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Volumn 88, Issue 12, 1996, Pages 4500-4509

Identification of the proximal erythroid promoter region of the mouse anion exchanger gene

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ANION EXCHANGE; ARTICLE; CONTROLLED STUDY; ERYTHROID CELL; GENETIC ANALYSIS; GENETIC TRANSCRIPTION; MOUSE; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROMOTER REGION; RNA ANALYSIS; TRANSCRIPTION INITIATION;

EID: 0029988266     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v88.12.4500.bloodjournal88124500     Document Type: Article
Times cited : (26)

References (50)
  • 1
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger (AE1)
    • Tanner MJA: Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Semin Hematol 30:34, 1993
    • (1993) Semin Hematol , vol.30 , pp. 34
    • Tanner, M.J.A.1
  • 2
    • 0016226796 scopus 로고
    • The organization of proteins in the human red cell membrane
    • Steck TL: The organization of proteins in the human red cell membrane. J Cell Biol 62:1, 1974
    • (1974) J Cell Biol , vol.62 , pp. 1
    • Steck, T.L.1
  • 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 316:234, 1985
    • (1985) Nature , vol.316 , pp. 234
    • 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 MJA, Martin PG, High S: The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence. Biochem J 256:703, 1988
    • (1988) Biochem J , vol.256 , pp. 703
    • Tanner, M.J.A.1    Martin, P.G.2    High, S.3
  • 5
    • 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 USA 86:9089, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9089
    • Lux, S.E.1    John, K.M.2    Kopito, R.R.3    Lodish, H.F.4
  • 6
    • 0019321291 scopus 로고
    • Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane
    • Bennett V, Stenbuck PJ: Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane. J Biol Chem 255:6424, 1980
    • (1980) J Biol Chem , vol.255 , pp. 6424
    • Bennett, V.1    Stenbuck, P.J.2
  • 7
    • 10544255610 scopus 로고
    • The spectrin-actin junction of erythrocyte membrane skeletons
    • Bennett V: The spectrin-actin junction of erythrocyte membrane skeletons. Biochim Biophys Acta 689:475, 1989
    • (1989) Biochim Biophys Acta , vol.689 , pp. 475
    • Bennett, V.1
  • 8
    • 0021940465 scopus 로고
    • Interactions between protein 4.1 and band 3: An alternative binding site for an element of the membrane skeleton
    • Pasternack GR, Anderson RA, Leto TL, Marchesi VT: Interactions between protein 4.1 and band 3: An alternative binding site for an element of the membrane skeleton. J Biol Chem 260:3676, 1985
    • (1985) J Biol Chem , vol.260 , pp. 3676
    • Pasternack, G.R.1    Anderson, R.A.2    Leto, T.L.3    Marchesi, V.T.4
  • 9
    • 0023766055 scopus 로고
    • Associations of human erythrocyte band 4.2: Binding to ankyrin and to the cytoplasmic domain of band 3
    • Korsgren C, Cohen CM: Associations of human erythrocyte band 4.2: Binding to ankyrin and to the cytoplasmic domain of band 3. J Biol Chem 263:10212, 1988
    • (1988) J Biol Chem , vol.263 , pp. 10212
    • Korsgren, C.1    Cohen, C.M.2
  • 10
    • 0025896582 scopus 로고
    • Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability
    • Low PS, Willardson BM, Mohandas N: Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability. Blood 77:1581, 1991
    • (1991) Blood , vol.77 , pp. 1581
    • Low, P.S.1    Willardson, B.M.2    Mohandas, N.3
  • 11
    • 0022922389 scopus 로고
