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Volumn 348, Issue 1, 2000, Pages 137-144

Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of β-amyloid peptide

Author keywords

Alzheimer's disease; Density gradient centrifugation; Protofibrils

Indexed keywords

AMYLOID BETA PROTEIN; NEUROTOXIN; OLIGOMER;

EID: 0034658615     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3480137     Document Type: Article
Times cited : (151)

References (42)
  • 1
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • 1 Glenner, G. G. and Wong, C. W. (1984) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122, 1131-1135
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 3
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • 3 Selkoe, D. J. (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 4
    • 0024472693 scopus 로고
    • Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease
    • 4 Yankner, B. A., Dawes, L. R., Fisher, S., Villa-Komaroff, L., Oster-Granite, M. L. and Neve, R. L. (1989) Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease. Science 245, 417-420
    • (1989) Science , vol.245 , pp. 417-420
    • Yankner, B.A.1    Dawes, L.R.2    Fisher, S.3    Villa-Komaroff, L.4    Oster-Granite, M.L.5    Neve, R.L.6
  • 5
    • 0027217527 scopus 로고
    • Heat shock partially protects rat pheochromocytoma PC12 cells from amyloid beta peptide toxicity
    • 5 Behl, C. and Schubert, D. (1993) Heat shock partially protects rat pheochromocytoma PC12 cells from amyloid beta peptide toxicity. Neurosci. Lett. 154, 1-4
    • (1993) Neurosci. Lett. , vol.154 , pp. 1-4
    • Behl, C.1    Schubert, D.2
  • 7
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro, the role of peptide assembly state
    • 7 Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G. and Cotman, C. W. (1993) Neurodegeneration induced by beta-amyloid peptides in vitro, the role of peptide assembly state. J. Neurosci. 13, 1676-1687
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 10
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro
    • 10 Kirschner, D. A., Inouye, H., Duffy, L. K., Sinclair, A., Lind, M. and Selkoe, D. J. (1987) Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. U.S.A. 84, 6953-6957
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6953-6957
    • Kirschner, D.A.1    Inouye, H.2    Duffy, L.K.3    Sinclair, A.4    Lind, M.5    Selkoe, D.J.6
  • 11
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimers beta-amyloid peptide correlates with a distinct fiber morphology
    • 11 Seilheimer, B., Bohrmann, B., Bondolfi, L., Muller, F., Stuber, D. and Dobeli, H. (1997) The toxicity of the Alzheimers beta-amyloid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 119, 59-71
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Dobeli, H.6
  • 15
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell-culture
    • 15 Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydell, R. E., Teplow, D. B. and Selkoe, D. J. (1995) Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell-culture. J. Biol. Chem. 270, 9564-9570
    • (1995) J. Biol. Chem. , vol.270 , pp. 9564-9570
    • Podlisny, M.B.1    Ostaszewski, B.L.2    Squazzo, S.L.3    Koo, E.H.4    Rydell, R.E.5    Teplow, D.B.6    Selkoe, D.J.7
  • 16
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell-culture and stabilization of monomer by congo red
    • 16 Podlisny, M. B., Walsh, D. M., Amarante, P., Ostaszewski, B. L., Stimson, E. R., Maggio, J. E., Teplow, D. B. and Selkoe, D. J. (1998) Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell-culture and stabilization of monomer by congo red. Biochemistry 37, 3602-3611
    • (1998) Biochemistry , vol.37 , pp. 3602-3611
    • Podlisny, M.B.1    Walsh, D.M.2    Amarante, P.3    Ostaszewski, B.L.4    Stimson, E.R.5    Maggio, J.E.6    Teplow, D.B.7    Selkoe, D.J.8
  • 17
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • 17 Jarrett, J. T., Berger, E. P. and Lansbury, Jr., P. T. (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 18
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils - Detection of nuclei and quantitation of rate constants
    • 18 Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A. and Teplow, D. B. (1996) On the nucleation and growth of amyloid beta-protein fibrils - detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. U.S.A. 93, 1125-1129
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 19
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis - Detection of a protofibrillar intermediate
    • 19 Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M. and Teplow, D. B. (1997) Amyloid beta-protein fibrillogenesis - detection of a protofibrillar intermediate. J. Biol. Chem 272, 22364-22372
    • (1997) J. Biol. Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 20
    • 0031444010 scopus 로고    scopus 로고
    • Atomic-force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimers-disease amyloid-beta protein
    • 20 Harper, J. D., Lieber, C. M. and Lansbury, P. T. (1997) Atomic-force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimers-disease amyloid-beta protein. Chem. Biol. 4, 951-959
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 21
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • 21 Pike, C. J., Walencewicz, A. J., Glabe, C. G. and Cotman, C. W. (1991) Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures. Eur. J. Pharmacol 207, 367-368
