메뉴 건너뛰기




Volumn 85, Issue 1, 2000, Pages 19-24

Heavy transfusions and presence of an anti-protein 4.2 antibody in 4.2(- ) hereditary spherocytosis (949delG)

Author keywords

Anemia; Hereditary spherocytosis; Protein 4.2 Nancy; Transfusion

Indexed keywords

ERYTHROCYTE BAND 4.2 PROTEIN; PROTEIN ANTIBODY;

EID: 0033968683     PISSN: 03906078     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 0025162066 scopus 로고
    • Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2
    • Korsgren C, Lawler J, Lambert S, Speicher D, Cohen CM. Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. Proc Natl Acad Sci USA 1990; 87:613-7.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 613-617
    • Korsgren, C.1    Lawler, J.2    Lambert, S.3    Speicher, D.4    Cohen, C.M.5
  • 2
    • 0025117605 scopus 로고
    • Molecular cloning of human protein 4.2: A major component of the erythrocyte membrane
    • Sung LA, Chien S, Chang LS, et al. Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. Proc Natl Acad Sci USA 1990; 87:955-9.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 955-959
    • Sung, L.A.1    Chien, S.2    Chang, L.S.3
  • 3
    • 0026783795 scopus 로고
    • Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated
    • Risinger MA, Dotimas EM, Cohen CM. Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem 1992; 267: 5680-5.
    • (1992) J Biol Chem , vol.267 , pp. 5680-5685
    • Risinger, M.A.1    Dotimas, E.M.2    Cohen, C.M.3
  • 5
    • 0030890881 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a protein-palmitoyl acyltransferase from human erythrocytes
    • Das AK, Dasgupta B, Bhattacharya R, Basu J. Purification and biochemical characterization of a protein-palmitoyl acyltransferase from human erythrocytes. J Biol Chem 1997; 272:11021-5.
    • (1997) J Biol Chem , vol.272 , pp. 11021-11025
    • Das, A.K.1    Dasgupta, B.2    Bhattacharya, R.3    Basu, J.4
  • 6
    • 0026749810 scopus 로고
    • Human erythrocyte protein 4.2: Isoform expression, differential splicing, and chromosomal assignment
    • Sung LA, Chien S, Fan YS, et al. Human erythrocyte protein 4.2: isoform expression, differential splicing, and chromosomal assignment. Blood 1992; 79:2763-70.
    • (1992) Blood , vol.79 , pp. 2763-2770
    • Sung, L.A.1    Chien, S.2    Fan, Y.S.3
  • 7
    • 0025819205 scopus 로고
    • Organization of the gene for human erythrocyte membrane protein 4.2: Structural similarities with the gene for the α subunit of factor XIII
    • Korsgren C, Cohen CM. Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the α subunit of factor XIII. Proc Natl Acad Sci USA 1991; 88:4840-4.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4840-4844
    • Korsgren, C.1    Cohen, C.M.2
  • 8
    • 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 EE, Schwartz RS, Yawata Y, et al. 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 1992; 79:1846-54.
    • (1992) Blood , vol.79 , pp. 1846-1854
    • Bouhassira, E.E.1    Schwartz, R.S.2    Yawata, Y.3
  • 9
    • 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 ME, et al. A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia. Blood 1995; 85:250-6.
    • (1995) Blood , vol.85 , pp. 250-256
    • Hayette, S.1    Dhermy, D.2    Dos Santos, M.E.3
  • 10
    • 0028937282 scopus 로고
    • A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia
    • Hayette S, Morlé L, Bozon M, et al. A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. Br J Haematol 1995; 89:762-70.
    • (1995) Br J Haematol , vol.89 , pp. 762-770
    • Hayette, S.1    Morlé, L.2    Bozon, M.3
  • 11
    • 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, et al. 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 Haematol 1995; 61:165-78.
    • (1995) Int J Haematol , vol.61 , pp. 165-178
    • Kanzaki, A.1    Yawata, Y.2    Yawata, A.3
  • 12
    • 0024745370 scopus 로고
    • Pstl polymorphism for the human erythrocyte surface protein band 3 (EPB3) demonstrates close linkage of EPB3 to the nerve growth factor receptor
    • Stewart EA, Kopito R, Bowcock AM. Pstl polymorphism for the human erythrocyte surface protein band 3 (EPB3) demonstrates close linkage of EPB3 to the nerve growth factor receptor. Genomics 1989; 5:633-5.
    • (1989) Genomics , vol.5 , pp. 633-635
    • Stewart, E.A.1    Kopito, R.2    Bowcock, A.M.3
  • 13
    • 0027135217 scopus 로고
    • Analysis of a Pstl polymorphism of the human erythrocyte band 3 gene (EPB3)
    • Jenkins PB, Gallagher PG, Forget BG. Analysis of a Pstl polymorphism of the human erythrocyte band 3 gene (EPB3). Br J Haematol 1993; 85:816-8.
    • (1993) Br J Haematol , vol.85 , pp. 816-818
    • Jenkins, P.B.1    Gallagher, P.G.2    Forget, B.G.3
  • 14
    • 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 1989; 86:9089-93.
    • (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
    • 0017185162 scopus 로고
    • The removal of leukocytes and platelets from whole blood
    • Beutler E, West C, Blume KG. The removal of leukocytes and platelets from whole blood. J Lab Clin Med 1976; 88:328-33.
    • (1976) J Lab Clin Med , vol.88 , pp. 328-333
    • Beutler, E.1    West, C.2    Blume, K.G.3
  • 16
    • 0026593872 scopus 로고
    • Density separation of human red blood cells on self forming Percoll gradients: Correlation with cell age
