메뉴 건너뛰기




Volumn 23, Issue 3, 1997, Pages 417-421

Hematologically important mutations: Band 3 and protein 4.2 variants in hereditary spherocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ERYTHROCYTE MEMBRANE; GENE MUTATION; HEREDITARY SPHEROCYTOSIS; HUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION;

EID: 0031417692     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1006/bcmd.1997.0160     Document Type: Article
Times cited : (30)

References (37)
  • 1
    • 0142050379 scopus 로고
    • Disorders of the red cell membrane skeleton: Hereditary spherocytosis and hereditary elliptocytosis
    • New York: McGraw-Hill. p. 529-632
    • Becker P, Lux S. Disorders of the red cell membrane skeleton: Hereditary spherocytosis and hereditary elliptocytosis. The Metabolic Basis of Inherited Disease. 1995;McGraw-Hill, New York. p. 529-632.
    • (1995) The Metabolic Basis of Inherited Disease
    • Becker, P.1    Lux, S.2
  • 2
    • 0030971683 scopus 로고    scopus 로고
    • Molecular basis of erythrocyte membrane disorders
    • Gallagher P G, Ferriera J D. Molecular basis of erythrocyte membrane disorders. Curr Opin Hematol. 4:1997;128-135.
    • (1997) Curr Opin Hematol , vol.4 , pp. 128-135
    • Gallagher, P.G.1    Ferriera, J.D.2
  • 3
    • 0029825262 scopus 로고    scopus 로고
    • Hereditary spherocytosis: A review of the clinical and molecular aspects of the disease
    • Hassoun H, Palek J. Hereditary spherocytosis: a review of the clinical and molecular aspects of the disease. Blood Rev. 10:1996;129-147.
    • (1996) Blood Rev , vol.10 , pp. 129-147
    • Hassoun, H.1    Palek, J.2
  • 4
    • 0029084972 scopus 로고
    • Genetic disorders of the red cell membranes
    • Delaunay J. Genetic disorders of the red cell membranes. FEBS Lett. 369:1995;34-37.
    • (1995) FEBS Lett , vol.369 , pp. 34-37
    • Delaunay, J.1
  • 5
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • R. I Handin, S. E Lux, & T. P Stossel. Philadelphia: JB Lippincott
    • Lux S E, Palek J. Disorders of the red cell membrane. Handin R I, Lux S E, Stossel T P. Blood: Principles and Practice of Hematology. 1995;1701-1816 JB Lippincott, Philadelphia.
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1816
    • Lux, S.E.1    Palek, J.2
  • 6
    • 0027429066 scopus 로고
    • Clinical expression and laboratory detection of red blood cell membrane protein mutations
    • Palek J, Jarolim P. Clinical expression and laboratory detection of red blood cell membrane protein mutations. Semin Hematol. 30:1993;249-283.
    • (1993) Semin Hematol , vol.30 , pp. 249-283
    • Palek, J.1    Jarolim, P.2
  • 7
    • 0028298801 scopus 로고
    • B and 3 protein: Structure, flexibility and function
    • Wang D N. B and 3 protein: structure, flexibility and function. FEBS Lett. 346:1994;26-31.
    • (1994) FEBS Lett , vol.346 , pp. 26-31
    • Wang, D.N.1
  • 8
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger (AE1)
    • Tanner M J. Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Semin Hematol. 30:1993;34-57.
    • (1993) Semin Hematol , vol.30 , pp. 34-57
    • Tanner, M.J.1
  • 9
    • 0142064871 scopus 로고    scopus 로고
    • Structure-function relationships of band 3 variants
    • Bruce L J, Tanner M J. Structure-function relationships of band 3 variants. Cell Mol Biol (Noisy-Le-Grand). 42:1996;953-973.
