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Volumn 87, Issue 10, 1996, Pages 4433-4439

The cisternae decorating the red blood cell membrane in congenital dyserythropoietic anemia (type II) originate from the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

ANAZOLENE SODIUM; CALRETICULIN;

EID: 9344251085     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v87.10.4433.bloodjournal87104433     Document Type: Article
Times cited : (69)

References (41)
  • 1
    • 0025607312 scopus 로고
    • HEMPAS disease: Genetic defect of glycosylation
    • Fukuda MN: HEMPAS disease: Genetic defect of glycosylation. Glycobiology 1:9, 1990
    • (1990) Glycobiology , vol.1 , pp. 9
    • Fukuda, M.N.1
  • 2
    • 0027283744 scopus 로고
    • Congenital dyserythropoietic anaemia type II (HEMPAS) and its molecular basis
    • Fukuda MN: Congenital dyserythropoietic anaemia type II (HEMPAS) and its molecular basis. Clin Haematol 6:493, 1993
    • (1993) Clin Haematol , vol.6 , pp. 493
    • Fukuda, M.N.1
  • 3
    • 0015253170 scopus 로고
    • Congenital dyserythropoietic anemia type II: Ultrastructural and radioautographic studies of blood and bone marrow
    • Wong KY, Hug G, Lampkin BC: Congenital dyserythropoietic anemia type II: Ultrastructural and radioautographic studies of blood and bone marrow. Blood 39:23, 1972
    • (1972) Blood , vol.39 , pp. 23
    • Wong, K.Y.1    Hug, G.2    Lampkin, B.C.3
  • 4
    • 0015538559 scopus 로고
    • Anomalies ultrastructurales des érythroblastes et des érythrocytes dans six cas de dyserythropoïèse congénitale
    • Breton-Gorius J, Daniel MT, Clauvel JP, Dreyfus B: Anomalies ultrastructurales des érythroblastes et des érythrocytes dans six cas de dyserythropoïèse congénitale. Nouv Rev Fr Hematol 13:23, 1973
    • (1973) Nouv Rev Fr Hematol , vol.13 , pp. 23
    • Breton-Gorius, J.1    Daniel, M.T.2    Clauvel, J.P.3    Dreyfus, B.4
  • 5
    • 0018774486 scopus 로고
    • Morphological abnormalities in cultured erythroid colonies (BFU-E) from the blood of two patients with HEMPAS
    • Vainchencker W, Guichard I, Breton-Gorius J: Morphological abnormalities in cultured erythroid colonies (BFU-E) from the blood of two patients with HEMPAS. Br J Haematol 42:363, 1979
    • (1979) Br J Haematol , vol.42 , pp. 363
    • Vainchencker, W.1    Guichard, I.2    Breton-Gorius, J.3
  • 6
    • 0023177484 scopus 로고
    • Congenital dyserythropoietic anaemia type II (HEMPAS): Characterization of aberrant intracellular organelles by immunogold electron microscopy
    • Fukuda MN, Klier G, Scartezzini P: Congenital dyserythropoietic anaemia type II (HEMPAS): Characterization of aberrant intracellular organelles by immunogold electron microscopy. Br J Haematol 67:95, 1987
    • (1987) Br J Haematol , vol.67 , pp. 95
    • Fukuda, M.N.1    Klier, G.2    Scartezzini, P.3
  • 7
    • 0017336450 scopus 로고
    • Congenital dyserythropoietic anaemia, type I and II: Aberrant pattern of erythrocyte membrane proteins in CDAII, as revealed by two-dimensional polyacrylamide gel electrophoresis
    • Anselstetter V, Horstmann HJ, Heimpel H: Congenital dyserythropoietic anaemia, type I and II: Aberrant pattern of erythrocyte membrane proteins in CDAII, as revealed by two-dimensional polyacrylamide gel electrophoresis. Br J Haematol 35:209, 1977
    • (1977) Br J Haematol , vol.35 , pp. 209
    • Anselstetter, V.1    Horstmann, H.J.2    Heimpel, H.3
  • 8
    • 0020067631 scopus 로고
    • Erythrocyte membrane proteins in an unusual case of congenital dyserythropoietic anaemia type II (CDAII)
    • Harlow RW, Lowenthal RM: Erythrocyte membrane proteins in an unusual case of congenital dyserythropoietic anaemia type II (CDAII). Br J Haematol 50:35, 1982
    • (1982) Br J Haematol , vol.50 , pp. 35
    • Harlow, R.W.1    Lowenthal, R.M.2
  • 9
    • 0020045220 scopus 로고
    • Red cell membrane protein anomalies in congenital dyserythropoietic anaemia, type II (HEMPAS)
    • Baines AJ, Banga JPS, Gratzer WB, Linch DC, Huehns ER: Red cell membrane protein anomalies in congenital dyserythropoietic anaemia, type II (HEMPAS). Br J Haematol 50:563, 1982
    • (1982) Br J Haematol , vol.50 , pp. 563
