메뉴 건너뛰기




Volumn 349, Issue 1, 2000, Pages 299-308

Oligomerization of β-amyloid of the Alzheimer's and the Dutch-cerebral-haemorrhage types

Author keywords

Apoptosis; ELISA; Fibril; Parallel sheet; Toxicity

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0034235515     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3490299     Document Type: Article
Times cited : (60)

References (42)
  • 1
    • 0024412495 scopus 로고
    • Molecular biology of Alzheimer's disease
    • 1 Muller-Hill, B. and Beyreuther, K. (1989) Molecular biology of Alzheimer's disease. Annu. Rev Biochem. 58, 287-307
    • (1989) Annu. Rev Biochem. , vol.58 , pp. 287-307
    • Muller-Hill, B.1    Beyreuther, K.2
  • 2
    • 0025367646 scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis-Dutch type. Clinical and computed tomographic analysis of 24 cases
    • 2 Haan, J. Algra, P. R. and Roos, R. A. C. (1990) Hereditary cerebral hemorrhage with amyloidosis-Dutch type. Clinical and computed tomographic analysis of 24 cases. Arch. Neurol. 47, 649-653
    • (1990) Arch. Neurol. , vol.47 , pp. 649-653
    • Haan, J.1    Algra, P.R.2    Roos, R.A.C.3
  • 3
    • 0028031458 scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis (Dutch): A model for congophilic plaque formation without neurofibrillary pathology
    • 3 Maat-Schieman, M. L., van Duinen, S. G., Rozemuller, A. J., Haan, J. and Roos, R. A. (1994) Hereditary cerebral hemorrhage with amyloidosis (Dutch): a model for congophilic plaque formation without neurofibrillary pathology. Acta Neuropathol. 88, 371-378
    • (1994) Acta Neuropathol. , vol.88 , pp. 371-378
    • Maat-Schieman, M.L.1    Van Duinen, S.G.2    Rozemuller, A.J.3    Haan, J.4    Roos, R.A.5
  • 4
    • 0033564290 scopus 로고    scopus 로고
    • 693 → Gln 'Dutch' mutation on the production and stability of amyloid β-protein
    • 693 → Gln 'Dutch' mutation on the production and stability of amyloid β-protein. Biochem. J. 340, 703-709
    • (1999) Biochem. J. , vol.340 , pp. 703-709
    • Watson, D.J.1    Selkoe, D.J.2    Teplow, D.B.3
  • 5
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • 5 Pike, C. J., Burdick, A. J., Walencewicz, C. G., Glabe, C. G. and Cotman, C. W. (1993) Neurodegeneration induced by β-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, A.J.2    Walencewicz, C.G.3    Glabe, C.G.4    Cotman, C.W.5
  • 6
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • 6 Lorenzo, A. and Yankner, B. A. (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. U.S.A. 91, 12242-12247
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12242-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 7
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated beta-amyloid peptide are attenuated by basic FGF
    • 7 Mattson, M. P., Tomaselli, K. J. and Rydel, R. E. (1993) Calcium-destabilizing and neurodegenerative effects of aggregated beta-amyloid peptide are attenuated by basic FGF. Brain Res. 621, 35-49
    • (1993) Brain Res. , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.J.2    Rydel, R.E.3
  • 8
    • 0032105394 scopus 로고    scopus 로고
    • The role of A beta 42 in Alzheimer's disease
    • 8 Younkin, S. G. (1998) The role of A beta 42 in Alzheimer's disease. J. Physiol. (London) 92, 289-292
    • (1998) J. Physiol. (London) , vol.92 , pp. 289-292
    • Younkin, S.G.1
  • 9
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • 9 Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., 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.3    Diehl, T.4    Vassilev, P.M.5    Teplow, D.B.6    Selkoe, D.J.7
  • 10
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture
    • 10 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
  • 11
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Aβ-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • 11 Roher, A. E., Chaney, M. O., Kuo, Y. M., Webster, S. D., Stine, W. B., Haverkamp, L. J., Woods, A. S., Cotter, R. J. et al. (1996) Morphology and toxicity of Aβ-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J. Biol. Chem. 271, 20631-20635
    • (1996) J. Biol. Chem. , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Kuo, Y.M.3    Webster, S.D.4    Stine, W.B.5    Haverkamp, L.J.6    Woods, A.S.7    Cotter, R.J.8
  • 12
    • 0030611858 scopus 로고    scopus 로고
    • Soluble amyloid Aβ-(1-40) exists as a stable dimer at low concentrations
    • 12 Garzon-Rodriguez, W., Sepulveda-Becerra, M., Milton, S. and Glabe, C. G. (1997) Soluble amyloid Aβ-(1-40) exists as a stable dimer at low concentrations. J. Biol. Chem. 272, 21037-21044
