formation of large, membrane skeleton-free erythrocyte vesicles as a function of intracellular pH and temperature. Biochim Biophys Acta 1065: 135-144
    • (1991) Biochim Biophys Acta , vol.1065 , pp. 135-144
    • Lelkes, G.1    Fodor, I.2
  • 26
    • 0017720716 scopus 로고
    • Spontaneous reversible protein cross-linkings in the human erythrocyte membrane. Temperature and pH dependence
    • Liu SC, Fairbanks G, and Palek J (1977) Spontaneous reversible protein cross-linkings in the human erythrocyte membrane. Temperature and pH dependence. Biochemistry 16: 4066-4074
    • (1977) Biochemistry , vol.16 , pp. 4066-4074
    • Liu, S.C.1    Fairbanks, G.2    Palek, J.3
  • 27
    • 0017713374 scopus 로고
    • Release of spectrin-free vesicles from human erythrocytes during ATP-depletion
    • Lutz HU, Liu SC, and Palek J (1977) Release of spectrin-free vesicles from human erythrocytes during ATP-depletion. J Cell Biol 73: 548-560
    • (1977) J Cell Biol , vol.73 , pp. 548-560
    • Lutz, H.U.1    Liu, S.C.2    Palek, J.3
  • 29
    • 0020597843 scopus 로고
    • Binding of autologus IgG to human red cells before and after ATP-depletion. Selective exposure of binding sites (autoantigens) on spectrin free vesicles
    • Muller H, and Lutz HU (1983) Binding of autologus IgG to human red cells before and after ATP-depletion. Selective exposure of binding sites (autoantigens) on spectrin free vesicles. Biochim Biophys Acta 729: 249-257
    • (1983) Biochim Biophys Acta , vol.729 , pp. 249-257
    • Muller, H.1    Lutz, H.U.2
  • 30
    • 0027429066 scopus 로고
    • Clinical expression and laboratory detection of red blood cell membrane mutations
    • Palek J, and Jarolim P (1993) Clinical expression and laboratory detection of red blood cell membrane mutations. Sem Hematol 30: 249-283
    • (1993) Sem Hematol , vol.30 , pp. 249-283
    • Palek, J.1    Jarolim, P.2
  • 31
    • 0027236711 scopus 로고
    • Release of vesicles enriched in complement receptor 1 from human erythrocytes
    • Pascual M, Lutz HU, Steiger G, Stammler P, and Schifferili JA (1993) Release of vesicles enriched in complement receptor 1 from human erythrocytes. J Immunol 151: 397-404
    • (1993) J Immunol , vol.151 , pp. 397-404
    • Pascual, M.1    Lutz, H.U.2    Steiger, G.3    Stammler, P.4    Schifferili, J.A.5
  • 32
    • 0017353093 scopus 로고
    • Recovery of membrane microvesicles from human erythrocytes stored for transfusion: A mechanism for the discocyte-to-spherocyte shape transformation
    • Rumsby MG, Trotter J, Allan D, and Michell RH (1977) Recovery of membrane microvesicles from human erythrocytes stored for transfusion: A mechanism for the discocyte-to-spherocyte shape transformation. Biochem Soc Trans 5: 126-128
    • (1977) Biochem Soc Trans , vol.5 , pp. 126-128
    • Rumsby, M.G.1    Trotter, J.2    Allan, D.3    Michell, R.H.4
  • 33
    • 0042874070 scopus 로고
    • Mechanism underlying band 3 deficiency in a subset of patients with hereditary spherocytosis
    • Saad STO, Liu SC, and Golan D (1991) Mechanism underlying band 3 deficiency in a subset of patients with hereditary spherocytosis. Blood 78 (Suppl 1): 81a
    • (1991) Blood , vol.78 , Issue.1 SUPPL.
    • Saad, S.T.O.1    Liu, S.C.2    Golan, D.3
  • 34
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger (AE1)
    • Tanner MJA (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.A.1
  • 35
    • 0023688017 scopus 로고
    • Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork
    • Tsuji A, Kawasaki K, and Onishi S (1988) Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork. Biochemistry 27: 7447-7452
    • (1988) Biochemistry , vol.27 , pp. 7447-7452
    • Tsuji, A.1    Kawasaki, K.2    Onishi, S.3
  • 36
    • 0022526402 scopus 로고
    • Red cell vesiculation - A common membrane physiologic event
    • Wagner GM, Chiu YTD, Yee MC, and Bertram BH (1986): Red cell vesiculation - a common membrane physiologic event. J Lab Clin Med 108: 315-324
    • (1986) J Lab Clin Med , vol.108 , pp. 315-324
    • Wagner, G.M.1    Chiu, Y.T.D.2    Yee, M.C.3    Bertram, B.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.