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Volumn 77, Issue 2, 1999, Pages 865-878

Actin protofilament orientation at the erythrocyte membrane

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; F ACTIN; LIPID; PHALLOIDIN; RHODAMINE; SPECTRIN;

EID: 0032774449     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76938-9     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 0027291592 scopus 로고
    • Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C
    • Alloisio, N., N. Dalla Venezia, A. Rana, K. Andrabi, P. Texier, F. Gilsanz, J. P. Cartron, J. Delaunay, and A. H. Chishti. 1993. Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C. Blood. 82:1323-1327.
    • (1993) Blood , vol.82 , pp. 1323-1327
    • Alloisio, N.1    Dalla Venezia, N.2    Rana, A.3    Andrabi, K.4    Texier, P.5    Gilsanz, F.6    Cartron, J.P.7    Delaunay, J.8    Chishti, A.H.9
  • 2
    • 0018389150 scopus 로고
    • Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization
    • Axelrod, D. 1979. Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization. Biophys. J. 26: 557-574.
    • (1979) Biophys. J. , vol.26 , pp. 557-574
    • Axelrod, D.1
  • 3
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett, V., and P. J. Stenbuck. 1979. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature. 280:468-473,
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 4
    • 0029885486 scopus 로고    scopus 로고
    • The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy
    • Blackman, S. M., C. E. Cobb, A. H. Beth, and D. W. Piston. 1996. The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy. Biophys. J 71:194-208.
    • (1996) Biophys. J , vol.71 , pp. 194-208
    • Blackman, S.M.1    Cobb, C.E.2    Beth, A.H.3    Piston, D.W.4
  • 5
    • 0028297058 scopus 로고
    • Orientation of actin filaments during motion in in vitro motility assay
    • Borejdo, J., and S. Burlacu. 1994. Orientation of actin filaments during motion in in vitro motility assay. Biophys. J. 66:1319-1327.
    • (1994) Biophys. J. , vol.66 , pp. 1319-1327
    • Borejdo, J.1    Burlacu, S.2
  • 6
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers, T. J., and D. Branton. 1985. Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Nail. Acad. Sci. USA. 82:6153-6157.
    • (1985) Proc. Nail. Acad. Sci. USA , vol.82 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 7
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • Discher, D. E., N. Mohandas, and E. A. Evans. 1994. Molecular maps of red cell deformation: hidden elasticity and in situ connectivity. Science. 266:1032-1035.
    • (1994) Science , vol.266 , pp. 1032-1035
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3
  • 8
    • 0029162126 scopus 로고
    • Mechanochemistry of protein 4.1's spectin-actin binding domain: Ternary complex interactions, membrane binding, network integration, structural strengthening
    • Discher, D. E., R. Winardi, P. O. Schischmanoff, M. Parra, J. G. Conboy, and N. Mohandas. 1995. Mechanochemistry of protein 4.1's spectin-actin binding domain: ternary complex interactions, membrane binding, network integration, structural strengthening. J. Cell Biol. 130: 897-907.
    • (1995) J. Cell Biol. , vol.130 , pp. 897-907
    • Discher, D.E.1    Winardi, R.2    Schischmanoff, P.O.3    Parra, M.4    Conboy, J.G.5    Mohandas, N.6
  • 9
    • 0029818016 scopus 로고    scopus 로고
    • Kinematics of red cell aspiration by fluorescence-imaged microdeformation
    • Discher, D. E., and N. Mohandas. 1996. Kinematics of red cell aspiration by fluorescence-imaged microdeformation. Biophys. J 71:1680-1694.
    • (1996) Biophys. J , vol.71 , pp. 1680-1694
    • Discher, D.E.1    Mohandas, N.2
  • 10
    • 0031705402 scopus 로고    scopus 로고
    • Simulations of the erythrocyte cytoskeleton at large deformation. II. Micropipette aspiration
    • Discher, D. E., D. H. Boal, and S. K. Boey. 1998. Simulations of the erythrocyte cytoskeleton at large deformation. II. Micropipette aspiration. Biophys. J. 75:1584-1597.
    • (1998) Biophys. J. , vol.75 , pp. 1584-1597
    • Discher, D.E.1    Boal, D.H.2    Boey, S.K.3
  • 11
    • 0344898549 scopus 로고
    • Composite material structure of red cell membranes
    • G. J. Brewer, editor. Liss, New York
    • Evans, E. A. 1975. Composite material structure of red cell membranes. In Erythrocyte Structure and Function. G. J. Brewer, editor. Liss, New York. 491-506.
