메뉴 건너뛰기




Volumn 11, Issue 2, 2002, Pages 330-340

In vitro studies of Flemish, Dutch, and wild-type β-amyloid provide evidence for two-staged neurotoxicity

Author keywords

Alzheimer's disease; Amyloid precursor protein; Amyloid ; Cerebral amyloid angiopathy; Neurotoxicity; Phosphorylation; SH SY5Y cells; Tau

Indexed keywords

ACTIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; TAU PROTEIN; TUBULIN;

EID: 0036966278     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1006/nbdi.2002.0529     Document Type: Article
Times cited : (32)

References (41)
  • 1
    • 0033616590 scopus 로고    scopus 로고
    • Unusual phenotypic alteration of beta amyloid precursor protein (betaAPP) maturation by a new Val-715 → Met betaAPP-770 mutation responsible for probable early-onset Alzheimer's disease
    • Ancolio, K., Dumanchin, C., Barelli, H., Warter, J. M., Brice, A., Campion, D., Frebourg, T., & Checler, F. (1999) Unusual phenotypic alteration of beta amyloid precursor protein (betaAPP) maturation by a new Val-715 β Met betaAPP-770 mutation responsible for probable early-onset Alzheimer's disease. Proc. Natl. Acad. Sci. USA 96, 4119-4124.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4119-4124
    • Ancolio, K.1    Dumanchin, C.2    Barelli, H.3    Warter, J.M.4    Brice, A.5    Campion, D.6    Frebourg, T.7    Checler, F.8
  • 2
    • 0028986916 scopus 로고
    • beta-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) beta-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14, 879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 3
    • 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
    • Clements, A., Walsh, D. M., Williams, C. H., & 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
  • 5
    • 0029920991 scopus 로고    scopus 로고
    • Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein
    • Davis, J., & Van Nostrand, W. E. (1996) Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein. Proc. Natl. Acad. Sci. USA 93, 2996-3000.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2996-3000
    • Davis, J.1    Van Nostrand, W.E.2
  • 6
    • 0028982272 scopus 로고
    • Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells
    • Davis-Salinas, J., & Van Nostrand, W. E. (1995) Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells. J. Biol. Chem. 270, 20887-20890.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20887-20890
    • Davis-Salinas, J.1    Van Nostrand, W.E.2
  • 8
    • 0027529491 scopus 로고
    • Study of the synthesis and secretion of normal and artificial mutants of murine amyloid precursor protein (APP): Cleavage of APP occurs in a late compartment of the default secretion pathway
    • De Strooper, B., Umans, L., Van Leuven, F., & Van Den Berghe, H. (1993) Study of the synthesis and secretion of normal and artificial mutants of murine amyloid precursor protein (APP): Cleavage of APP occurs in a late compartment of the default secretion pathway. J. Cell Biol. 121, 295-304.
    • (1993) J. Cell Biol. , vol.121 , pp. 295-304
    • De Strooper, B.1    Umans, L.2    Van Leuven, F.3    Van Den Berghe, H.4
  • 9
    • 0034954544 scopus 로고    scopus 로고
    • Comparison of the aggregation properties, secondary structure and apoptotic effects of wild-type, Flemish and Dutch N-terminally truncated amyloid beta peptides
    • Demeester, N., Mertens, C., Caster, H., Goethals, M., Vandekerckhove, J., Rosseneu, M., & Labeur, C. (2001) Comparison of the aggregation properties, secondary structure and apoptotic effects of wild-type, Flemish and Dutch N-terminally truncated amyloid beta peptides. Eur. J. Neurosci. 13, 2015-2024.
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 2015-2024
    • Demeester, N.1    Mertens, C.2    Caster, H.3    Goethals, M.4    Vandekerckhove, J.5    Rosseneu, M.6    Labeur, C.7
  • 10
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • Grabowski, T. J., Cho, H. S., Vonsattel, J. P., Rebeck, G. W., & Greenberg, S. M. (2001) Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann. Neurol. 49, 697-705.
    • (2001) Ann. Neurol. , vol.49 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.3    Rebeck, G.W.4    Greenberg, S.M.5
  • 11
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor
    • Haass, C., Hung, A. Y., Selkoe, D. J., & Teplow, D. B. (1994) Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor. J. Biol. Chem. 269, 17741-17748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 12
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer disease
    • Hardy, J. (1997) Amyloid, the presenilins and Alzheimer disease. Trends Neurol. Sci. 20, 154-159.
    • (1997) Trends Neurol. Sci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 13
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & 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    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 15
    • 0033538334 scopus 로고    scopus 로고
    • No influence of presenilin1 I143T and G384A mutations on endogenous tau phosphorylation in human and mouse neuroblastoma cells
    • Julliams, A., Vanderhoeven, I., Kuhn, S., Van Broeckhoven, C., & De Jonghe, C. (1999) No influence of presenilin1 I143T and G384A mutations on endogenous tau phosphorylation in human and mouse neuroblastoma cells. Neurosci. Lett. 269, 83-86.
    • (1999) Neurosci. Lett. , vol.269 , pp. 83-86
    • Julliams, A.1    Vanderhoeven, I.2    Kuhn, S.3    Van Broeckhoven, C.4    De Jonghe, C.5
  • 21
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: Implications for initial events in amyloid plaque formation
