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Volumn 37, Issue 6, 1997, Pages 607-615

Blood group antigens Rba, Tra, and Wda are located in the third ectoplasmic loop of erythroid band 3

Author keywords

[No Author keywords available]

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; ASPARAGINE; BLOOD GROUP ANTIGEN; CHYMOTRYPSIN; DNA; EPITOPE; ERYTHROCYTE BAND 3 PROTEIN; LEUCINE; LYSINE; MESSENGER RNA; METHIONINE; PROLINE; SULFATE; VALINE;

EID: 0030920568     PISSN: 00411132     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1537-2995.1997.37697335155.x     Document Type: Article
Times cited : (31)

References (64)
  • 1
    • 0024316871 scopus 로고
    • Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)
    • Lux SE, John KM, Kopito RR, Lodish HF. Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Proc Natl Acad Sci U S A 1989;86:9089-93.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 9089-9093
    • Lux, S.E.1    John, K.M.2    Kopito, R.R.3    Lodish, H.F.4
  • 2
    • 0021972927 scopus 로고
    • Structure of the murine anion exchange protein
    • Kopito RR, Lodish HF. Structure of the murine anion exchange protein. J Cell Biochem 1985;29:1-17.
    • (1985) J Cell Biochem , vol.29 , pp. 1-17
    • Kopito, R.R.1    Lodish, H.F.2
  • 3
    • 0022428478 scopus 로고
    • Primary structure and transmembrane orientation of the murine anion exchange protein
    • Kopito RR, Lodish HF. Primary structure and transmembrane orientation of the murine anion exchange protein. Nature 1985;316:234-8.
    • (1985) Nature , vol.316 , pp. 234-238
    • Kopito, R.R.1    Lodish, H.F.2
  • 4
    • 0024264841 scopus 로고
    • The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence
    • Tanner MJ, Martin PG, High S. The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence. Biochem J 1988;256:703-12.
    • (1988) Biochem J , vol.256 , pp. 703-712
    • Tanner, M.J.1    Martin, P.G.2    High, S.3
  • 5
    • 0026354679 scopus 로고
    • Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis
    • Jarolim P, Palek J, Amato D, et al. Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis. Proc Natl Acad Sci U S A 1991;88:11022-6.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 11022-11026
    • Jarolim, P.1    Palek, J.2    Amato, D.3
  • 6
    • 0026608784 scopus 로고
    • Basis of unique red cell membrane properties in hereditary ovalocytosis
    • Schofield AE, Tanner MJ, Pinder JC, et al. Basis of unique red cell membrane properties in hereditary ovalocytosis. J Mol Biol 1992;223:949-58.
    • (1992) J Mol Biol , vol.223 , pp. 949-958
    • Schofield, A.E.1    Tanner, M.J.2    Pinder, J.C.3
  • 7
    • 0026696751 scopus 로고
    • 327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2
    • 327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2. Blood 1992;80:523-9.
    • (1992) Blood , vol.80 , pp. 523-529
    • Jarolim, P.1    Palek, J.2    Rubin, H.L.3
  • 9
    • 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, et al. 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 1995;85:634-40.
    • (1995) Blood , vol.85 , pp. 634-640
    • Jarolim, P.1    Rubin, H.L.2    Brabec, V.3
  • 11
    • 0027312707 scopus 로고
    • Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868→Leu in the membrane domain of band 3
    • Bruce LJ, Kay MM, Lawrence C, Tanner MJ. Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868→Leu in the membrane domain of band 3. Biochem J 1993;293:317-20.
    • (1993) Biochem J , vol.293 , pp. 317-320
    • Bruce, L.J.1    Kay, M.M.2    Lawrence, C.3    Tanner, M.J.4
  • 12
    • 0026006230 scopus 로고
    • Human erythrocyte band 3 polymorphism (band 3 Memphis): Characterization of the structural modification (Lys 56→Glu) by protein chemistry methods
    • Yannoukakos D, Vasseur C, Driancourt C, et al. Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56→Glu) by protein chemistry methods. Blood 1991;78:1117-20.