    • (1991) Eur. J. Pharmacol , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 22
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • 22 Behl, C., Davis, J. B., Lesley, R. and Schubert, D. (1994) Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77, 817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 23
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death
    • 23 Shearman, M. S., Ragan, C. I. and Iversen, L. L. (1994) Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death. Proc. Natl. Acad. Sci. U.S.A. 91, 1470-1474
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 25
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous βA4 peptides in human cerebrospinal-fluid and blood by a newly developed sensitive western-blot assay
    • 25 Ida, N., Hartmann, T., Pantel, J., Schroder, J., Zerfass, R., Forstl, H., Sandbrink, R., Masters, C. L. and Beyreuther, K. (1996) Analysis of heterogeneous βA4 peptides in human cerebrospinal-fluid and blood by a newly developed sensitive western-blot assay. J. Biol. Chem. 271, 22908-22914
    • (1996) J. Biol. Chem. , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 26
    • 0020176542 scopus 로고
    • CONTIN: A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • 26 Provencher, S. W. (1982) CONTIN: A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput. Phys. Commun. 27, 213-227
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 27
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packaging events
    • 27 Laemmli, U. K. and Favre, M. (1973) Maturation of the head of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80, 575-599
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • 28 Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0031559602 scopus 로고    scopus 로고
    • Isolation, chemical characterization, and quantitation of A beta 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits
    • 31 Kuo, Y. M., Emmerling, M. R., Woods, A. S., Cotter, R. J. and Roher, A. E. (1997) Isolation, chemical characterization, and quantitation of A beta 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits. Biochem. Biophys. Res. Commun 237, 188-191
    • (1997) Biochem. Biophys. Res. Commun , vol.237 , pp. 188-191
    • Kuo, Y.M.1    Emmerling, M.R.2    Woods, A.S.3    Cotter, R.J.4    Roher, A.E.5
  • 32
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • 32 Pike, C. J., Walencewicz, A. J., Glabe, C. G. and Cotman, C. W. (1991) In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563, 311-314
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 33
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidoses. The beta-fibrilloses
    • 33 Glenner, G. G. (1980) Amyloid deposits and amyloidoses. The beta-fibrilloses. N. Engl. J. Med. 302, 1283-1292
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 36
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • 36 Lansbury, P. T. (1999) Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. U.S.A. 96, 3342-3344
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3342-3344
    • Lansbury, P.T.1
  • 37
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • 37 Hartley, D. M., Walsh, D. M., Ye, C. P. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B. and Selkoe, D. J. (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19, 8876-8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 38
    • 0030778396 scopus 로고    scopus 로고
    • Hemin and related porphyrins inhibit beta-amyloid aggregation
    • 38 Howlett, D., Cutler, P., Heales, S. and Camilleri, P. (1997) Hemin and related porphyrins inhibit beta-amyloid aggregation. FEBS Lett. 417, 249-251
    • (1997) FEBS Lett. , vol.417 , pp. 249-251
    • Howlett, D.1    Cutler, P.2    Heales, S.3    Camilleri, P.4
  • 39
    • 0033569444 scopus 로고    scopus 로고
    • Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer beta-amyloid fibril formation
    • 39 Howlett, D. R., George, A. R., Owen, D. E., Ward, R. V. and Markwell, R. E. (1999) Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer beta-amyloid fibril formation. Biochem. J. 343, 419-423
    • (1999) Biochem. J. , vol.343 , pp. 419-423
    • Howlett, D.R.1    George, A.R.2    Owen, D.E.3    Ward, R.V.4    Markwell, R.E.5
  • 40
    • 0032729982 scopus 로고    scopus 로고
    • Computationally derived structural models of beta amyloid found in Alzheimer's disease plaques and its interaction with possible aggregation inhibitors
    • 40 George, A. R. and Howlett, D. R. (1999) Computationally derived structural models of beta amyloid found in Alzheimer's disease plaques and its interaction with possible aggregation inhibitors. Biopolymers 50, 733-741
    • (1999) Biopolymers , vol.50 , pp. 733-741
    • George, A.R.1    Howlett, D.R.2
  • 41
    • 0028169925 scopus 로고
    • Visualisation of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is A beta 42(43)
    • 41 Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N. and Ihara, Y. (1994) Visualisation of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is A beta 42(43) Neuron 13, 45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 42
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • 42 Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W. et al. (1996) Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2, 864-870
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6    Bird, T.D.7    Hardy, J.8    Hutton, M.9    Kukull, W.10


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