    • Lemere, C. A., Blusztajn, J. K., Yamaguchi, H., Wisniewski, T., Saido, T. C., & Selkoe, D. J. (1996) Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: Implications for initial events in amyloid plaque formation. Neurobiol. Dis. 3, 16-32.
    • (1996) Neurobiol. Dis. , vol.3 , pp. 16-32
    • Lemere, C.A.1    Blusztajn, J.K.2    Yamaguchi, H.3    Wisniewski, T.4    Saido, T.C.5    Selkoe, D.J.6
  • 24
    • 0029927290 scopus 로고    scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D). II. A review of histopathological aspects
    • Maat-Schieman, M. L., van Duinen, S. G., Bornebroek, M., Haan, J., & Roos, R. A. (1996) Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D). II. A review of histopathological aspects. Brain Pathol. 6, 115-120.
    • (1996) Brain Pathol. , vol.6 , pp. 115-120
    • Maat-Schieman, M.L.1    Van Duinen, S.G.2    Bornebroek, M.3    Haan, J.4    Roos, R.A.5
  • 26
    • 0034737720 scopus 로고    scopus 로고
    • Fibrillar amyloid beta-protein mediates the pathologic accumulation of its secreted precursor in human cerebrovascular smooth muscle cells
    • Melchor, J. P., & Van Nostrand, W. E. (2000) Fibrillar amyloid beta-protein mediates the pathologic accumulation of its secreted precursor in human cerebrovascular smooth muscle cells. J. Biol. Chem. 275, 9782-9791.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9782-9791
    • Melchor, J.P.1    Van Nostrand, W.E.2
  • 27
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimer's A{beta} peptide induce conformational changes and diverse apoptotic effects in human cerebral endothelial cells
    • Miravalle, L., Tokuda, T., Chiarle, R., Giaccone, G., Bugiani, O., Tagliavini, F., Frangione, B., & Ghiso, J. (2000) Substitutions at codon 22 of Alzheimer's A{beta} peptide induce conformational changes and diverse apoptotic effects in human cerebral endothelial cells. J. Biol. Chem. 275, 27110-27116.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27110-27116
    • Miravalle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5    Tagliavini, F.6    Frangione, B.7    Ghiso, J.8
  • 28
    • 0021176611 scopus 로고
    • Retinoic acid-induced differentiation of cultured human neuroblastoma cells: A comparison with phorbol-ester-induced differentiation
    • Pahlman, S., Ruusala, A. I., Abrahamsson, L., Mattsson, M. E., & Esscher, T. (1984) Retinoic acid-induced differentiation of cultured human neuroblastoma cells: A comparison with phorbol-ester-induced differentiation. Cell Differ. 14, 135-144.
    • (1984) Cell Differ. , vol.14 , pp. 135-144
    • Pahlman, S.1    Ruusala, A.I.2    Abrahamsson, L.3    Mattsson, M.E.4    Esscher, T.5
  • 29
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro
    • Pike, C. J., Overman, M. J., & Cotman, C. W. (1995) Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro. J. Biol. Chem. 270, 23895-23898.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 30
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • Pike, C. J., Walencewicz, A. J., Glabe, C. G., & 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
  • 32
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain
    • Saido, T. C., Yamao-Harigaya, W., Iwatsubo, T., & Kawashima, S. (1996) Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain. Neurosci. Lett. 215, 173-176.
    • (1996) Neurosci. Lett. , vol.215 , pp. 173-176
    • Saido, T.C.1    Yamao-Harigaya, W.2    Iwatsubo, T.3    Kawashima, S.4
  • 33
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. (1998) The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends. Cell Biol. 8, 447-453.
    • (1998) Trends. Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 35
    • 0035800847 scopus 로고    scopus 로고
    • The amyloidogenic pathway of amyloid precursor protein (APP) is independent of its cleavage by caspases
    • Soriano, S., Lu, D. C., Chandra, S., Pietrzik, C. U., & Koo, E. H. (2001) The amyloidogenic pathway of amyloid precursor protein (APP) is independent of its cleavage by caspases. J. Biol. Chem. 276, 29045-29050.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29045-29050
    • Soriano, S.1    Lu, D.C.2    Chandra, S.3    Pietrzik, C.U.4    Koo, E.H.5
  • 37
    • 0035339688 scopus 로고    scopus 로고
    • In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692 → Gly) Alzheimer's disease
    • Walsh, D. M., Hartley, D. M., Condron, M. M., Selkoe, D. J., & Teplow, D. B. (2001) In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692 β Gly) Alzheimer's disease. Biochem. J. 355, 869-877.
    • (2001) Biochem. J. , vol.355 , pp. 869-877
    • Walsh, D.M.1    Hartley, D.M.2    Condron, M.M.3    Selkoe, D.J.4    Teplow, D.B.5
  • 38
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 39
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & 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
  • 40
    • 0033951944 scopus 로고    scopus 로고
    • Toxicity of Dutch (E22Q) and Flemish (A21G) mutant amyloid beta proteins to human cerebral microvessel and aortic smooth muscle cells
    • Wang, Z., Natte, R., Berliner, J. A., van Duinen, S. G., Vinters, H. V., & Rosenblum, W. I. (2000) Toxicity of Dutch (E22Q) and Flemish (A21G) mutant amyloid beta proteins to human cerebral microvessel and aortic smooth muscle cells. Stroke 31, 534-538.
    • (2000) Stroke , vol.31 , pp. 534-538
    • Wang, Z.1    Natte, R.2    Berliner, J.A.3    Van Duinen, S.G.4    Vinters, H.V.5    Rosenblum, W.I.6
  • 41
    • 0025720097 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation
    • Wisniewski, T., Ghiso, J., & 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. 180, 1528.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1528
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.