    • (1991) Blood , vol.78 , pp. 1117-1120
    • Yannoukakos, D.1    Vasseur, C.2    Driancourt, C.3
  • 13
    • 0026767441 scopus 로고
    • Band 3 Memphis: A widespread polymorphism with abnormal electrophoretic mobility of erythrocyte band 3 protein caused by substitution AAG→GAG (Lys→Glu) in codon 56
    • Jarolim P, Rubin HL, Zhai S, et al. Band 3 Memphis: a widespread polymorphism with abnormal electrophoretic mobility of erythrocyte band 3 protein caused by substitution AAG→GAG (Lys→Glu) in codon 56. Blood 1992;80:1592-8.
    • (1992) Blood , vol.80 , pp. 1592-1598
    • Jarolim, P.1    Rubin, H.L.2    Zhai, S.3
  • 14
    • 0021885318 scopus 로고
    • A new variant of the anion transport protein in human erythrocytes
    • Hsu L, Morrison M. A new variant of the anion transport protein in human erythrocytes. Biochemistry 1985;24:3086-90.
    • (1985) Biochemistry , vol.24 , pp. 3086-3090
    • Hsu, L.1    Morrison, M.2
  • 16
    • 0013030502 scopus 로고
    • Nuevo grupo sanguineo encontrado en descencientes de Indios
    • Layrisse M, Arends T, Dominguez-Sisco R. Nuevo grupo sanguineo encontrado en descencientes de Indios. Acta Med Venez 1955;3:132.
    • (1955) Acta Med Venez , vol.3 , pp. 132
    • Layrisse, M.1    Arends, T.2    Dominguez-Sisco, R.3
  • 18
    • 0342797951 scopus 로고
    • Molecular characterization of the Diego blood group antigen
    • Jarolim P, Rubin HL, Moulds JM. Molecular characterization of the Diego blood group antigen (abstract). Blood 1994;84(Suppl 1):237a.
    • (1994) Blood , vol.84 , Issue.1 SUPPL.
    • Jarolim, P.1    Rubin, H.L.2    Moulds, J.M.3
  • 20
    • 0028867451 scopus 로고
    • Blood group terminology 1995. ISBT Working Party on terminology for red cell surface antigens
    • Daniels GL, Anstee DJ, Cartron JP, et al. Blood group terminology 1995. ISBT Working Party on terminology for red cell surface antigens. Vox Sang 1995;69:265-79.
    • (1995) Vox Sang , vol.69 , pp. 265-279
    • Daniels, G.L.1    Anstee, D.J.2    Cartron, J.P.3
  • 21
    • 0020653478 scopus 로고
    • b antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells
    • b antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells. Biochem J 1983;209:273-6.
    • (1983) Biochem J , vol.209 , pp. 273-276
    • Ridgwell, K.1    Tanner, M.J.2    Anstee, D.J.3
  • 26
    • 0025162398 scopus 로고
    • b antigen to an interaction between glycophorin A and band 3
    • b antigen to an interaction between glycophorin A and band 3. Blood 1990;76:842-8.
    • (1990) Blood , vol.76 , pp. 842-848
    • Telen, M.J.1    Chasis, J.A.2
  • 28
    • 0028909047 scopus 로고
    • Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: A site of interaction between band 3 and glycophorin A under certain conditions
    • Bruce LJ, Ring SM, Anstee DJ, et al. Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: a site of interaction between band 3 and glycophorin A under certain conditions. Blood 1995;85:541-7.
    • (1995) Blood , vol.85 , pp. 541-547
    • Bruce, L.J.1    Ring, S.M.2    Anstee, D.J.3
  • 31
    • 0022398082 scopus 로고
    • Multiplicity of genetic polymorphisms of blood in the Schmiedeleut Hutterites
    • Lewis M, Kaita H, Giblett ER, et al. Multiplicity of genetic polymorphisms of blood in the Schmiedeleut Hutterites. Am J Med Genet 1985;22:477-85.
