메뉴 건너뛰기




Volumn 87, Issue 6, 1996, Pages 2538-2545

Hereditary spherocytosis with spectrin deficiency due to an unstable truncated β spectrin

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; ERYTHROCYTE BAND 3 PROTEIN; ERYTHROCYTE BAND 4.2 PROTEIN; MESSENGER RNA; MUTANT PROTEIN; SPECTRIN;

EID: 0029870245     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v87.6.2538.bloodjournal8762538     Document Type: Article
Times cited : (32)

References (53)
  • 1
    • 0020083327 scopus 로고
    • Deficient red-cell spectrin in severe, recessively inherited spherocytosis
    • Agre P, Orringer EP, Bennett V: Deficient red-cell spectrin in severe, recessively inherited spherocytosis. N Engl J Med 306:1155, 1982
    • (1982) N Engl J Med , vol.306 , pp. 1155
    • Agre, P.1    Orringer, E.P.2    Bennett, V.3
  • 2
    • 0022916675 scopus 로고
    • Inheritance pattern and clinical response to splenectomy as a reflection of erythrocyte spectrin deficiency in hereditary spherocytosis
    • Agre P, Asimos A, Casella JF, McMillan D: Inheritance pattern and clinical response to splenectomy as a reflection of erythrocyte spectrin deficiency in hereditary spherocytosis. N Engl J Med 315:1579, 1986
    • (1986) N Engl J Med , vol.315 , pp. 1579
    • Agre, P.1    Asimos, A.2    Casella, J.F.3    McMillan, D.4
  • 3
    • 0026628758 scopus 로고
    • Mutations of the red blood cell membrane proteins: From clinical evaluations to detection of the underlying genetic defect
    • Palek J, Sahr KE. Mutations of the red blood cell membrane proteins: From clinical evaluations to detection of the underlying genetic defect. Blood 80:308, 1992
    • (1992) Blood , vol.80 , pp. 308
    • Palek, J.1    Sahr, K.E.2
  • 4
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett V, Gilligan DM: The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol 9:27, 1993
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 27
    • Bennett, V.1    Gilligan, D.M.2
  • 7
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher DW, Marchesi VT: Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311:177, 1984
    • (1984) Nature , vol.311 , pp. 177
    • Speicher, D.W.1    Marchesi, V.T.2
  • 9
    • 0020288393 scopus 로고
    • A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains
    • Speicher DW, Morrow JS, Knowles WJ, Marchesi VT. A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains. J Biol Chem 257:9093, 1982
    • (1982) J Biol Chem , vol.257 , pp. 9093
    • Speicher, D.W.1    Morrow, J.S.2    Knowles, W.J.3    Marchesi, V.T.4
  • 10
    • 0026653822 scopus 로고
    • Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site
    • Speicher DW, Weglarz L, DeSilva TM: Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J Biol Chem 267:14775, 1992
    • (1992) J Biol Chem , vol.267 , pp. 14775
    • Speicher, D.W.1    Weglarz, L.2    DeSilva, T.M.3
  • 11
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythoid and nonerythroid β-spectrin
    • Kennedy SP, Warren SL, Forget BG, Morrow JS: Ankyrin binds to the 15th repetitive unit of erythoid and nonerythroid β-spectrin. J Cell Biol 115:267, 1991
    • (1991) J Cell Biol , vol.115 , pp. 267
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.G.3    Morrow, J.S.4
  • 12
    • 0021914750 scopus 로고
    • Partial deficiency of erythrocyte spectrin in hereditary spherocytosis
    • Agre P, Casella JF, Zinkham WH: Partial deficiency of erythrocyte spectrin in hereditary spherocytosis. Nature 314:380, 1985
    • (1985) Nature , vol.314 , pp. 380
    • Agre, P.1    Casella, J.F.2    Zinkham, W.H.3
  • 14
    • 0027490813 scopus 로고
    • Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis
    • Savvides P, Shalev O, John KM, Lux SE: Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis. Blood 82:2953, 1993
    • (1993) Blood , vol.82 , pp. 2953
    • Savvides, P.1    Shalev, O.2    John, K.M.3    Lux, S.E.4
  • 16
    • 0342430428 scopus 로고
    • A subset of patients with dominantly inherited hereditary spherocytosis has a marked deficiency of the band 3 protein
    • abstr
    • Jarolim P, Ruff P, Coetzer TL, Prchal JT, Batlas SK, Poon M, Barbec V, Palek J: A subset of patients with dominantly inherited hereditary spherocytosis has a marked deficiency of the band 3 protein. Blood 76:37a, 1990 (suppl, abstr)
    • (1990) Blood , vol.76 , Issue.SUPPL.