    • (1975) Erythrocyte Structure and Function , pp. 491-506
    • Evans, E.A.1
  • 13
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and striated muscle
    • Fowler, V. M. 1996. Regulation of actin filament length in erythrocytes and striated muscle. Curr. Opin. Cell Biol. 8:86-96.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 14
    • 0028969850 scopus 로고
    • Does actin bind to membrane lipids under conditions compatible with those existing in vivo?
    • Gicquaud, C. 1995. Does actin bind to membrane lipids under conditions compatible with those existing in vivo? Biochem. Biophys. Res. Com. 208:1154-1158.
    • (1995) Biochem. Biophys. Res. Com. , vol.208 , pp. 1154-1158
    • Gicquaud, C.1
  • 16
    • 0025336497 scopus 로고
    • Spectrin, actin and the structure of the cortical lattice in mammalian cochlear outer hair cells
    • Holley, M. C., and J. F. Ashmore. 1990. Spectrin, actin and the structure of the cortical lattice in mammalian cochlear outer hair cells. J. Cell Sci. 96:283-291.
    • (1990) J. Cell Sci. , vol.96 , pp. 283-291
    • Holley, M.C.1    Ashmore, J.F.2
  • 17
    • 0030025568 scopus 로고    scopus 로고
    • F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions
    • Kas, J., H. Strey, J. X. Tang, D. Finger, R. Ezzell, E. Sackmann, and P. A. Janmey. 1996. F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions. Biophys. J. 70: 609-625.
    • (1996) Biophys. J. , vol.70 , pp. 609-625
    • Kas, J.1    Strey, H.2    Tang, J.X.3    Finger, D.4    Ezzell, R.5    Sackmann, E.6    Janmey, P.A.7
  • 18
    • 0025992141 scopus 로고
    • Dual-view microscopy with a single camera: Real-time imaging of molecular orientations and calcium
    • Kinosita, K., H. Itoh, Jr., S. Ishiwata, K. Hirano, T. Nishizaka, and T. Hayakawa. 1991. Dual-view microscopy with a single camera: real-time imaging of molecular orientations and calcium. J. Cell Biol. 115:67-73.
    • (1991) J. Cell Biol. , vol.115 , pp. 67-73
    • Kinosita, K.1    Itoh H., Jr.2    Ishiwata, S.3    Hirano, K.4    Nishizaka, T.5    Hayakawa, T.6
  • 19
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A., and T. Yanagida. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature. 334:74-76.
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 20
    • 0024462505 scopus 로고
    • Hemolytic holes in human erythrocyte membrane ghosts
    • Lieber, M. R., and T. L. Steck. 1989. Hemolytic holes in human erythrocyte membrane ghosts. Meth. Enzymol. 173:356-367.
    • (1989) Meth. Enzymol. , vol.173 , pp. 356-367
    • Lieber, M.R.1    Steck, T.L.2
  • 21
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., D. Popp, and K. C. Holmes. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 22
    • 0023600841 scopus 로고
    • Erythrocyte adducin: A calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding
    • Mische, S. M., M. S. Mooseker, and J. S. Morrow. 1987. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. J. Cell Biol, 105:2837-2845.
    • (1987) J. Cell Biol , vol.105 , pp. 2837-2845
    • Mische, S.M.1    Mooseker, M.S.2    Morrow, J.S.3
  • 23
    • 0028263839 scopus 로고
    • Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects
    • Mohandas, N., and E. Evans. 1994. Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects. Ann. Rev. Biophys. Biomol. Struct. 23:787-818.
    • (1994) Ann. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 24
    • 0025175943 scopus 로고
    • Effects of deficiencies of glycophorins C and D on the physical properties of the red cell
    • Nash, G. B., J. Parmar, M. E. Reid. 1990. Effects of deficiencies of glycophorins C and D on the physical properties of the red cell. Brit. J. Haemat. 76:282-287.
    • (1990) Brit. J. Haemat. , vol.76 , pp. 282-287
    • Nash, G.B.1    Parmar, J.2    Reid, M.E.3
  • 25
    • 0031984179 scopus 로고    scopus 로고
    • Fluorescence-imaged microdeformation of the outer hair cell lateral wall
    • Oghalai, J. S., A. A. Patel, T. Nakagawa, and W. E. Brownell. 1998. Fluorescence-imaged microdeformation of the outer hair cell lateral wall. J. Neurosci. 18:48-58.