    • (1985) Am J Med Genet , vol.22 , pp. 477-485
    • Lewis, M.1    Kaita, H.2    Giblett, E.R.3
  • 32
    • 0025010121 scopus 로고
    • Wd(a+) red blood cells in two sisters of a Hei//om Khoisan family in Namibia
    • Moores P, Smart E, Marks M, Botha MC. Wd(a+) red blood cells in two sisters of a Hei//om Khoisan family in Namibia. Hum Hered 1990;40:257-61.
    • (1990) Hum Hered , vol.40 , pp. 257-261
    • Moores, P.1    Smart, E.2    Marks, M.3    Botha, M.C.4
  • 33
    • 0028985558 scopus 로고
    • Assignment of the Waldner blood group locus (WD) to 17q12-q21
    • Zelinski T, Coghlan G, White L, Philipps S. Assignment of the Waldner blood group locus (WD) to 17q12-q21. Genomics 1995;25:320-2.
    • (1995) Genomics , vol.25 , pp. 320-322
    • Zelinski, T.1    Coghlan, G.2    White, L.3    Philipps, S.4
  • 36
    • 0019738069 scopus 로고
    • DNA analysis in the diagnosis of hemoglobin disorders
    • Goossens M, Kan YY. DNA analysis in the diagnosis of hemoglobin disorders. Methods Enzymol 1981;76:805-17.
    • (1981) Methods Enzymol , vol.76 , pp. 805-817
    • Goossens, M.1    Kan, Y.Y.2
  • 37
    • 0024595101 scopus 로고
    • Detection of polymorphisms of human DNA by gel electrophoresis as single-strand conformation polymorphisms
    • Orita M, Iwahana H, Kanazawa H, et al. Detection of polymorphisms of human DNA by gel electrophoresis as single-strand conformation polymorphisms. Proc Natl Acad Sci USA 1989;86:2766-70.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2766-2770
    • Orita, M.1    Iwahana, H.2    Kanazawa, H.3
  • 38
    • 0024756969 scopus 로고
    • Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction
    • Orita M, Suzuki Y, Sekiya T, Hayashi K. Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics 1989;5:874-9.
    • (1989) Genomics , vol.5 , pp. 874-879
    • Orita, M.1    Suzuki, Y.2    Sekiya, T.3    Hayashi, K.4
  • 39
    • 0024355240 scopus 로고
    • Primary structure of the rat kidney band 3 anion exchange protein deduced from a cDNA
    • Kudrycki KE, Shull GE. Primary structure of the rat kidney band 3 anion exchange protein deduced from a cDNA. J Biol Chem 1989;264:8185-92.
    • (1989) J Biol Chem , vol.264 , pp. 8185-8192
    • Kudrycki, K.E.1    Shull, G.E.2
  • 41
    • 0023973454 scopus 로고
    • Alternative primary structures in the transmembrane domain of the chicken erythroid anionic transporter
    • Cox JV, Lazarides E. Alternative primary structures in the transmembrane domain of the chicken erythroid anionic transporter. Mol Cell Biol 1988;8:1327-35.
    • (1988) Mol Cell Biol , vol.8 , pp. 1327-1335
    • Cox, J.V.1    Lazarides, E.2
  • 42
    • 0026628247 scopus 로고
    • Amino acid sequence of band-3 protein from rainbow trout erythrocytes derived from cDNA
    • Hubner S, Michel F, Rudloff V, Appelhans H. Amino acid sequence of band-3 protein from rainbow trout erythrocytes derived from cDNA. Biochem J 1992;285:17-23.
    • (1992) Biochem J , vol.285 , pp. 17-23
    • Hubner, S.1    Michel, F.2    Rudloff, V.3    Appelhans, H.4
  • 43
    • 0026602804 scopus 로고
    • Complete nucleotide sequence of band 3 related anion transport protein AE2 from human kidney
    • Gehrig H, Muller W, Appelhans H. Complete nucleotide sequence of band 3 related anion transport protein AE2 from human kidney. Biochim Biophys Acta 1992;1130:326-8.
