메뉴 건너뛰기




Volumn 58, Issue 3, 1998, Pages 200-205

Preliminary characterization of a structural defect in homozygous sickled cell alpha spectrin demonstrated by a rabbit autoantibody

Author keywords

Membrane skeleton; Red blood cell; Sickle cell disease; Spectrin

Indexed keywords

ACTIN; AUTOANTIBODY; CELL MEMBRANE PROTEIN; DITHIOTHREITOL; FODRIN; SPECTRIN;

EID: 0031816278     PISSN: 03618609     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1096-8652(199807)58:3<200::AID-AJH7>3.0.CO;2-V     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0021169761 scopus 로고
    • An objective sign in painful crisis in sickle cell anemia: The concomitant reduction in high density red cells
    • Fabry ME, Benjamin L, Lawrence C, Nagel RL: An objective sign in painful crisis in sickle cell anemia: The concomitant reduction in high density red cells. Blood 64:559, 1984.
    • (1984) Blood , vol.64 , pp. 559
    • Fabry, M.E.1    Benjamin, L.2    Lawrence, C.3    Nagel, R.L.4
  • 2
    • 0014315876 scopus 로고
    • Irreversibly sickled erythrocytes: A consequence of the heterogenous distribution of hemoglobin types in sickle-cell anemia
    • Bertles JF, Milner PFA: Irreversibly sickled erythrocytes: A consequence of the heterogenous distribution of hemoglobin types in sickle-cell anemia. J Clin Invest 47:1731, 1968.
    • (1968) J Clin Invest , vol.47 , pp. 1731
    • Bertles, J.F.1    Milner, P.F.A.2
  • 3
    • 0022812367 scopus 로고
    • Vaso-occlusion by sickle cells: Evidence for selective trapping of dense red cells
    • Kaul DK, Fabry ME, Nagel RL: Vaso-occlusion by sickle cells: Evidence for selective trapping of dense red cells. Blood 68:1162, 1986.
    • (1986) Blood , vol.68 , pp. 1162
    • Kaul, D.K.1    Fabry, M.E.2    Nagel, R.L.3
  • 4
    • 0344812230 scopus 로고
    • Microvascular sites and characteristics of sickle cell adhesion to vascular endothelium in sheer flow conditions: Pathophysiological implications
    • Kaul DK, Fabry ME, Nagel RL: Microvascular sites and characteristics of sickle cell adhesion to vascular endothelium in sheer flow conditions: pathophysiological implications. Proc Natl Acad Sci USA 86:3356, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3356
    • Kaul, D.K.1    Fabry, M.E.2    Nagel, R.L.3
  • 6
    • 0026099699 scopus 로고
    • Beyond hemoglobin polymerization: The red blood cell membrane and sickle disease pathophysiology
    • Hebbel RP: Beyond hemoglobin polymerization: The red blood cell membrane and sickle disease pathophysiology. Blood 77:214, 1991.
    • (1991) Blood , vol.77 , pp. 214
    • Hebbel, R.P.1
  • 7
    • 0017101401 scopus 로고
    • Irreversible deformation of the spectrin-actin lattice in irreversibly sickled cells
    • Lux SE, John KM, Karnovsky MJ: Irreversible deformation of the spectrin-actin lattice in irreversibly sickled cells. J Clin Invest 58:955, 1976.
    • (1976) J Clin Invest , vol.58 , pp. 955
    • Lux, S.E.1    John, K.M.2    Karnovsky, M.J.3
  • 9
    • 0015863154 scopus 로고
    • Selective solubilization of proteins and phospholipids of red blood cell membranes by nonionic detergents
    • Yu J, Fischman DA, Steck TL: Selective solubilization of proteins and phospholipids of red blood cell membranes by nonionic detergents. J Supramol Struct 1:233, 1973.
    • (1973) J Supramol Struct , vol.1 , pp. 233
    • Yu, J.1    Fischman, D.A.2    Steck, T.L.3
  • 10
    • 0018677111 scopus 로고
    • Integral membrane protein interactions with triton cytoskeletons of erythrocytes
    • Sheetz MP: Integral membrane protein interactions with triton cytoskeletons of erythrocytes. Biochem Biophys Acta 551:122, 1979.
    • (1979) Biochem Biophys Acta , vol.551 , pp. 122
    • Sheetz, M.P.1
  • 11
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies
    • Shotton D, Burke BE, Branton D: The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. J Mol Biol 131:303, 1979.
    • (1979) J Mol Biol , vol.131 , pp. 303
    • Shotton, D.1    Burke, B.E.2    Branton, D.3
  • 14
    • 0018720539 scopus 로고
    • Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link f-actin