    • (1998) J. Neurosci. , vol.18 , pp. 48-58
    • Oghalai, J.S.1    Patel, A.A.2    Nakagawa, T.3    Brownell, W.E.4
  • 27
    • 0029006972 scopus 로고
    • Interaction of protein 4.1 with the red cell membrane: Effects of phosphorylation by protein kinase C
    • Pinder, J. C., B. Gardner, and W. B. Gratzer. 1995. Interaction of protein 4.1 with the red cell membrane: effects of phosphorylation by protein kinase C. Biochem. Biophys. Res. Comm 210:478-482.
    • (1995) Biochem. Biophys. Res. Comm , vol.210 , pp. 478-482
    • Pinder, J.C.1    Gardner, B.2    Gratzer, W.B.3
  • 28
    • 0026058552 scopus 로고
    • Bilayer/cytoskeleton interactions in lipid-symmetric erythrocytes assessed by a photoactivable phospholipid analogue
    • Pradhan, D., P. Williamson, and R. A. Schlegel. Bilayer/cytoskeleton interactions in lipid-symmetric erythrocytes assessed by a photoactivable phospholipid analogue. 1991. Biochemistry. 30:7754-7758.
    • (1991) Biochemistry , vol.30 , pp. 7754-7758
    • Pradhan, D.1    Williamson, P.2    Schlegel, R.A.3
  • 29
    • 0025354418 scopus 로고
    • Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1
    • Reid, M. E., Y. Takakuwa, J. Conboy, G. Tchernia, and N. Mohandas. 1990. Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1. Blood. 75:2229-2234.
    • (1990) Blood , vol.75 , pp. 2229-2234
    • Reid, M.E.1    Takakuwa, Y.2    Conboy, J.3    Tchernia, G.4    Mohandas, N.5
  • 30
    • 0032486127 scopus 로고    scopus 로고
    • Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibres
    • Sabido-David, C., S. C. Hopkins, L. D. Saraswat, S. Lowey, Y. E. Goldman, and M. Irving. 1998. Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibres. J. Mol. Biol. 279:387-402.
    • (1998) J. Mol. Biol. , vol.279 , pp. 387-402
    • Sabido-David, C.1    Hopkins, S.C.2    Saraswat, L.D.3    Lowey, S.4    Goldman, Y.E.5    Irving, M.6
  • 31
    • 0025950955 scopus 로고
    • Distance between skeletal protein 4.1 and the erythrocyte membrane bilayer measured by resonance energy transfer
    • Shahrokh, Z., A. S. Verkman, and S. B. Shohet. 1991. Distance between skeletal protein 4.1 and the erythrocyte membrane bilayer measured by resonance energy transfer. J. Biol. Chem 266:12082-12089.
    • (1991) J. Biol. Chem , vol.266 , pp. 12082-12089
    • Shahrokh, Z.1    Verkman, A.S.2    Shohet, S.B.3
  • 32
    • 0022486512 scopus 로고
    • Ultrastructure of the intact skeleton of the human erythrocyte membrane
    • Shen, B. W., R. Josephs, and T. L. Steck. 1986. Ultrastructure of the intact skeleton of the human erythrocyte membrane. J. Cell. Biol. 102: 997-1006.
    • (1986) J. Cell. Biol. , vol.102 , pp. 997-1006
    • Shen, B.W.1    Josephs, R.2    Steck, T.L.3
  • 33
    • 0028348960 scopus 로고
    • Quantitation of the number of molecules of glycophorins C and D on normal red blood cells using radioiodinated Fab fragments of monoclonal antibodies
    • Smythe, J., B. Gardner, and D. J. Anstee. 1994. Quantitation of the number of molecules of glycophorins C and D on normal red blood cells using radioiodinated Fab fragments of monoclonal antibodies. Blood. 83: 1668-1672.
    • (1994) Blood , vol.83 , pp. 1668-1672
    • Smythe, J.1    Gardner, B.2    Anstee, D.J.3
  • 34
    • 0020570547 scopus 로고
    • Pinocytosis and locomotion of amoebae. XIX. Immunocytochemical demonstration of actin and myosin in Amoeba proteus
    • Stockem, W., W. Naib-Majani, K. E. Wohlfarth-Bottermann, M. Osborn, and K. Weber. 1983. Pinocytosis and locomotion of amoebae. XIX. Immunocytochemical demonstration of actin and myosin in Amoeba proteus. Eur. J. Cell. Bio. 29:171-178.