    • (1996) Cell Mol Biol (Noisy-Le-Grand) , vol.42 , pp. 953-973
    • Bruce, L.J.1    Tanner, M.J.2
  • 10
    • 0028209353 scopus 로고
    • Red cell membrane protein band 4.2: Phenotypic, genetic and electron microscopic aspects
    • Yawata Y. Red cell membrane protein band 4.2: phenotypic, genetic and electron microscopic aspects. Biochim Biophys Acta. 1204:1994;131-148.
    • (1994) Biochim Biophys Acta , vol.1204 , pp. 131-148
    • Yawata, Y.1
  • 11
    • 0027288548 scopus 로고
    • Human erythrocyte membrane protein band 4.2 (pallidin)
    • Cohen C M, Dotimas E, Korsgren C. Human erythrocyte membrane protein band 4.2 (pallidin). Semin Hematol. 30:1993;119-137.
    • (1993) Semin Hematol , vol.30 , pp. 119-137
    • Cohen, C.M.1    Dotimas, E.2    Korsgren, C.3
  • 12
    • 0026696751 scopus 로고
    • Band 3 Tuscaloosa: Pro327 - -Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2
    • Jarolim P, Palek J, Rubin H L, Prchal J T, Korsgren C, Cohen C M. Band 3 Tuscaloosa: Pro327 - -Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2. Blood. 80:1992;523-529.
    • (1992) Blood , vol.80 , pp. 523-529
    • Jarolim, P.1    Palek, J.2    Rubin, H.L.3    Prchal, J.T.4    Korsgren, C.5    Cohen, C.M.6
  • 13
    • 0027532063 scopus 로고
    • Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40glutamic acid→lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore)
    • Rybicki A C, Qiu J J, Musto S, Rosen N L, Nagel R L, Schwartz R S. Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40glutamic acid→lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore). Blood. 81:1993;2155-2165.
    • (1993) Blood , vol.81 , pp. 2155-2165
    • Rybicki, A.C.1    Qiu, J.J.2    Musto, S.3    Rosen, N.L.4    Nagel, R.L.5    Schwartz, R.S.6
  • 14
    • 0024316871 scopus 로고
    • Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)
    • Lux S E, John K M, Kopito R R, Lodish H F. Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Proc Natl Acad Sci USA. 86:1989;9089-9093.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9089-9093
    • Lux, S.E.1    John, K.M.2    Kopito, R.R.3    Lodish, H.F.4
  • 15
    • 0025117605 scopus 로고
    • Molecular cloning of human protein 4.2: A major component of the erythrocyte membrane
    • Sung L A, Chien S, Chang L S. Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. Proc Natl Acad Sci USA. 87:1990;955-959.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 955-959
    • Sung, L.A.1    Chien, S.2    Chang, L.S.3
  • 17
    • 0031022915 scopus 로고    scopus 로고
    • Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: Status of the D38A polymorphism within the EPB3 locus
    • Miraglia del Giudice E, Vallier A, Maillet P. Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: status of the D38A polymorphism within the EPB3 locus. Br J Haematol. 96:1997;70-76.
    • (1997) Br J Haematol , vol.96 , pp. 70-76
    • Miraglia Del Giudice, E.1    Vallier, A.2    Maillet, P.3
  • 18
    • 0010583929 scopus 로고    scopus 로고
    • Molecular and genetic characteristics in Japanese patients with hereditary spherocytosis: Frequent band 3 mutations and rarer ankyrin mutations
    • Kanzaki A, Takezono M, Kaku M. Molecular and genetic characteristics in Japanese patients with hereditary spherocytosis: frequent band 3 mutations and rarer ankyrin mutations. Blood. 90:1997;6b.
    • (1997) Blood , vol.90
    • Kanzaki, A.1    Takezono, M.2    Kaku, M.3
  • 19
    • 10544253080 scopus 로고    scopus 로고
    • Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency
    • Jarolim P, Murray J L, Rubin H L. Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency. Blood. 88:1996;4366-4374.