    • Structure and function of the cytoplasmic domain of band 3: Center of erythrocyte membrane-peripheral protein interactions
    • Low PS: Structure and function of the cytoplasmic domain of band 3: Center of erythrocyte membrane-peripheral protein interactions. Biochim Biophys Acta 864:145, 1986
    • (1986) Biochim Biophys Acta , vol.864 , pp. 145
    • Low, P.S.1
  • 12
    • 0023726261 scopus 로고
    • Localization of the carboxyl terminus of band 3 to the cytoplasmic side of the erythrocyte membrane using antibodies raised against a synthetic peptide
    • Lieberman DM, Reithmeier RAF: Localization of the carboxyl terminus of band 3 to the cytoplasmic side of the erythrocyte membrane using antibodies raised against a synthetic peptide. J Biol Chem 263:10022, 1988
    • (1988) J Biol Chem , vol.263 , pp. 10022
    • Lieberman, D.M.1    Reithmeier, R.A.F.2
  • 13
    • 0022411389 scopus 로고
    • Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney
    • Drenckhahn D, Schlüter K, Allen DP, Bennett V: Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney. Science 230:1287, 1985
    • (1985) Science , vol.230 , pp. 1287
    • Drenckhahn, D.1    Schlüter, K.2    Allen, D.P.3    Bennett, V.4
  • 14
    • 0023490109 scopus 로고
    • Restriction of the human kidney band 3-like anion exchanger to specialized subdomains of the basolateral plasma membrane of intercalated cells
    • Drenckhahn D, Merte C: Restriction of the human kidney band 3-like anion exchanger to specialized subdomains of the basolateral plasma membrane of intercalated cells. Eur J Cell Biol 45:107, 1987
    • (1987) Eur J Cell Biol , vol.45 , pp. 107
    • Drenckhahn, D.1    Merte, C.2
  • 15
    • 0023583790 scopus 로고
    • Changes in erythroid membrane proteins during erythropoietin-mediated terminal differentiation
    • Koury MJ, Bondurant MC, Rana SS: Changes in erythroid membrane proteins during erythropoietin-mediated terminal differentiation. J Cell Physiol 133:438, 1987
    • (1987) J Cell Physiol , vol.133 , pp. 438
    • Koury, M.J.1    Bondurant, M.C.2    Rana, S.S.3
  • 16
    • 0026768754 scopus 로고
    • The expression and synthesis of band 3 protein initiates the formation of a stable membrane skeleton in murine Rauscher-transformed erythroid cells
    • Hanspal M, Hanspal JS, Kalraiya R, Palek J: The expression and synthesis of band 3 protein initiates the formation of a stable membrane skeleton in murine Rauscher-transformed erythroid cells. Eur J Cell Biol 58:313, 1992
    • (1992) Eur J Cell Biol , vol.58 , pp. 313
    • Hanspal, M.1    Hanspal, J.S.2    Kalraiya, R.3    Palek, J.4
  • 17
    • 0021605962 scopus 로고
    • Assembly and topogenesis of the spectrin-based membrane skeleton in erythroid development
    • Lazarides E, Moon RT: Assembly and topogenesis of the spectrin-based membrane skeleton in erythroid development. Cell 37:354, 1984
    • (1984) Cell , vol.37 , pp. 354
    • Lazarides, E.1    Moon, R.T.2
  • 18
    • 0026775240 scopus 로고
    • Biogenesis of normal and abnormal red blood cell membrane skeleton
    • Hanspal M, Palek J: Biogenesis of normal and abnormal red blood cell membrane skeleton. Semin Hematol 29:305, 1992
    • (1992) Semin Hematol , vol.29 , pp. 305
    • Hanspal, M.1    Palek, J.2
  • 19
    • 0023424369 scopus 로고
    • Specific pattern of gene expression during induction of mouse erythroleukemia cells
    • Fraser PJ, Curtis PJ: Specific pattern of gene expression during induction of mouse erythroleukemia cells. Genes Dev 1:855, 1987
    • (1987) Genes Dev , vol.1 , pp. 855
