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Volumn 1798, Issue 6, 2010, Pages 1090-1099

Surface-induced phase separation of a sphingomyelin/cholesterol/ganglioside GM1-planar bilayer on mica surfaces and microdomain molecular conformation that accelerates Aβ oligomerization

Author keywords

Cholesterol; Ganglioside GM1; Lipid bilayer; Molecular dynamics; Phase separation; Sphingomyelin

Indexed keywords

AMYLOID BETA PROTEIN; CHOLESTEROL; GANGLIOSIDE GM1; MICA; SILICON DIOXIDE; SPHINGOMYELIN;

EID: 77952510090     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.03.003     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 0025021931 scopus 로고
    • The role(s) of gangliosides in neural differentiation and repair: a perspective
    • Schengrund C.L. The role(s) of gangliosides in neural differentiation and repair: a perspective. Brain Res. Bull. 1990, 24:131-141.
    • (1990) Brain Res. Bull. , vol.24 , pp. 131-141
    • Schengrund, C.L.1
  • 2
    • 36448995805 scopus 로고    scopus 로고
    • Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains
    • Ngamukote S., Yanagisawa M., Ariga T., Ando S., Yu R.K. Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains. J. Neurochem. 2007, 103:2327-2341.
    • (2007) J. Neurochem. , vol.103 , pp. 2327-2341
    • Ngamukote, S.1    Yanagisawa, M.2    Ariga, T.3    Ando, S.4    Yu, R.K.5
  • 3
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K., Odaka A., Suzuki N., Ihara Y. GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nat. Med. 1995, 1:1062-1066.
    • (1995) Nat. Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 4
    • 0030823756 scopus 로고    scopus 로고
    • Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles
    • Choo-Smith L.P., Garzon-Rodriguez W., Glabe C.G., Surewicz W.K. Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles. J. Biol. Chem. 1997, 272:22987-22990.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22987-22990
    • Choo-Smith, L.P.1    Garzon-Rodriguez, W.2    Glabe, C.G.3    Surewicz, W.K.4
  • 5
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid
    • Kakio A., Nishimoto S., Yanagisawa K., Kozutsumi Y., Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 2001, 276:24985-24990.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 6
    • 0037062582 scopus 로고    scopus 로고
    • Interactions of amyloid β-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid
    • Kakio A., Nishimoto S., Yanagisawa K., Kozutsumi Y., Matsuzaki K. Interactions of amyloid β-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 2002, 41:7385-7390.
    • (2002) Biochemistry , vol.41 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 8
    • 34047269583 scopus 로고    scopus 로고
    • GM1-ganglioside-induced Aβ assembly on synaptic membranes of cultured neurons
    • Yamamoto N., Fukata Y., Fukata M., Yanagisawa K. GM1-ganglioside-induced Aβ assembly on synaptic membranes of cultured neurons. Biochim. Biophys. Acta 2007, 1768:1128-1137.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1128-1137
    • Yamamoto, N.1    Fukata, Y.2    Fukata, M.3    Yanagisawa, K.4
  • 9
    • 34447255463 scopus 로고    scopus 로고
    • Formation of toxic fibrils of Alzheimer's amyloid β-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component
    • Okada T., Wakabayashi M., Ikeda K., Matsuzaki K. Formation of toxic fibrils of Alzheimer's amyloid β-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component. J. Mol. Biol. 2007, 371:481-489.
    • (2007) J. Mol. Biol. , vol.371 , pp. 481-489
    • Okada, T.1    Wakabayashi, M.2    Ikeda, K.3    Matsuzaki, K.4
  • 11
    • 33847076858 scopus 로고    scopus 로고
    • Ganglioside GM1-mediated amyloid-beta fibrillogenesis and membrane disruption
    • Chi E.Y., Frey S.L., Lee K.Y.C. Ganglioside GM1-mediated amyloid-beta fibrillogenesis and membrane disruption. Biochemistry 2007, 46:1913-1924.
    • (2007) Biochemistry , vol.46 , pp. 1913-1924
    • Chi, E.Y.1    Frey, S.L.2    Lee, K.Y.C.3
  • 12
    • 46549089088 scopus 로고    scopus 로고
    • Development of photocrosslinked sialic acid containing polymers for use in Aβ toxicity attenuation
    • Cowan C.B., Coté G.L., Good T.A. Development of photocrosslinked sialic acid containing polymers for use in Aβ toxicity attenuation. Biomaterials 2008, 29:3408-3414.
    • (2008) Biomaterials , vol.29 , pp. 3408-3414
    • Cowan, C.B.1    Coté, G.L.2    Good, T.A.3
  • 13
    • 0032548943 scopus 로고    scopus 로고
    • Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides
    • McLaurin J., Franklin T., Fraser P.E., Chakrabartty A. Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides. J. Biol. Chem. 1998, 273:4506-4515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4506-4515
    • McLaurin, J.1    Franklin, T.2    Fraser, P.E.3    Chakrabartty, A.4
  • 14