    • (1997) J. Biol. Chem. , vol.272 , pp. 21037-21044
    • Garzon-Rodriguez, W.1    Sepulveda-Becerra, M.2    Milton, S.3    Glabe, C.G.4
  • 13
    • 0032983254 scopus 로고    scopus 로고
    • Presence of sodium dodecyl sulfate-stable amyloid beta-protein dimers in the hippocampus CA1 not exhibiting neurofibrillary tangle formation
    • 13 Funato, H., Enya, M., Yoshimura, M., Morishima-Kawashima, M. and Ihara, Y. (1999) Presence of sodium dodecyl sulfate-stable amyloid beta-protein dimers in the hippocampus CA1 not exhibiting neurofibrillary tangle formation. Am. J. Pathol. 155, 23-28
    • (1999) Am. J. Pathol. , vol.155 , pp. 23-28
    • Funato, H.1    Enya, M.2    Yoshimura, M.3    Morishima-Kawashima, M.4    Ihara, Y.5
  • 14
    • 0002931434 scopus 로고    scopus 로고
    • Improved solid-phase synthesis of amyloid proteins associated with neurodegenerative diseases
    • 14 El-Agnaf, O. M. A., Goodwin, H., Sheridan, J. M., Frears, E. R. and Austen, B. M. (1999) Improved solid-phase synthesis of amyloid proteins associated with neurodegenerative diseases. Pep. Protein Lett. 7, 1-8
    • (1999) Pep. Protein Lett. , vol.7 , pp. 1-8
    • El-Agnaf, O.M.A.1    Goodwin, H.2    Sheridan, J.M.3    Frears, E.R.4    Austen, B.M.5
  • 15
    • 0029864517 scopus 로고    scopus 로고
    • Metabolites of the beta-amyloid precursor protein generated by beta-secretase localise to the trans-Golgi network and late endosome in 293 cells
    • 15 Stephens, D. J. and Austen, B. M. (1996) Metabolites of the beta-amyloid precursor protein generated by beta-secretase localise to the trans-Golgi network and late endosome in 293 cells. J. Neurosci. Res. 45, 211-225
    • (1996) J. Neurosci. Res. , vol.45 , pp. 211-225
    • Stephens, D.J.1    Austen, B.M.2
  • 16
    • 0032573597 scopus 로고    scopus 로고
    • Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments
    • 16 El-Agnaf, O. M. A., Jakes, R., Curran, M. D., Middleton, D., Ingenito, R., Bianchi, E., Pessi, A., Neill, D. and Wallace, A. (1998) Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett. 440, 71-75
    • (1998) FEBS Lett. , vol.440 , pp. 71-75
    • El-Agnaf, O.M.A.1    Jakes, R.2    Curran, M.D.3    Middleton, D.4    Ingenito, R.5    Bianchi, E.6    Pessi, A.7    Neill, D.8    Wallace, A.9
  • 17
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • 17 Denziot, F. and Lang, R., (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J. Immunol. Methods 89, 271-277
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denziot, F.1    Lang, R.2
  • 18
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • 18 Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M. B., Teplow, D. B., Haas, C., Seubert, P., Koo, E. H. and Selkoe, D. J. (1997) Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272, 7977-7982
    • (1997) J. Biol. Chem. , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haas, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 19
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • 19 Pitschke, M., Prior, R., Haupt, M. and Riesner, D. (1998) Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy. Nat. Med. 4, 832-834
    • (1998) Nat. Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 20
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • 20 Harper, J. D., Wong, S. S., Lieber, C. M. and Lansbury, P. T. (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 21
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • 21 Walsh, D. M., Lomarkin, 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    Lomarkin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 23
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease
    • 23 Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C. L. and Beyreuther, K. (1991) Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease. J. Mol. Biol. 218, 149-163
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 24
    • 0033543141 scopus 로고    scopus 로고
    • Deposition of monomeric, not oligomeric, Aβ mediates growth of Alzheimer Disease amyloid plaques in human brain preparations
    • 24 Tseng, B. P., Esler, W. P., Clish, C. B., Stimson, E. R., Ghilardi, J. R., Vinters, H. V., Mantyh, P. W., Lee, J. P. and Maggio, J. E. (1999) Deposition of monomeric, not oligomeric, Aβ mediates growth of Alzheimer Disease amyloid plaques in human brain preparations. Biochemistry 38, 633-642
    • (1999) Biochemistry , vol.38 , pp. 633-642