    • Fraser, P.J.1    Curtis, P.J.2
  • 20
    • 0023655074 scopus 로고
    • Structure and organization of the murine band 3 gene
    • Kopito RR, Andersson M, Lodish HF: Structure and organization of the murine band 3 gene. J Biol Chem 262:8035, 1987
    • (1987) J Biol Chem , vol.262 , pp. 8035
    • Kopito, R.R.1    Andersson, M.2    Lodish, H.F.3
  • 21
    • 0021972927 scopus 로고
    • Structure of the murine anion exchanger protein
    • Kopito RR, Lodish HF: Structure of the murine anion exchanger protein. J Cell Biochem 29:1, 1985
    • (1985) J Cell Biochem , vol.29 , pp. 1
    • Kopito, R.R.1    Lodish, H.F.2
  • 22
    • 0023551464 scopus 로고
    • Multiple tissue-specific sites of transcriptional initiation of the mouse anion antiport gene in erythroid and renal cells
    • Kopito RR, Andersson MA, Lodish HF: Multiple tissue-specific sites of transcriptional initiation of the mouse anion antiport gene in erythroid and renal cells. Proc Natl Acad Sci USA 84:7149, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7149
    • Kopito, R.R.1    Andersson, M.A.2    Lodish, H.F.3
  • 23
    • 0024383334 scopus 로고
    • The major kidney band 3 gene transcript predicts an amino-terminal truncated band 3 polypeptide
    • Brosius FC, Alper SL, Garcia AM, Lodish HF: The major kidney band 3 gene transcript predicts an amino-terminal truncated band 3 polypeptide. J Biol Chem 264:7784, 1989
    • (1989) J Biol Chem , vol.264 , pp. 7784
    • Brosius, F.C.1    Alper, S.L.2    Garcia, A.M.3    Lodish, H.F.4
  • 25
    • 0021752389 scopus 로고
    • Splenic erythroblasts in anemia-inducing Friend disease: A source of cells for studies of erythropoietin-mediated differentiation
    • Koury MJ, Sawyer ST, Bondurant MC: Splenic erythroblasts in anemia-inducing Friend disease: A source of cells for studies of erythropoietin-mediated differentiation. J Cell Physiol 121:526, 1984
    • (1984) J Cell Physiol , vol.121 , pp. 526
    • Koury, M.J.1    Sawyer, S.T.2    Bondurant, M.C.3
  • 26
    • 0026747194 scopus 로고
    • Asynchronous synthesis of membrane skeleton proteins during terminal maturation of murine erythroblasts
    • Hanspal M, Hanspal JS, Kalraiya R, Liu S-C, Sahr KE, Howard D, Palek J: Asynchronous synthesis of membrane skeleton proteins during terminal maturation of murine erythroblasts. Blood 80:530, 1992
    • (1992) Blood , vol.80 , pp. 530
    • Hanspal, M.1    Hanspal, J.S.2    Kalraiya, R.3    Liu, S.-C.4    Sahr, K.E.5    Howard, D.6    Palek, J.7
  • 27
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin JM, Przbyla AE, MacDonald RJ, Rutter WJ: Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294, 1979
    • (1979) Biochemistry , vol.18 , pp. 5294
    • Chirgwin, J.M.1    Przbyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 28
    • 10544240646 scopus 로고
    • The effects of erythropoietin on biosynthesis of translatable globin mRNA
    • Goldwasser E (ed): New York, NY, Elsevier Science
    • Sahr K, Goldwasser E: The effects of erythropoietin on biosynthesis of translatable globin mRNA, in Goldwasser E (ed): Regulation of Hemoglobin Biosynthesis. New York, NY, Elsevier Science, 1983, p 153
    • (1983) Regulation of Hemoglobin Biosynthesis , pp. 153
    • Sahr, K.1    Goldwasser, E.2
  • 29
    • 0019738069 scopus 로고
    • DNA analysis in the diagnosis of hemoglobin disorders
    • Goossens M, Kan YW: DNA analysis in the diagnosis of hemoglobin disorders. Methods Enzymol 76:805, 1981
    • (1981) Methods Enzymol , vol.76 , pp. 805