    • Jarolim, P.1    Ruff, P.2    Coetzer, T.L.3    Prchal, J.T.4    Batlas, S.K.5    Poon, M.6    Barbec, V.7    Palek, J.8
  • 21
    • 0025217072 scopus 로고
    • A genetic defect of erythrocytc band 4.2 protein associated with hereditary spherocytosis
    • Ideguchi H, Nishimura J, Nawata H, Hamasaki N: A genetic defect of erythrocytc band 4.2 protein associated with hereditary spherocytosis. Br J Haematol 74:347, 1990
    • (1990) Br J Haematol , vol.74 , pp. 347
    • Ideguchi, H.1    Nishimura, J.2    Nawata, H.3    Hamasaki, N.4
  • 22
    • 0023867132 scopus 로고
    • Deficiency of protein 4.2 in erythrocytes from a patient with a Coombs negative hemolytic anemia
    • Rybicki AC, Heath R, WolfJ L, Lubin B, Schwartz RS: Deficiency of protein 4.2 in erythrocytes from a patient with a Coombs negative hemolytic anemia. J Clin Invest 81:893, 1988
    • (1988) J Clin Invest , vol.81 , pp. 893
    • Rybicki, A.C.1    Heath, R.2    Wolfj, L.3    Lubin, B.4    Schwartz, R.S.5
  • 26
    • 6844257056 scopus 로고
    • Discovery of 8 ankyrin mutations in hereditary spherocytosis (HS) indicates that ankyrin defects arc a major cause of dominant and recessive HS
    • abstr
    • Eber SW, Lux ML, Gonzalez JM, Scarpa A, Tse WT, Gallagher PG, Pekrun A, Forget BG, Lux SE: Discovery of 8 ankyrin mutations in hereditary spherocytosis (HS) indicates that ankyrin defects arc a major cause of dominant and recessive HS. Blood 82:3089a, 1993 (abstr, suppl 1)
    • (1993) Blood , vol.82 , Issue.1 SUPPL.
    • Eber, S.W.1    Lux, M.L.2    Gonzalez, J.M.3    Scarpa, A.4    Tse, W.T.5    Gallagher, P.G.6    Pekrun, A.7    Forget, B.G.8    Lux, S.E.9
  • 27
    • 0023582256 scopus 로고
    • Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors
    • abstr
    • Hanspal M, Patek J: Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors. J Cell Biol 105:1417, 1987 (abstr)
    • (1987) J Cell Biol , vol.105 , pp. 1417
    • Hanspal, M.1    Patek, J.2
  • 28
    • 0026747194 scopus 로고
    • Asynchronous synthesis of membrane skeletal proteins during terminal maturation of murine erythroblasts
    • Hanspal M, Hanspal J, Kalraiya R: Asynchronous synthesis of membrane skeletal proteins during terminal maturation of murine erythroblasts. Blood 80:530, 1992
    • (1992) Blood , vol.80 , pp. 530
    • Hanspal, M.1    Hanspal, J.2    Kalraiya, R.3
  • 29
    • 0022362442 scopus 로고
    • Degradation of unassembled a and β spectrin by distinct intracellular pathways: Regulation of spectrin topogenesis by β spectrin degradation
    • Woods CM, Lazarides E. Degradation of unassembled a and β spectrin by distinct intracellular pathways: Regulation of spectrin topogenesis by β spectrin degradation. Cell 40:959, 1985
    • (1985) Cell , vol.40 , pp. 959
    • Woods, C.M.1    Lazarides, E.2
  • 30
    • 13344296461 scopus 로고
    • Identification of the molecular defect of β spectrin in autosomal dominant hereditary spherocytosis (HS) associated with defective binding of protein 4.1, HS(Sp-4.1)
    • abstr
    • Becker PS, Tse WT, Lux SE, Forget BG: Identification of the molecular defect of β spectrin in autosomal dominant hereditary spherocytosis (HS) associated with defective binding of protein 4.1, HS(Sp-4.1). Blood 76:25a, 1990 (suppl, abstr)
    • (1990) Blood , vol.76 , Issue.SUPPL.