    • (1983) Eur. J. Cell. Bio. , vol.29 , pp. 171-178
    • Stockem, W.1    Naib-Majani, W.2    Wohlfarth-Bottermann, K.E.3    Osborn, M.4    Weber, K.5
  • 35
    • 0022646311 scopus 로고
    • Spectrin, human erythrocyte shapes, and mechanochemical properties
    • Stokke, B. T., A. Mikkelsen, and A. Elgsaeter. 1986. Spectrin, human erythrocyte shapes, and mechanochemical properties. Biophys. J. 49: 319-327.
    • (1986) Biophys. J. , vol.49 , pp. 319-327
    • Stokke, B.T.1    Mikkelsen, A.2    Elgsaeter, A.3
  • 36
    • 0029821217 scopus 로고    scopus 로고
    • Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe haemolytic anaemia despite a normal membrane skeleton
    • Southgate, C. D., A. H. Chishti, B. Mitchell, S. J. Yi, J. Palek. 1996. Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe haemolytic anaemia despite a normal membrane skeleton. Nat. Genet. 14:227-230.
    • (1996) Nat. Genet. , vol.14 , pp. 227-230
    • Southgate, C.D.1    Chishti, A.H.2    Mitchell, B.3    Yi, S.J.4    Palek, J.5
  • 37
    • 0017172843 scopus 로고
    • Fluctuations and mechanical strength of alpha-helices of polyglycine and poly(L-alanine)
    • Suezaki, Y., and N. Go. 1976. Fluctuations and mechanical strength of alpha-helices of polyglycine and poly(L-alanine). Biopolymers. 15: 2137-2153.
    • (1976) Biopolymers , vol.15 , pp. 2137-2153
    • Suezaki, Y.1    Go, N.2
  • 38
    • 0022518092 scopus 로고
    • Restoration of normal membrane stability to unstable protein 4.1-deficient erythrocyte membranes by incorporation of purified protein 4.1
    • Takakuwa, Y., G. Tchemia, M. Rossi, M. Benabadji, and N. Mohandas. 1986. Restoration of normal membrane stability to unstable protein 4.1-deficient erythrocyte membranes by incorporation of purified protein 4.1. J. Clin. Invest. 78:80-85.
    • (1986) J. Clin. Invest. , vol.78 , pp. 80-85
    • Takakuwa, Y.1    Tchemia, G.2    Rossi, M.3    Benabadji, M.4    Mohandas, N.5
  • 39
    • 0029127417 scopus 로고
    • Effect of cytochalasin D on the mechanical properties and morphology of passive human neutrophils
    • Ting-Beall, H. P., A. S. Lee, and R. M. Hochmuth. 1995. Effect of cytochalasin D on the mechanical properties and morphology of passive human neutrophils. Ann. Biomed. Eng. 23:666-671.
    • (1995) Ann. Biomed. Eng. , vol.23 , pp. 666-671
    • Ting-Beall, H.P.1    Lee, A.S.2    Hochmuth, R.M.3
  • 40
    • 0016756968 scopus 로고
    • Polarization from a helix of fluorophores and its relation to that obtained from muscle
    • Tregear, T. T., and M. Mendelson. 1975. Polarization from a helix of fluorophores and its relation to that obtained from muscle. Biophys. J. 15:455-466.
    • (1975) Biophys. J. , vol.15 , pp. 455-466
    • Tregear, T.T.1    Mendelson, M.2
  • 41
    • 0023688017 scopus 로고
    • Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork
    • Tsuji, A., K. Kawasaki, S. Ohnishi, H. Merkle, and A. Kusumi. 1988. Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork. Biochemistry. 27: 7447-7452.
    • (1988) Biochemistry , vol.27 , pp. 7447-7452
    • Tsuji, A.1    Kawasaki, K.2    Ohnishi, S.3    Merkle, H.4    Kusumi, A.5
  • 42
    • 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, J. M., W. R. Hargreaves, and D. Branton. 1979. 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. 76:5192-5196.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5192-5196
    • Tyler, J.M.1    Hargreaves, W.R.2    Branton, D.3
  • 43
    • 0028246498 scopus 로고
    • Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons
    • Ursitti, J. A., and V. M. Fowler. 1994. Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons. J.Cell. Sci. 107:1633-1639.
    • (1994) J.cell. Sci. , vol.107 , pp. 1633-1639
    • Ursitti, J.A.1    Fowler, V.M.2
  • 44
    • 0023915893 scopus 로고
    • Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis
    • Waugh, R. E., and P. Agre. 1988. Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis. J. Clin. Invest. 81:133-141.
    • (1988) J. Clin. Invest. , vol.81 , pp. 133-141
    • Waugh, R.E.1    Agre, P.2
  • 45


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