    • Goossens, M.1    Kan, Y.W.2
  • 30
    • 0026625655 scopus 로고
    • Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C
    • GuptaRoy B, Cohen CM: Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C. J Biol Chem 267:15326, 1992
    • (1992) J Biol Chem , vol.267 , pp. 15326
    • GuptaRoy, B.1    Cohen, C.M.2
  • 31
    • 0024212067 scopus 로고
    • A Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman MA, Dush MK, Martin GR: A Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85:8998, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8998
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 32
    • 0024492484 scopus 로고
    • Polymerase chain reaction with single-sided specificity: Analysis of T cell receptor δ chain
    • Loh EY, Elliott JF, Cwirla S, Lanier LL, Davis MM: Polymerase chain reaction with single-sided specificity: Analysis of T cell receptor δ chain. Science 243:217, 1989
    • (1989) Science , vol.243 , pp. 217
    • Loh, E.Y.1    Elliott, J.F.2    Cwirla, S.3    Lanier, L.L.4    Davis, M.M.5
  • 35
    • 0023687042 scopus 로고
    • A simple phase-extraction assay for chloramphenicol acyltransferase activity
    • Seed B, Sheen J-Y. A simple phase-extraction assay for chloramphenicol acyltransferase activity. Gene 67:271, 1988
    • (1988) Gene , vol.67 , pp. 271
    • Seed, B.1    Sheen, J.-Y.2
  • 36
    • 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 264:8185, 1989
    • (1989) J Biol Chem , vol.264 , pp. 8185
    • Kudrycki, K.E.1    Shull, G.E.2
  • 37
    • 0027533902 scopus 로고
    • - exchanger mRNA is transcribed from an alternative promoter
    • - exchanger mRNA is transcribed from an alternative promoter. Am J Physiol 264:F540, 1993
    • (1993) Am J Physiol , vol.264
    • Kudrycki, K.E.1    Shull, G.E.2
  • 38
    • 0027740329 scopus 로고
    • Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus
    • Kollert-Jöns A, Wagner S, Hübner S, Appelhans H, Drenckhahn D: Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus. Am J Physiol 265:F813, 1993
    • (1993) Am J Physiol , vol.265
    • Kollert-Jöns, A.1    Wagner, S.2    Hübner, S.3    Appelhans, H.4    Drenckhahn, D.5
  • 39
    • 0023713201 scopus 로고
    • Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression
    • Chretien S, Dubart A, Beaupain D, Raich N, Grandchamp B, Rosa J, Goossens M, Romeo P-H: Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. Proc Natl Acad Sci USA 85:6, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6
    • Chretien, S.1    Dubart, A.2    Beaupain, D.3    Raich, N.4    Grandchamp, B.5    Rosa, J.6    Goossens, M.7    Romeo, P.-H.8
  • 40
    • 0000976220 scopus 로고
    • Cis- and transacting elements involved in the regulation of the erythroid promoter of the human porphobilinogen deaminase gene
    • Mignotte V, Eleouet JF, Raich N, Romeo P-H: Cis- and transacting elements involved in the regulation of the erythroid promoter of the human porphobilinogen deaminase gene. Proc Natl Acad Sci USA 86:6548, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6548
    • Mignotte, V.1    Eleouet, J.F.2    Raich, N.3    Romeo, P.-H.4
  • 42
    • 0024348561 scopus 로고
    • Regulated expression of the overlapping ubiquitous and erythroid transcription units of the human porphobilinogen deaminase (PBG-D) gene introduced into non-erythroid and erythroid cells