    • (1992) Biochim Biophys Acta , vol.1130 , pp. 326-328
    • Gehrig, H.1    Muller, W.2    Appelhans, H.3
  • 44
    • 0023760537 scopus 로고
    • Cloning and characterization of a murine band 3-related cDNa from kidney and from a lymphoid cell line
    • Alper SL, Kopito RR, Libresco SM, Lodish HM. Cloning and characterization of a murine band 3-related cDNA from kidney and from a lymphoid cell line. J Biol Chem 1988;263:17092-9.
    • (1988) J Biol Chem , vol.263 , pp. 17092-17099
    • Alper, S.L.1    Kopito, R.R.2    Libresco, S.M.3    Lodish, H.M.4
  • 45
    • 0025078761 scopus 로고
    • Functional expression and subcellular localization of an anion exchanger cloned from choroid plexus
    • Lindsey AE, Schneider K, Simmons DM, et al. Functional expression and subcellular localization of an anion exchanger cloned from choroid plexus. Proc Natl Acad Sci U S A 1990;87:5278-82.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5278-5282
    • Lindsey, A.E.1    Schneider, K.2    Simmons, D.M.3
  • 46
    • 0026687280 scopus 로고
    • cDNA cloning and localization of a band 3-related protein from ileum
    • Chow A, Dobbins JW, Aronson PS, Igarashi P. cDNA cloning and localization of a band 3-related protein from ileum. Am J Physiol 1992;263:G345-52.
    • (1992) Am J Physiol , vol.263
    • Chow, A.1    Dobbins, J.W.2    Aronson, P.S.3    Igarashi, P.4
  • 47
    • 0027936966 scopus 로고
    • Molecular cloning, expression, and chromosomal localization of two isoforms of the AE3 anion exchanger from human heart
    • Yannoukakos D, Stuart-Tilley A, Fernandez HA, et al. Molecular cloning, expression, and chromosomal localization of two isoforms of the AE3 anion exchanger from human heart. Circ Res 1994;75:603-14.
    • (1994) Circ Res , vol.75 , pp. 603-614
    • Yannoukakos, D.1    Stuart-Tilley, A.2    Fernandez, H.A.3
  • 48
    • 0024805898 scopus 로고
    • Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger
    • Kopito RR, Lee BS, Simmons DM, et al. Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger. Cell 1989;59:927-37.
    • (1989) Cell , vol.59 , pp. 927-937
    • Kopito, R.R.1    Lee, B.S.2    Simmons, D.M.3
  • 49
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • Dodge JT, Mitchell C, Hanahan DJ. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys 1963;100:119-30.
    • (1963) Arch Biochem Biophys , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 50
    • 0021914750 scopus 로고
    • Partial deficiency of erythrocyte spectrin in hereditary spherocytosis
    • Agre P, Casella JF, Zinkham WH, et al. Partial deficiency of erythrocyte spectrin in hereditary spherocytosis. Nature 1985;314:380-3.
    • (1985) Nature , vol.314 , pp. 380-383
    • Agre, P.1    Casella, J.F.2    Zinkham, W.H.3
  • 51
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G, Steck TL, Wallach DF. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 1971;10:2606-17.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 52
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 54
    • 10544253847 scopus 로고    scopus 로고
    • Terminology for red cell surface antigens - Makuhari report
    • Daniels GL, Anstee DJ, Cartron JP, et al. Terminology for red cell surface antigens - Makuhari report. Vox Sang 1996;71:246-8.
    • (1996) Vox Sang , vol.71 , pp. 246-248
    • Daniels, G.L.1    Anstee, D.J.2    Cartron, J.P.3
  • 56
    • 0027566866 scopus 로고
    • Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen
    • Kay MM. Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen. Cell Mol Biol (Noisy-legrand) 1993;39:131-53.