    • Brenner SL, Korn E: Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link f-actin. J Biol Chem 254: 8620, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 8620
    • Brenner, S.L.1    Korn, E.2
  • 15
    • 0018938853 scopus 로고
    • Spectrin-actin association studied by electron microscopy of shadowed preparations
    • Cohen CM, Tyler JM, Branton D: Spectrin-actin association studied by electron microscopy of shadowed preparations. Cell 21:875, 1980.
    • (1980) Cell , vol.21 , pp. 875
    • Cohen, C.M.1    Tyler, J.M.2    Branton, D.3
  • 16
    • 0022486512 scopus 로고
    • Ultrastructure of the intact skeleton of the human erythrocyte membrane
    • Shen BW, Josephs R, Steck TL: Ultrastructure of the intact skeleton of the human erythrocyte membrane. J Cell Biol 102:957, 1986.
    • (1986) J Cell Biol , vol.102 , pp. 957
    • Shen, B.W.1    Josephs, R.2    Steck, T.L.3
  • 17
    • 0025290039 scopus 로고
    • The identification of the actin binding domain of human red blood cell β-spectrin
    • Karinch AM, Zimmer WE, Goodman SR: The identification of the actin binding domain of human red blood cell β-spectrin. J Biol Chem 265:11833, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 11833
    • Karinch, A.M.1    Zimmer, W.E.2    Goodman, S.R.3
  • 18
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers TJ, Branton D: Visualization of the protein associations in the erythrocyte membrane skeleton. Proc Natl Acad Sci USA 82:6151, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 6151
    • Byers, T.J.1    Branton, D.2
  • 19
    • 0023150141 scopus 로고
    • Visualization of the hexagonal lattice in the erythrocyte membrane skeleton
    • Liu SC, Derick LH, Palek J: Visualization of the hexagonal lattice in the erythrocyte membrane skeleton. J Cell Biol 104:527, 1987.
    • (1987) J Cell Biol , vol.104 , pp. 527
    • Liu, S.C.1    Derick, L.H.2    Palek, J.3
  • 20
    • 0009470593 scopus 로고
    • Purification of two spectrin-binding proteins: Biochemical and electron microscopic evidence for site specific reassociation between spectrin and bands 2.1 and 4.1
    • Tyler JM, Hargreaves WR, Branton D: Purification of two spectrin-binding proteins: Biochemical and electron microscopic evidence for site specific reassociation between spectrin and bands 2.1 and 4.1. Proc Natl Acad Sci USA 76:5192, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 5192
    • Tyler, J.M.1    Hargreaves, W.R.2    Branton, D.3
  • 21
    • 0018646622 scopus 로고
    • In vitro formation of a complex between cytoskeletal proteins of the human erythrocyte
    • Ungewickell E, Bennett PM, Calvert R, Ohanian V, Gratzer WB: In vitro formation of a complex between cytoskeletal proteins of the human erythrocyte. Nature (Lond) 280:811, 1979.
    • (1979) Nature (Lond) , vol.280 , pp. 811
    • Ungewickell, E.1    Bennett, P.M.2    Calvert, R.3    Ohanian, V.4    Gratzer, W.B.5
  • 22
    • 0019310758 scopus 로고
    • Spectrin plus band 4.1 crosslink actin. Regulation by micromolar calcium
    • Fowler VM, Taylor DL: Spectrin plus band 4.1 crosslink actin. Regulation by micromolar calcium. J Cell Biol 85:361, 1980.
    • (1980) J Cell Biol , vol.85 , pp. 361
    • Fowler, V.M.1    Taylor, D.L.2
  • 23
    • 0018397366 scopus 로고
    • Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin
    • Bennett V, Stenbuck PJ: Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. J Biol Chem 254:2533, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 2533
    • Bennett, V.1    Stenbuck, P.J.2
  • 24
    • 0019321291 scopus 로고
    • Association between ankyrin and the cytoplasmic domain of band 3 isolated from erythrocyte membrane
    • Bennett V, Stenbuck PJ: Association between ankyrin and the cytoplasmic domain of band 3 isolated from erythrocyte membrane. J Biol Chem 255:6424, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 6424
    • Bennett, V.1    Stenbuck, P.J.2
  • 25
    • 0346761425 scopus 로고
    • Syndeins: The spectrin-binding protein(s) of the human erythrocyte membrane