    • Lutz HU, Stammler P, Fasler S, Ingold M, Fehr J. Density separation of human red blood cells on self forming Percoll gradients: correlation with cell age. Biochim Biophys Acta 1992; 1116:1-10.
    • (1992) Biochim Biophys Acta , vol.1116 , pp. 1-10
    • Lutz, H.U.1    Stammler, P.2    Fasler, S.3    Ingold, M.4    Fehr, J.5
  • 17
    • 0023803502 scopus 로고
    • Electrophoretic properties of human IgG and its subclasses on sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblots
    • Fasler S, Skvaril F, Lutz HU. Electrophoretic properties of human IgG and its subclasses on sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblots. Anal Biochem 1988; 174:593-600.
    • (1988) Anal Biochem , vol.174 , pp. 593-600
    • Fasler, S.1    Skvaril, F.2    Lutz, H.U.3
  • 18
    • 0027453622 scopus 로고
    • Naturally occurring anti-band 3 antibodies have a unique affinity for C3
    • Lutz HU, Nater M, Stammler P. Naturally occurring anti-band 3 antibodies have a unique affinity for C3. Immunology 1993; 80:191-6.
    • (1993) Immunology , vol.80 , pp. 191-196
    • Lutz, H.U.1    Nater, M.2    Stammler, P.3
  • 19
    • 7344233086 scopus 로고    scopus 로고
    • Homozygous missense mutation (band 3 Fukuoka: G130R): A mild form of hereditary spherocytosis with near-normal band 3 content and minimal changes of membrane ultrastructure despite moderate protein 4.2 deficiency
    • Inoue T, Kanzaki A, Kaku M, et al. Homozygous missense mutation (band 3 Fukuoka: G130R): a mild form of hereditary spherocytosis with near-normal band 3 content and minimal changes of membrane ultrastructure despite moderate protein 4.2 deficiency. Br J Haematol 1998; 102:932-9.
    • (1998) Br J Haematol , vol.102 , pp. 932-939
    • Inoue, T.1    Kanzaki, A.2    Kaku, M.3
  • 20
    • 0031417692 scopus 로고    scopus 로고
    • Hematologically important mutations: Band 3 and protein 4.2 in hereditary spherocytosis
    • Gallagher PG, Forget BG. Hematologically important mutations: band 3 and protein 4.2 in hereditary spherocytosis. Blood Cells Mol Dis 1997; 23:417-21.
    • (1997) Blood Cells Mol Dis , vol.23 , pp. 417-421
    • Gallagher, P.G.1    Forget, B.G.2
  • 21
    • 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 1994; 88:527-33.
    • (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
  • 22
    • 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, et al. 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 1995; 91:333-40.
    • (1995) Br J Haematol , vol.91 , pp. 333-340
    • Kanzaki, A.1    Yasunaga, M.2    Okamoto, N.3
  • 23
    • 0029070964 scopus 로고
    • A novel mutation causing an aberrant splicing in the protein 4.2 gene associated with hereditary spherocytosis (protein 4.2 Notame)
    • Matsuda M, Hatano N, Ideguchi H, Takahira H, Fukumaki Y. A novel mutation causing an aberrant splicing in the protein 4.2 gene associated with hereditary spherocytosis (protein 4.2 Notame). Hum Mol Genet 1995; 4:1187-91.
    • (1995) Hum Mol Genet , vol.4 , pp. 1187-1191
    • Matsuda, M.1    Hatano, N.2    Ideguchi, H.3    Takahira, H.4    Fukumaki, Y.5
  • 24
    • 0027499770 scopus 로고
    • Human gene mutations affecting RNA processing and translation
    • Cooper DN. Human gene mutations affecting RNA processing and translation. Ann Med 1993; 25:11-7.
    • (1993) Ann Med , vol.25 , pp. 11-17
    • Cooper, D.N.1
  • 25
    • 0029330286 scopus 로고
    • When cells stop making sense: Effects of nonsense codons on RNA metabolism in vertebrate cells
    • Maquat LE. When cells stop making sense: effects of nonsense codons on RNA metabolism in vertebrate cells. RNA 1995; 1:453-65.
    • (1995) RNA , vol.1 , pp. 453-465
    • Maquat, L.E.1
  • 26
    • 0029835707 scopus 로고    scopus 로고
    • Defects in RNA splicing and the consequence of shortened translational reading frames
    • Maquat LE. Defects in RNA splicing and the consequence of shortened translational reading frames. Am J Hum Genet 1996; 59:279-86.
    • (1996) Am J Hum Genet , vol.59 , pp. 279-286
    • Maquat, L.E.1
  • 27
    • 0020078184 scopus 로고
    • Naturally occurring autoantibodies to skeletal proteins from human red blood cells
    • Lutz HU, Wipf G. Naturally occurring autoantibodies to skeletal proteins from human red blood cells. J Immunol 1982; 128:1695-9.
    • (1982) J Immunol , vol.128 , pp. 1695-1699
    • Lutz, H.U.1    Wipf, G.2
  • 28
    • 0346079412 scopus 로고
    • Naturally occurring anti-band-3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes
    • Lutz HU, Bussolino F, Flepp R, et al. Naturally occurring anti-band-3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes. Proc Natl Acad Sci USA 1987; 84:7368-72.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7368-7372
    • Lutz, H.U.1    Bussolino, F.2    Flepp, R.3
  • 30
    • 0032781763 scopus 로고    scopus 로고
    • Miraglia del Giudice E. 4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis
    • Perrotta S, Iolascon A, Polito R, d'Urzo G, Conte ML, Miraglia del Giudice E. 4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis. Haematologica 1999 84:660-2.
    • (1999) Haematologica , vol.84 , pp. 660-662
    • Perrotta, S.1    Iolascon, A.2    Polito, R.3    D'Urzo, G.4    Conte, M.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.