    • Raich N, Mignotte V, Dubart A, Beaupain D, Leboulch Ph, Romana M, Chabret C. Charnay P, Papayannopoulou T, Goossens M, Romeo PH: Regulated expression of the overlapping ubiquitous and erythroid transcription units of the human porphobilinogen deaminase (PBG-D) gene introduced into non-erythroid and erythroid cells. J Biol Chem 264:10186, 1989
    • (1989) J Biol Chem , vol.264 , pp. 10186
    • Raich, N.1    Mignotte, V.2    Dubart, A.3    Beaupain, D.4    Leboulch, Ph.5    Romana, M.6    Chabret, C.7    Charnay, P.8    Papayannopoulou, T.9    Goossens, M.10    Romeo, P.H.11
  • 43
    • 0028915871 scopus 로고
    • Variant chicken AE1 anion exchangers possess divergent NH2-terminal cytoplasmic domains
    • Cox KH, Cox JV: Variant chicken AE1 anion exchangers possess divergent NH2-terminal cytoplasmic domains. Am J Physiol 268:F503, 1995
    • (1995) Am J Physiol , vol.268
    • Cox, K.H.1    Cox, J.V.2
  • 44
    • 0028585820 scopus 로고
    • The structure and organization of the human erythroid anion exchanger (AE1) gene
    • Sahr KE, Taylor WM, Daniels BP, Rubin HL, Jarolim P: The structure and organization of the human erythroid anion exchanger (AE1) gene. Genomics 24:491, 1994
    • (1994) Genomics , vol.24 , pp. 491
    • Sahr, K.E.1    Taylor, W.M.2    Daniels, B.P.3    Rubin, H.L.4    Jarolim, P.5
  • 45
    • 0028065446 scopus 로고
    • The structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene
    • Schofield AE, Martin PG, Spillett D, Tanner MJA: The structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene. Blood 84:2000, 1994
    • (1994) Blood , vol.84 , pp. 2000
    • Schofield, A.E.1    Martin, P.G.2    Spillett, D.3    Tanner, M.J.A.4
  • 46
    • 0028925734 scopus 로고
    • Transcription factors and hematopoietic development
    • Orkin SH: Transcription factors and hematopoietic development. J Biol Chem 270:4955, 1995
    • (1995) J Biol Chem , vol.270 , pp. 4955
    • Orkin, S.H.1
  • 47
    • 0345184762 scopus 로고
    • An erythrocyte-specific DNA-binding factor recognizes a regulatory sequence common to all chicken globin genes
    • Evans T, Reitman M, Felsenfeld G: An erythrocyte-specific DNA-binding factor recognizes a regulatory sequence common to all chicken globin genes. Proc Natl Acad Sci USA 85:5976, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5976
    • Evans, T.1    Reitman, M.2    Felsenfeld, G.3
  • 48
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughter-less, MyoD, and myc proteins
    • Murre C, McCaw PS, Baltimore D: A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughter-less, MyoD, and myc proteins. Cell 56:777, 1989
    • (1989) Cell , vol.56 , pp. 777
    • Murre, C.1    McCaw, P.S.2    Baltimore, D.3
  • 49
    • 0024848239 scopus 로고
    • Developmental modulation of protein binding to β-globin gene regulatory sites within chicken erythrocyte nuclei
    • Jackson PD, Evans T, Nickol JM, Felsenfeld G: Developmental modulation of protein binding to β-globin gene regulatory sites within chicken erythrocyte nuclei. Genes Dev 3:1860, 1989
    • (1989) Genes Dev , vol.3 , pp. 1860
    • Jackson, P.D.1    Evans, T.2    Nickol, J.M.3    Felsenfeld, G.4
  • 50
    • 0024534370 scopus 로고
    • Two tissue-specific factors bind the erythroid promoter of the human porphobilinogen deaminase gene
    • Mignotte V, Wall L, deBoer E, Grosveld F, Romeo P-H: Two tissue-specific factors bind the erythroid promoter of the human porphobilinogen deaminase gene. Nucleic Acids Res 17:37, 1989
    • (1989) Nucleic Acids Res , vol.17 , pp. 37
    • Mignotte, V.1    Wall, L.2    DeBoer, E.3    Grosveld, F.4    Romeo, P.-H.5


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