    • Baines, A.J.1    Banga, J.P.S.2    Gratzer, W.B.3    Linch, D.C.4    Huehns, E.R.5
  • 11
    • 0019977542 scopus 로고
    • Decreased glycosylation of band 3 and band 4.5 glycoproteins of erythrocyte membrane in congenital dyserythropoietic anaemia type II
    • Scartezzini P, Forni GL, Baldi M, Izzo C, Sansone G: Decreased glycosylation of band 3 and band 4.5 glycoproteins of erythrocyte membrane in congenital dyserythropoietic anaemia type II. Br J Haematol 51:569, 1982
    • (1982) Br J Haematol , vol.51 , pp. 569
    • Scartezzini, P.1    Forni, G.L.2    Baldi, M.3    Izzo, C.4    Sansone, G.5
  • 12
    • 0020571298 scopus 로고
    • Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia type H (CDAII)
    • Mawby WJ, Tanner MHA, Anstee DJ, Clamp JR: Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia type H (CDAII). Br J Haematol 55:357, 1983
    • (1983) Br J Haematol , vol.55 , pp. 357
    • Mawby, W.J.1    Tanner, M.H.A.2    Anstee, D.J.3    Clamp, J.R.4
  • 13
    • 0021320047 scopus 로고
    • Defect in glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia type II (HEMPAS)
    • Fukuda MN, Papayannopoulou T, Gordon-Smith EC, Rochant H, Testa U: Defect in glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia type II (HEMPAS). Br J Haematol 56:55, 1984
    • (1984) Br J Haematol , vol.56 , pp. 55
    • Fukuda, M.N.1    Papayannopoulou, T.2    Gordon-Smith, E.C.3    Rochant, H.4    Testa, U.5
  • 14
    • 0022520245 scopus 로고
    • Anomalous clustering in underglycosylated band 3 in erythrocytes and their precursor cells in congenital dyserythropoietic anemia type II
    • Fukuda MN, Klier G, Scartezzini P: Anomalous clustering in underglycosylated band 3 in erythrocytes and their precursor cells in congenital dyserythropoietic anemia type II. Blood 68:521, 1986
    • (1986) Blood , vol.68 , pp. 521
    • Fukuda, M.N.1    Klier, G.2    Scartezzini, P.3
  • 15
    • 0021986428 scopus 로고
    • Abnormal fatty acid composition of erythrocyte glycosphingolipids in congenital dyserythropoietic anemia type II
    • Bouhours JF, Bouhours D, Delaunay J: Abnormal fatty acid composition of erythrocyte glycosphingolipids in congenital dyserythropoietic anemia type II. J Lipids Res 26:435, 1985
    • (1985) J Lipids Res , vol.26 , pp. 435
    • Bouhours, J.F.1    Bouhours, D.2    Delaunay, J.3
  • 17
    • 0023227217 scopus 로고
    • Primary defect in congenital dyserythropoietic anaemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II
    • Fukuda MN, Dell A, Scartezzini P: Primary defect in congenital dyserythropoietic anaemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II. J Biol Chem 262:7195, 1987
    • (1987) J Biol Chem , vol.262 , pp. 7195
    • Fukuda, M.N.1    Dell, A.2    Scartezzini, P.3
  • 18
    • 0024506085 scopus 로고
    • Defective glycosylation of erythrocyte membrane glycoconjugates in a variant of congenital dyserythropoietic anaemia type II: Association of low level of membrane-bound form of galactosyltransferase
    • Fukuda MN, Masri KA, Dell A, Thonar EJM, Klier G, Lowenthal RM: Defective glycosylation of erythrocyte membrane glycoconjugates in a variant of congenital dyserythropoietic anaemia type II: Association of low level of membrane-bound form of galactosyltransferase. Blood 73:1331, 1989
    • (1989) Blood , vol.73 , pp. 1331
    • Fukuda, M.N.1    Masri, K.A.2    Dell, A.3    Thonar, E.J.M.4    Klier, G.5    Lowenthal, R.M.6
  • 19
    • 11944260919 scopus 로고
    • Incomplete synthesis of N-glycans in congenital dyserythropoietic anaemia type II caused by a defect in the gene encoding alpha-mannosidase II
    • Fukuda MN, Masri KA, Dell A, Luzzatto L, Morement KW: Incomplete synthesis of N-glycans in congenital dyserythropoietic anaemia type II caused by a defect in the gene encoding alpha-mannosidase II. Proc Natl Acad Sci USA 87:7443, 1990
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7443
    • Fukuda, M.N.1    Masri, K.A.2    Dell, A.3    Luzzatto, L.4    Morement, K.W.5
  • 20
    • 0023890443 scopus 로고
    • Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: Structure, conservation, and regulation