    • (1996) Blood , vol.88 , pp. 4366-4374
    • Jarolim, P.1    Murray, J.L.2    Rubin, H.L.3
  • 20
    • 9044220232 scopus 로고    scopus 로고
    • Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis
    • Eber S W, Gonzalez J M, Lux M L. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nat Genet. 13:1996;214-218.
    • (1996) Nat Genet , vol.13 , pp. 214-218
    • Eber, S.W.1    Gonzalez, J.M.2    Lux, M.L.3
  • 21
    • 0029763223 scopus 로고    scopus 로고
    • Hereditary spherocytosis with band 3 deficiency. Association with a nonsense mutation of the band 3 gene (allele Lyon), and aggravation by a low-expression allele occurring in trans (allele Genas)
    • Alloisio N, Maillet P, Carre G. Hereditary spherocytosis with band 3 deficiency. Association with a nonsense mutation of the band 3 gene (allele Lyon), and aggravation by a low-expression allele occurring in trans (allele Genas). Blood. 88:1996;1062-1069.
    • (1996) Blood , vol.88 , pp. 1062-1069
    • Alloisio, N.1    Maillet, P.2    Carre, G.3
  • 22
    • 0030758937 scopus 로고    scopus 로고
    • Band 3 Campinas: A novel splicing mutation in the band 3 gene (AE1) associated with hereditary spherocytosis, hyperactivity of Na+/Li+ countertransport and an abnormal renal bicarbonate handling
    • Lima P RM, Gontijo J AR, Lopes de Faria J B, Costa F F, Saad S TO. Band 3 Campinas: a novel splicing mutation in the band 3 gene (AE1) associated with hereditary spherocytosis, hyperactivity of Na+/Li+ countertransport and an abnormal renal bicarbonate handling. Blood. 90:1997;2810-2818.
    • (1997) Blood , vol.90 , pp. 2810-2818
    • Lima, P.R.M.1    Gontijo, J.A.R.2    Lopes De Faria, J.B.3    Costa, F.F.4    Saad, S.T.O.5
  • 23
    • 8544257359 scopus 로고    scopus 로고
    • Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects
    • Dhermy D, Galand C, Bournier O. Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects. Br J Haematol. 98:1997;32-40.
    • (1997) Br J Haematol , vol.98 , pp. 32-40
    • Dhermy, D.1    Galand, C.2    Bournier, O.3
  • 24
    • 13344262715 scopus 로고    scopus 로고
    • A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis
    • Jenkins P B, Abou-Alfa G K, Dhermy D. A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis. J Clin Invest. 97:1996;373-380.
    • (1996) J Clin Invest , vol.97 , pp. 373-380
    • Jenkins, P.B.1    Abou-Alfa, G.K.2    Dhermy, D.3
  • 25
    • 0030946079 scopus 로고    scopus 로고
    • Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis
    • Alloisio N, Texier P, Vallier A. Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis. Blood. 90:1997;414-420.
    • (1997) Blood , vol.90 , pp. 414-420
    • Alloisio, N.1    Texier, P.2    Vallier, A.3
  • 26
    • 8544227633 scopus 로고    scopus 로고
    • A variant of the EPB3 gene of the anti-Lepore type in hereditary spherocytosis
    • Bianchi P, Zanella A, Alloisio N. A variant of the EPB3 gene of the anti-Lepore type in hereditary spherocytosis. Br J Haematol. 98:1997;283-288.
    • (1997) Br J Haematol , vol.98 , pp. 283-288
    • Bianchi, P.1    Zanella, A.2    Alloisio, N.3
  • 27
    • 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 H L, Brabec V. 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. 85:1995;634-640.
    • (1995) Blood , vol.85 , pp. 634-640
    • Jarolim, P.1    Rubin, H.L.2    Brabec, V.3
  • 28
    • 0028862501 scopus 로고
    • Band 3 Chur: A variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11
    • Maillet P, Vallier A, Reinhart W H. Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11. Br J Haematol. 91:1995;804-810.