    • Becker, P.S.1    Tse, W.T.2    Lux, S.E.3    Forget, B.G.4
  • 31
    • 0027328064 scopus 로고
    • β Spectrin Kissimmee - A spectrin variant associated with autosomal dominant hereditary spherocytosis and defective binding to protein 4.1
    • Becker PS, Tse WT, Lux SE, Forget BG: β Spectrin Kissimmee - A spectrin variant associated with autosomal dominant hereditary spherocytosis and defective binding to protein 4.1. J Clin Invest 92:612, 1993
    • (1993) J Clin Invest , vol.92 , pp. 612
    • Becker, P.S.1    Tse, W.T.2    Lux, S.E.3    Forget, B.G.4
  • 32
    • 13344252212 scopus 로고
    • A deletion within the β spectrin gene associated with a truncated protein and resulting in hereditary spherocytosis: β spectrin Durham
    • abstr
    • Hassoun H, Vassiliadis JN, Murray J, Yi SJ, Hanspal M, Ware RE, Winter SS, Chiou S, Palek J: A deletion within the β spectrin gene associated with a truncated protein and resulting in hereditary spherocytosis: β spectrin Durham. Blood 84.4a, 1994 (abstr)
    • (1994) Blood , vol.84
    • Hassoun, H.1    Vassiliadis, J.N.2    Murray, J.3    Yi, S.J.4    Hanspal, M.5    Ware, R.E.6    Winter, S.S.7    Chiou, S.8    Palek, J.9
  • 33
    • 0022651111 scopus 로고
    • Partial spectrin deficiency in hereditary pyropoikilocytosis
    • Coetzer TL, Palek J: Partial spectrin deficiency in hereditary pyropoikilocytosis. Blood 67:919, 1986
    • (1986) Blood , vol.67 , pp. 919
    • Coetzer, T.L.1    Palek, J.2
  • 34
    • 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 100:119, 1963
    • (1963) Arch Biochem Biophys , vol.100 , pp. 119
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 35
    • 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 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 36
    • 0019374012 scopus 로고
    • Altered spectrin dimer-dimer association and instability of erythrocyte membrane skeletons in hereditary pyropoikilocytosis
    • Liu SC, Palek J, Prchal JT, Castleberry P: Altered spectrin dimer-dimer association and instability of erythrocyte membrane skeletons in hereditary pyropoikilocytosis. J Clin Invest 68:597, 1981
    • (1981) J Clin Invest , vol.68 , pp. 597
    • Liu, S.C.1    Palek, J.2    Prchal, J.T.3    Castleberry, P.4
  • 37
    • 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
  • 38
    • 0020841311 scopus 로고
    • DNA in heritable diseases
    • Sykes BJ: DNA in heritable diseases. Lancet 2:787, 1983
    • (1983) Lancet , vol.2 , pp. 787
    • Sykes, B.J.1
  • 40
    • 0028211009 scopus 로고
    • PCR amplification of up to 35-kb DNA with high fidelity and high yield from bacteriophage templates
    • Barnes WM: PCR amplification of up to 35-kb DNA with high fidelity and high yield from bacteriophage templates. Proc Natl Acad Sci USA 91:2216, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2216
    • Barnes, W.M.1
  • 43
    • 0024581574 scopus 로고
    • Proliferation and maturation of human erythroid progenitors in liquid culture
    • Fibach E, Manor D, Oppenheim A, Rachmilewitz EA: Proliferation and maturation of human erythroid progenitors in liquid culture. Blood 73:100, 1989
    • (1989) Blood , vol.73 , pp. 100
    • Fibach, E.1    Manor, D.2    Oppenheim, A.3    Rachmilewitz, E.A.4
  • 44
    • 0018382303 scopus 로고
    • Molecular changes in the membranes of mouse erythroid cells accompanying differentiation
    • Geiduschek JB, Singer SJ: Molecular changes in the membranes of mouse erythroid cells accompanying differentiation. Cell 16:149, 1979
    • (1979) Cell , vol.16 , pp. 149
    • Geiduschek, J.B.1    Singer, S.J.2