    • (1993) Cell Mol Biol (Noisy-legrand) , vol.39 , pp. 131-153
    • Kay, M.M.1
  • 57
    • 0021918068 scopus 로고
    • Plasmodium falciparum malaria: Band 3 as a possible receptor during invasion of human erythrocytes
    • Okoye VC, Bennett V. Plasmodium falciparum malaria: band 3 as a possible receptor during invasion of human erythrocytes. Science 1985;227:169-71.
    • (1985) Science , vol.227 , pp. 169-171
    • Okoye, V.C.1    Bennett, V.2
  • 58
    • 0024397422 scopus 로고
    • Naturally occurring anti-band 3 autoantibodies recognize a high molecular weight protein on the surface of Plasmodium falciparum infected erythrocytes
    • Winograd E, Sherman IW. Naturally occurring anti-band 3 autoantibodies recognize a high molecular weight protein on the surface of Plasmodium falciparum infected erythrocytes. Biochem Biophys Res Commun 1989;160:1357-63.
    • (1989) Biochem Biophys Res Commun , vol.160 , pp. 1357-1363
    • Winograd, E.1    Sherman, I.W.2
  • 59
    • 0028210659 scopus 로고
    • Cytoadherence-related neoantigens on Plasmodium falciparum (human malaria)-infected human erythrocytes result from the exposure of normally cryptic regions of the band 3 protein
    • Crandall I, Sherman IW. Cytoadherence-related neoantigens on Plasmodium falciparum (human malaria)-infected human erythrocytes result from the exposure of normally cryptic regions of the band 3 protein. Parasitology 1994;108:257-67.
    • (1994) Parasitology , vol.108 , pp. 257-267
    • Crandall, I.1    Sherman, I.W.2
  • 60
    • 0027215528 scopus 로고
    • Synthetic peptides based on motifs present in human band 3 protein inhibit cytoadherence/sequestration of the malaria parasite Plasmodium falciparum
    • Crandall I, Collins WE, Gysin J, Sherman IW. Synthetic peptides based on motifs present in human band 3 protein inhibit cytoadherence/sequestration of the malaria parasite Plasmodium falciparum. Proc Natl Acad Sci U S A 1993;90:4703-7.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 4703-4707
    • Crandall, I.1    Collins, W.E.2    Gysin, J.3    Sherman, I.W.4
  • 61
    • 0029076411 scopus 로고
    • Cytoadherence-related homologous motifs in Plasmodium falciparum antigen Pf155/RESA and erythrocyte band 3 protein
    • Iqbal J, Siddique AB, Ahlborg N, et al. Cytoadherence-related homologous motifs in Plasmodium falciparum antigen Pf155/RESA and erythrocyte band 3 protein. Parasitology 1995;110:503-11.
    • (1995) Parasitology , vol.110 , pp. 503-511
    • Iqbal, J.1    Siddique, A.B.2    Ahlborg, N.3
  • 62
    • 0029049593 scopus 로고
    • Plasmodium falciparum: Sera of individuals living in a malaria-endemic region recognize peptide motifs of the human erythrocyte anion transport protein
    • Crandall I, Guthrie N, Sherman IW. Plasmodium falciparum: sera of individuals living in a malaria-endemic region recognize peptide motifs of the human erythrocyte anion transport protein. Am J Trop Med Hyg 1995;52:450-5.
    • (1995) Am J Trop Med Hyg , vol.52 , pp. 450-455
    • Crandall, I.1    Guthrie, N.2    Sherman, I.W.3
  • 63
    • 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, et al. 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 1994;62:4362-6.
    • (1994) Infect Immun , vol.62 , pp. 4362-4366
    • Hogh, B.1    Petersen, E.2    Crandall, I.3
  • 64
    • 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 IE, Marini S, et al. 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 1995;144:117-23.
    • (1995) Mol Cell Biochem , vol.144 , pp. 117-123
    • Guthrie, N.1    Crandall, I.E.2    Marini, S.3


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