    • (1995) Br J Haematol , vol.91 , pp. 804-810
    • Maillet, P.1    Vallier, A.2    Reinhart, W.H.3
  • 29
    • 0028057275 scopus 로고
    • Duplication of 10 nucleotides in the erythroid band 3 (AE1) gene in a kindred with hereditary spherocytosis and band 3 protein deficiency (band 3PRAGUE)
    • Jarolim P, Rubin H L, Liu S C. Duplication of 10 nucleotides in the erythroid band 3 (AE1) gene in a kindred with hereditary spherocytosis and band 3 protein deficiency (band 3PRAGUE). J Clin Invest. 93:1994;121-130.
    • (1994) J Clin Invest , vol.93 , pp. 121-130
    • Jarolim, P.1    Rubin, H.L.2    Liu, S.C.3
  • 30
    • 85030334653 scopus 로고    scopus 로고
    • Hereditary spherocytosis due to an elongated band 3: Band 3 Vesuvio
    • Perrotta S, Nigro V, Polito R, Nobili B. Hereditary spherocytosis due to an elongated band 3: Band 3 Vesuvio. Blood. 90:1997;270a.
    • (1997) Blood , vol.90
    • Perrotta, S.1    Nigro, V.2    Polito, R.3    Nobili, B.4
  • 31
    • 0028794760 scopus 로고
    • A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia
    • Hayette S, Dhermy D, dos Santos M E. A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia. Blood. 85:1995;250-256.
    • (1995) Blood , vol.85 , pp. 250-256
    • Hayette, S.1    Dhermy, D.2    Dos Santos, M.E.3
  • 32
    • 0027970175 scopus 로고
    • A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka)
    • Takaoka Y, Ideguchi H, Matsuda M, Sakamoto N, Takeuchi T, Fukumaki Y. A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka). Br J Haematol. 88:1994;527-533.
    • (1994) Br J Haematol , vol.88 , pp. 527-533
    • Takaoka, Y.1    Ideguchi, H.2    Matsuda, M.3    Sakamoto, N.4    Takeuchi, T.5    Fukumaki, Y.6
  • 33
    • 0026504463 scopus 로고
    • An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2 NIPPON)
    • Bouhassira E E, Schwartz R S, Yawata Y. An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2 NIPPON). Blood. 79:1992;1846-1854.
    • (1992) Blood , vol.79 , pp. 1846-1854
    • Bouhassira, E.E.1    Schwartz, R.S.2    Yawata, Y.3
  • 34
    • 0029026258 scopus 로고
    • Band 4.2 Komatsu: 523 GAT→TAT (175 Asp→Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network
    • Kanzaki A, Yawata Y, Yawata A. Band 4.2 Komatsu: 523 GAT→TAT (175 Asp→Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network. Int J Hematol. 61:1995;165-178.
    • (1995) Int J Hematol , vol.61 , pp. 165-178
    • Kanzaki, A.1    Yawata, Y.2    Yawata, A.3
  • 36
    • 0028937282 scopus 로고
    • A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia
    • Hayette S, Morle L, Bozon M. A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. Br J Haematol. 89:1995;762-770.
    • (1995) Br J Haematol , vol.89 , pp. 762-770
    • Hayette, S.1    Morle, L.2    Bozon, M.3
  • 37
    • 0028810476 scopus 로고
    • Band 4.2 shiga: 317 CGC→TGC in compound heterozygotes with 142 GCT→ACT results in band 4.2 deficiency and microspherocytosis
    • Kanzaki A, Yasunaga M, Okamoto N. Band 4.2 shiga: 317 CGC→TGC in compound heterozygotes with 142 GCT→ACT results in band 4.2 deficiency and microspherocytosis. Br J Haematol. 91:1995;333-340.
    • (1995) Br J Haematol , vol.91 , pp. 333-340
    • Kanzaki, A.1    Yasunaga, M.2    Okamoto, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.