    • 0036791002 scopus 로고    scopus 로고
    • One O-linked sugar can affect the coil-to-β structural transition of the prion peptide
    • Chen P.Y., Lin C.C., Chang Y.T., Lin S.C., Chan S.I. One O-linked sugar can affect the coil-to-β structural transition of the prion peptide. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:12633-12638.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12633-12638
    • Chen, P.Y.1    Lin, C.C.2    Chang, Y.T.3    Lin, S.C.4    Chan, S.I.5
  • 15
    • 33846036362 scopus 로고    scopus 로고
    • Monomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock-lock mechanism
    • Nguyen P.H., Li M.S., Stock G., Straub J.E., Thirumalai D. Monomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock-lock mechanism. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:111-116.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 111-116
    • Nguyen, P.H.1    Li, M.S.2    Stock, G.3    Straub, J.E.4    Thirumalai, D.5
  • 17
    • 33846228438 scopus 로고    scopus 로고
    • Molecular dynamics studies of hexamers of amyloid-β peptide (16-35) and its mutants: influence of charge states on amyloid formation
    • Han W., Wu Y.D. Molecular dynamics studies of hexamers of amyloid-β peptide (16-35) and its mutants: influence of charge states on amyloid formation. Proteins 2007, 66:575-587.
    • (2007) Proteins , vol.66 , pp. 575-587
    • Han, W.1    Wu, Y.D.2
  • 18
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrate that Amyloid(beta)(1-40) and Amyloid(beta)(1-42) form different fibrillar structures under identical conditions
    • Olofsson A., Lindhagen-Persson M., Sauer-Eriksson A.E., Öhman A. Amide solvent protection analysis demonstrate that Amyloid(beta)(1-40) and Amyloid(beta)(1-42) form different fibrillar structures under identical conditions. Biochem. J. 2007, 404:63-70.
    • (2007) Biochem. J. , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Öhman, A.4
  • 19
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova A.T., Yau W.M., Tycko R. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 2006, 45:498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 22
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 23
    • 4143091360 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy relates rafts in model and native membranes
    • Bacia K., Scherfeld D., Kahya N., Schwille P. Fluorescence correlation spectroscopy relates rafts in model and native membranes. Biophys. J. 2004, 87:1034-1043.
    • (2004) Biophys. J. , vol.87 , pp. 1034-1043
    • Bacia, K.1    Scherfeld, D.2    Kahya, N.3    Schwille, P.4
  • 24
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there?
    • Chini B., Parenti M. G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there?. J. Mol. Endocrinol. 2004, 32:325-338.
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 26
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton R.G. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 1994, 42:155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 27
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: scientific and practical applications
    • Sackmann E. Supported membranes: scientific and practical applications. Science 1996, 271:43-48.
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 28
    • 49449108464 scopus 로고    scopus 로고
    • Multiplexing ligand-receptor binding measurements by chemically patterning microfluidic channels
    • Shi J.J., Yang T.L., Cremer P.S. Multiplexing ligand-receptor binding measurements by chemically patterning microfluidic channels. Anal. Chem. 2008, 80:6078-6084.
    • (2008) Anal. Chem. , vol.80 , pp. 6078-6084
    • Shi, J.J.1    Yang, T.L.2    Cremer, P.S.3
  • 29
    • 51649092841 scopus 로고    scopus 로고
    • Quantitative fluorescence microscopy using supported lipid bilayer standards
    • Galush W.J., Nye J.A., Groves J.T. Quantitative fluorescence microscopy using supported lipid bilayer standards. Biophys. J. 2008, 95:2512-2519.
    • (2008) Biophys. J. , vol.95 , pp. 2512-2519
    • Galush, W.J.1    Nye, J.A.2    Groves, J.T.3
  • 30
    • 33845195666 scopus 로고    scopus 로고
    • Lipid lateral mobility and membrane phase structure modulation by protein binding
    • Forstner M.B., Yee C.K., Parikh A.N., Groves J.T. Lipid lateral mobility and membrane phase structure modulation by protein binding. J. Am. Chem. Soc. 2006, 128:15221-15227.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15221-15227
    • Forstner, M.B.1    Yee, C.K.2    Parikh, A.N.3    Groves, J.T.4
  • 31
    • 34248582600 scopus 로고    scopus 로고
    • GM1 clustering inhibits cholera toxin binding in supported phospholipid membranes
    • Shi J., Yang T., Kataoka S., Zhang Y., Diaz A.J., Cremer P.S. GM1 clustering inhibits cholera toxin binding in supported phospholipid membranes. J. Am. Chem. Soc. 2007, 129:5954-5961.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5954-5961