    • Tseng, B.P.1    Esler, W.P.2    Clish, C.B.3    Stimson, E.R.4    Ghilardi, J.R.5    Vinters, H.V.6    Mantyh, P.W.7    Lee, J.P.8    Maggio, J.E.9
  • 26
    • 0027330265 scopus 로고
    • Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid beta/A4 peptide
    • 26 Clements, A., Walsh, D. M., Williams, C. H. and Allsop, D. (1993) Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid beta/A4 peptide. Neurosci. Lett. 161, 17-20
    • (1993) Neurosci. Lett. , vol.161 , pp. 17-20
    • Clements, A.1    Walsh, D.M.2    Williams, C.H.3    Allsop, D.4
  • 27
    • 0026045862 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation
    • 27 Wisniewski, T., Ghiso, J. and Frangione, B. (1991) Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation. Biochem. Biophys. Res. Commun. 179, 1247-1254
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1247-1254
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 28
    • 0030778396 scopus 로고    scopus 로고
    • Hemin and related porphyrins inhibit β-amyloid aggregation
    • 28 Howlett, D., Cutler, P., Heales, S. and Cammilleri, P (1997) Hemin and related porphyrins inhibit β-amyloid aggregation. FEBS. Lett. 417, 249-251
    • (1997) FEBS. Lett. , vol.417 , pp. 249-251
    • Howlett, D.1    Cutler, P.2    Heales, S.3    Cammilleri, P.4
  • 32
    • 0032530466 scopus 로고    scopus 로고
    • The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's beta-amyloid peptide
    • 32 El-Agnaf, O. M. A., Guthrie, D. J. S., Walsh, D. M. and Irvine, G. B. (1998) The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's beta-amyloid peptide. Eur. J. Biochem. 256, 560-569
    • (1998) Eur. J. Biochem. , vol.256 , pp. 560-569
    • El-Agnaf, O.M.A.1    Guthrie, D.J.S.2    Walsh, D.M.3    Irvine, G.B.4
  • 33
    • 0027249811 scopus 로고
    • Comparative analysis of human and Dutch-type Alzheimer beta-amyloid peptides by infrared spectroscopy and circular dichroism
    • 33 Fabian, H., Szendrei, G. I., Mantsch, H. H. and Otvos, L. (1993) Comparative analysis of human and Dutch-type Alzheimer beta-amyloid peptides by infrared spectroscopy and circular dichroism. Biochem. Biophys. Res. Commun. 191, 232-239
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 232-239
    • Fabian, H.1    Szendrei, G.I.2    Mantsch, H.H.3    Otvos, L.4
  • 36
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • 36 Anderson, A. J., Su, J. H. and Cotman, C. W. (1996) DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J. Neurosci. 16, 1710-1719
    • (1996) J. Neurosci. , vol.16 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 37
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct liber morphology
    • 37 Seilheimer, B., Bohrmann, B., Bondolfi, L., Muller, F., Stuber, D. and Dobeli, H. (1997) The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct liber 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
  • 38
    • 0026453127 scopus 로고
    • Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein
    • 38 Fraser, P. E., Nguyen, J. T., Inouye, H., Surewicz, W. K., Selkoe, D. J., Podlisny, M. B. and Kirschner, D. A. (1992) Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein. Biochemistry 31, 107161-10723
    • (1992) Biochemistry , vol.31 , pp. 107161-110723
    • Fraser, P.E.1    Nguyen, J.T.2    Inouye, H.3    Surewicz, W.K.4    Selkoe, D.J.5    Podlisny, M.B.6    Kirschner, D.A.7
  • 40
    • 0029920991 scopus 로고    scopus 로고
    • Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein
    • 40 Davis, J. and van Nostrand, W. E. (1996) Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein. Proc. Natl. Acad. Sci. U.S.A. 93, 2996-3000
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 2996-3000
    • Davis, J.1    Van Nostrand, W.E.2
  • 41
    • 0031983456 scopus 로고    scopus 로고
    • Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells
    • 41 van Nostrand, W. E., Melchor, J. P. and Ruffinini, L. (1998) Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J. Neurochem. 70, 216-223
    • (1998) J. Neurochem. , vol.70 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffinini, L.3
  • 42
    • 0031017399 scopus 로고    scopus 로고
    • Rapid degeneration of cultured human brain pericytes by amyloid beta protein
    • 42 Verbeek, M. M., Dewaal, R. M. W., Schipper, J. J. and van Nostrand, W. E. (1997) Rapid degeneration of cultured human brain pericytes by amyloid beta protein. J. Neurochem. 68, 1135-1141
    • (1997) J. Neurochem. , vol.68 , pp. 1135-1141
    • Verbeek, M.M.1    Dewaal, R.M.W.2    Schipper, J.J.3    Van Nostrand, W.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.