  • 45
    • 0018849207 scopus 로고
    • Quantitation of spectrin-containing erythroid precursor cells in normal and perturbed erythropoiesis
    • Hasthorpe S: Quantitation of spectrin-containing erythroid precursor cells in normal and perturbed erythropoiesis. Exp Hematol 8:1001, 1980
    • (1980) Exp Hematol , vol.8 , pp. 1001
    • Hasthorpe, S.1
  • 46
    • 0021704597 scopus 로고
    • Spectrin deficient inherited hemolytic anemias in the mouse: Characterization by spectrin synthesis and mRNA activity in reticulocytes
    • Bodine DM, Birkenmeier CS, Barker JE: Spectrin deficient inherited hemolytic anemias in the mouse: Characterization by spectrin synthesis and mRNA activity in reticulocytes. Cell 37:721, 1984
    • (1984) Cell , vol.37 , pp. 721
    • Bodine, D.M.1    Birkenmeier, C.S.2    Barker, J.E.3
  • 47
    • 0026083898 scopus 로고
    • Molecular basis of spectrin and ankyrin deficiencies in severe hereditary spherocytosis: Evidence implicating a primary defect of ankyrin
    • Hanspal M, Yoon S, Yu H, Hanspal JS, Lambert S, Palek J, Prchal J: Molecular basis of spectrin and ankyrin deficiencies in severe hereditary spherocytosis: Evidence implicating a primary defect of ankyrin. Blood 77:165, 1991
    • (1991) Blood , vol.77 , pp. 165
    • Hanspal, M.1    Yoon, S.2    Yu, H.3    Hanspal, J.S.4    Lambert, S.5    Palek, J.6    Prchal, J.7
  • 48
    • 0020551681 scopus 로고
    • β-Spectrin limits α-spectrin assembly on membranes following synthesis in a chicken erythroid cell lysate
    • Moon RT, Lazarides E: β-Spectrin limits α-spectrin assembly on membranes following synthesis in a chicken erythroid cell lysate. Nature 305:62, 1983
    • (1983) Nature , vol.305 , pp. 62
    • Moon, R.T.1    Lazarides, E.2
  • 49
    • 0028149097 scopus 로고
    • The murine mutation jaundiced is caused by replacement of an arginine with a stop codon in the mRNA encoding the ninth repeat of β spectrin
    • Bloom ML, Kaysser TM, Birkenmeier CS, Barker JE: The murine mutation jaundiced is caused by replacement of an arginine with a stop codon in the mRNA encoding the ninth repeat of β spectrin. Proc Natl Acad Sci USA 91:10099, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10099
    • Bloom, M.L.1    Kaysser, T.M.2    Birkenmeier, C.S.3    Barker, J.E.4
  • 50
    • 0028222873 scopus 로고
    • Construction of a novel database containing aberrant splicing mutations of mammalian genes
    • Nakai K, Sakamoto H: Construction of a novel database containing aberrant splicing mutations of mammalian genes. Gene 141:171, 1994
    • (1994) Gene , vol.141 , pp. 171
    • Nakai, K.1    Sakamoto, H.2
  • 51
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget SM: Exon recognition in vertebrate splicing. J Biol Chem 270:2411, 1995
    • (1995) J Biol Chem , vol.270 , pp. 2411
    • Berget, S.M.1
  • 52
    • 0028282980 scopus 로고
    • A sequence compilation and comparison of exons that are alternatively spliced in neurons
    • Stamm S, Zhang MQ, Marr TG, Helfman D: A sequence compilation and comparison of exons that are alternatively spliced in neurons. Nucleic Acids Res 22:1515, 1994
    • (1994) Nucleic Acids Res , vol.22 , pp. 1515
    • Stamm, S.1    Zhang, M.Q.2    Marr, T.G.3    Helfman, D.4
  • 53
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro MB, Senapathy P: RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression. Nucleic Acids Res 15:7155, 1987
    • (1987) Nucleic Acids Res , vol.15 , pp. 7155
    • Shapiro, M.B.1    Senapathy, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.