    • Shi, J.1    Yang, T.2    Kataoka, S.3    Zhang, Y.4    Diaz, A.J.5    Cremer, P.S.6
  • 32
    • 33749359415 scopus 로고    scopus 로고
    • Phase separation of lipid membranes analyzed with high-resolution secondary ion mass spectrometry
    • Kraft M.L., Weber P.K., Longo M.L., Hutcheon I.D., Boxer S.G. Phase separation of lipid membranes analyzed with high-resolution secondary ion mass spectrometry. Science 2006, 313:1948-1951.
    • (2006) Science , vol.313 , pp. 1948-1951
    • Kraft, M.L.1    Weber, P.K.2    Longo, M.L.3    Hutcheon, I.D.4    Boxer, S.G.5
  • 33
    • 0034695038 scopus 로고    scopus 로고
    • Advances in the characterization of supported lipid films with the atomic force microscope
    • Dufrêne Y.F., Lee G.U. Advances in the characterization of supported lipid films with the atomic force microscope. Biochim. Biophys. Acta 2000, 1509:14-41.
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 14-41
    • Dufrêne, Y.F.1    Lee, G.U.2
  • 34
    • 27744527489 scopus 로고    scopus 로고
    • Relating structure, biomechanics and function of single membrane proteins
    • Contera S.A., Lemaitre V., de Planque M.R.R., Watts A., Ryan J.F. Relating structure, biomechanics and function of single membrane proteins. Biophys. J. 2005, 89:3129-3140.
    • (2005) Biophys. J. , vol.89 , pp. 3129-3140
    • Contera, S.A.1    Lemaitre, V.2    de Planque, M.R.R.3    Watts, A.4    Ryan, J.F.5
  • 37
    • 0017383689 scopus 로고
    • Lateral diffusion in phospholipid multibilayers measured by fluorescence recovery after photobleaching
    • E-S Wu., Jacobson K., Papahadjopoulos D. Lateral diffusion in phospholipid multibilayers measured by fluorescence recovery after photobleaching. Biochemistry 1977, 16:3936-3941.
    • (1977) Biochemistry , vol.16 , pp. 3936-3941
    • E-S, W.1    Jacobson, K.2    Papahadjopoulos, D.3
  • 38
    • 0030753816 scopus 로고    scopus 로고
    • Lipid domains in the membrane: thermotropic properties of sphingomyelin vesicles containing GM1 ganglioside and cholesterol
    • Ferraretto A., Pitto M., Palestini P., Masserini M. Lipid domains in the membrane: thermotropic properties of sphingomyelin vesicles containing GM1 ganglioside and cholesterol. Biochemistry 1997, 36:9232-9236.
    • (1997) Biochemistry , vol.36 , pp. 9232-9236
    • Ferraretto, A.1    Pitto, M.2    Palestini, P.3    Masserini, M.4
  • 39
    • 0034906633 scopus 로고    scopus 로고
    • Atomic force microscopy studies of ganglioside GM1 domains in phosphatidylcholine and phosphatidylcholine/cholesterol bilayers
    • Yuan C., Johnston L.J. Atomic force microscopy studies of ganglioside GM1 domains in phosphatidylcholine and phosphatidylcholine/cholesterol bilayers. Biophys. J. 2001, 81:1059-1069.
    • (2001) Biophys. J. , vol.81 , pp. 1059-1069
    • Yuan, C.1    Johnston, L.J.2
  • 41
    • 0028324639 scopus 로고
    • Direct evidence of induction of interdigitated gel structure in large unilamellar vesicles of dipalmitoylphosphatidylcholine by ethanol: studies by excimer method and high-resolution electron cryomicroscopy
    • Yamazaki M., Miyazu M., Asano T., Yuba A., Kume N. Direct evidence of induction of interdigitated gel structure in large unilamellar vesicles of dipalmitoylphosphatidylcholine by ethanol: studies by excimer method and high-resolution electron cryomicroscopy. Biophys. J. 1994, 66:729-733.
    • (1994) Biophys. J. , vol.66 , pp. 729-733
    • Yamazaki, M.1    Miyazu, M.2    Asano, T.3    Yuba, A.4    Kume, N.5
  • 42
    • 0030950270 scopus 로고    scopus 로고
    • Probing the ethanol-induced chain interdigitations in gel-state bilayers of mixed-chain phosphatidylcholines
    • Huang C., McIntosh T.J. Probing the ethanol-induced chain interdigitations in gel-state bilayers of mixed-chain phosphatidylcholines. Biophys. J. 1997, 72:2702-2709.
    • (1997) Biophys. J. , vol.72 , pp. 2702-2709
    • Huang, C.1    McIntosh, T.J.2
  • 43
    • 24144473649 scopus 로고    scopus 로고
    • True atomic resolution in liquid by frequency-modulation atomic force microscopy
    • Fukuma T., Kobayashi K., Matsushige K., Yamada H. True atomic resolution in liquid by frequency-modulation atomic force microscopy. Appl. Phys. Lett. 2005, 87:34101-34103.
    • (2005) Appl. Phys. Lett. , vol.87 , pp. 34101-34103
    • Fukuma, T.1    Kobayashi, K.2    Matsushige, K.3    Yamada, H.4
  • 44
    • 0037135766 scopus 로고    scopus 로고
    • Structure of water adsorbed on a mica surface
    • Park S.H., Sposito G. Structure of water adsorbed on a mica surface. Phys. Rev. Lett. 2002, 89:85501-85503.
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 85501-85503
    • Park, S.H.1    Sposito, G.2


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