    • Ting J, Lee AS: Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: Structure, conservation, and regulation. DNA 7:275, 1988
    • (1988) DNA , vol.7 , pp. 275
    • Ting, J.1    Lee, A.S.2
  • 21
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro S, Pelham HRB: An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46:291, 1986
    • (1986) Cell , vol.46 , pp. 291
    • Munro, S.1    Pelham, H.R.B.2
  • 23
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M: Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 264:21522, 1989
    • (1989) J Biol Chem , vol.264 , pp. 21522
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Michalak, M.5
  • 24
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium-binding ER/SR protein
    • Smith MJ, Koch GLE: Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium-binding ER/SR protein. EMBO J 8:3581, 1989
    • (1989) EMBO J , vol.8 , pp. 3581
    • Smith, M.J.1    Koch, G.L.E.2
  • 25
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman JC, Ellis L, Blacher RW, Roth RA, Rutter WJ: Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317:267, 1985
    • (1985) Nature , vol.317 , pp. 267
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 26
    • 0023749218 scopus 로고
    • Identification of a set of calcium-binding protein in reticuloplasm, the luminal content of the endoplasmic reticulum
    • Macer DRJ, Koch GLE: Identification of a set of calcium-binding protein in reticuloplasm, the luminal content of the endoplasmic reticulum. J Cell Sci 91:61, 1988
    • (1988) J Cell Sci , vol.91 , pp. 61
    • Macer, D.R.J.1    Koch, G.L.E.2
  • 31
    • 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, Chobrak L, Zolotaref AS, Alper SL, Brugnara C, Wichterle H, Palek J: 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 85:634, 1995
    • (1995) Blood , vol.85 , pp. 634
    • Jarolim, P.1    Rubin, H.L.2    Brabec, V.3    Chobrak, L.4    Zolotaref, A.S.5    Alper, S.L.6    Brugnara, C.7    Wichterle, H.8    Palek, J.9
  • 32
    • 3042972346 scopus 로고
    • Molecular characterization of hereditary spherocytosis with band 3 deficiency
    • abstr
    • Jarolim P, Murray J, Rubin HL, Palek J, The Hemolytic Anemia Study Group: Molecular characterization of hereditary spherocytosis with band 3 deficiency. Blood 84:362a, 1994 (abstr, suppl 1)
    • (1994) Blood , vol.84 , Issue.1 SUPPL.
    • Jarolim, P.1    Murray, J.2    Rubin, H.L.3    Palek, J.4
  • 34
    • 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
  • 35
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G, Steck TL, Wallach DFH: Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606, 1971
    • (1971) Biochemistry , vol.10 , pp. 2606
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 39
    • 77956850966 scopus 로고
    • Localization of macromolecular components by application of the immunogold technique on cryosectioned bacteria
    • Slot JW, Geuze JJ, Weerkamp AJ: Localization of macromolecular components by application of the immunogold technique on cryosectioned bacteria. Methods Microbiol 20:236, 1988
    • (1988) Methods Microbiol , vol.20 , pp. 236
    • Slot, J.W.1    Geuze, J.J.2    Weerkamp, A.J.3
  • 40
    • 7944229047 scopus 로고
    • Decreased band 3 content, sulfate flux, and band 3 fractional mobility in congenital dyserythropoietic anemia
    • abstr
    • Jarolim P, Brabec V, Chobrak L, Alper SL, Brugnara C, Corbett JD, Cho MR, Golan DE: Decreased band 3 content, sulfate flux, and band 3 fractional mobility in congenital dyserythropoietic anemia. Blood 84:6a, 1994 (abstr, suppl 1)
    • (1994) Blood , vol.84 , Issue.1 SUPPL.
    • Jarolim, P.1    Brabec, V.2    Chobrak, L.3    Alper, S.L.4    Brugnara, C.5    Corbett, J.D.6    Cho, M.R.7    Golan, D.E.8
  • 41
    • 0022833371 scopus 로고
    • Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin
    • Koch G, Smith M, Macer D, Webster P, Mortara R: Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. J Cell Sci 86:217, 1986
    • (1986) J Cell Sci , vol.86 , pp. 217
    • Koch, G.1    Smith, M.2    Macer, D.3    Webster, P.4    Mortara, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.