    • Yu J, Goodman SR: Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane. Proc Natl Acad Sci USA 76:2340, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 2340
    • Yu, J.1    Goodman, S.R.2
  • 26
    • 0019287394 scopus 로고
    • Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles
    • Hargreaves WR, Giedd KN, Verkleij A, Branton D: Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles. J Biol Chem 255:11965, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 11965
    • Hargreaves, W.R.1    Giedd, K.N.2    Verkleij, A.3    Branton, D.4
  • 27
    • 0021211784 scopus 로고
    • A structural model of human erythrocyte band 2.1: Alignment of chemical and functional domains
    • Wallin R, Gulp EN, Coleman DB, Goodman SR: A structural model of human erythrocyte band 2.1: Alignment of chemical and functional domains. Proc Natl Acad Sci USA 81:4095, 1984.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4095
    • Wallin, R.1    Gulp, E.N.2    Coleman, D.B.3    Goodman, S.R.4
  • 28
    • 0021219573 scopus 로고
    • Protein 4.1: Its association with the human erythrocyte membrane
    • Shifter KA, Goodman SR: Protein 4.1: Its association with the human erythrocyte membrane. Proc Natl Acad Sci USA 81:4404, 1984.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4404
    • Shifter, K.A.1    Goodman, S.R.2
  • 30
    • 0029883813 scopus 로고    scopus 로고
    • High density sickle cell erythrocyte core membrane skeletons demonstrate slow temperature dependent dissociation
    • Shartava A, Miranda P, Williams KN, Shah A, Monteiro CA, Goodman SR: High density sickle cell erythrocyte core membrane skeletons demonstrate slow temperature dependent dissociation. Am J Hematol 51:214, 1996.
    • (1996) Am J Hematol , vol.51 , pp. 214
    • Shartava, A.1    Miranda, P.2    Williams, K.N.3    Shah, A.4    Monteiro, C.A.5    Goodman, S.R.6
  • 31
    • 0029949220 scopus 로고    scopus 로고
    • Identification of the disulfide-linked peptide in irreversibly sickled cell β-actin
    • Benscath FA, Shartava A, Monteiro CA, Goodman SR: Identification of the disulfide-linked peptide in irreversibly sickled cell β-actin. Biochemistry 35:4403, 1996.
    • (1996) Biochemistry , vol.35 , pp. 4403
    • Benscath, F.A.1    Shartava, A.2    Monteiro, C.A.3    Goodman, S.R.4
  • 32
    • 0030745431 scopus 로고    scopus 로고
    • Irreversibly sickled cell β-actin: Defective filament formation
    • Shartava A, Korn W, Shah AK, Goodman SR: Irreversibly sickled cell β-actin: Defective filament formation. Am J Hematol 55:97, 1997.
    • (1997) Am J Hematol , vol.55 , pp. 97
    • Shartava, A.1    Korn, W.2    Shah, A.K.3    Goodman, S.R.4
  • 33
    • 0242582357 scopus 로고    scopus 로고
    • The role of the membrane skeleton in formation of the irreversibly sickled cell: A review
    • Goodman SR: The role of the membrane skeleton in formation of the irreversibly sickled cell: A review. Cell Mol Biol Lett 1:105, 1996.
    • (1996) Cell Mol Biol Lett , vol.1 , pp. 105
    • Goodman, S.R.1
  • 34
    • 0027392464 scopus 로고
    • Dependence of the permanent deformation of red blood cell membranes on spectrin dimer-tetramer equilibrium: Implication for permanent membrane deformation fo irreversibly sickled cells
    • Liu SC, Derrick LH, Palek J: Dependence of the permanent deformation of red blood cell membranes on spectrin dimer-tetramer equilibrium: Implication for permanent membrane deformation fo irreversibly sickled cells. Blood 81:522, 1993.
    • (1993) Blood , vol.81 , pp. 522
    • Liu, S.C.1    Derrick, L.H.2    Palek, J.3
  • 35
    • 0029130023 scopus 로고
    • Membrane protein interactions in sickle red blood cells: Evidence of abnormal protein 3 function
    • Platt OS, Falcone JF: Membrane protein interactions in sickle red blood cells: Evidence of abnormal protein 3 function. Blood 86:1992, 1995.
    • (1995) Blood , vol.86 , pp. 1992
    • Platt, O.S.1    Falcone, J.F.2
  • 36
    • 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 (Lond.) 227:680, 1970.
    • (1970) Nature (Lond.) , vol.227 , pp. 680
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.