메뉴 건너뛰기




Volumn 105, Issue 3, 2003, Pages 252-258

Aβ species, including IsoAsp23 Aβ, in Iowa-type familial cerebral amyloid angiopathy

Author keywords

Alzheimer's disease; Isomerization; Mutation; Vascular dementia

Indexed keywords

AMYLOID BETA PROTEIN; ASPARAGINE; ASPARTIC ACID; BRAIN EXTRACT; MONOCLONAL ANTIBODY; ANTIBODY; DIAGNOSTIC AGENT; ISOASPARTIC ACID;

EID: 0037775901     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00401-002-0639-0     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 0031942889 scopus 로고    scopus 로고
    • Progression of cerebral amyloid angiopathy. Accumulation of Aβ40 in already affected vessels
    • Alonzo NC, Hyman BT, Rebeck GW, Greenberg SM (1998) Progression of cerebral amyloid angiopathy. Accumulation of Aβ40 in already affected vessels. J Neuropathol Exp Neurol 57:353-359
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 353-359
    • Alonzo, N.C.1    Hyman, B.T.2    Rebeck, G.W.3    Greenberg, S.M.4
  • 2
    • 0028984919 scopus 로고
    • Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells
    • Asami-Odaka A, Ishibashi Y, Kikuchi T, Kitada C, Suzuki N (1995) Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells. Biochemistry 34:10272-10278
    • (1995) Biochemistry , vol.34 , pp. 10272-10278
    • Asami-Odaka, A.1    Ishibashi, Y.2    Kikuchi, T.3    Kitada, C.4    Suzuki, N.5
  • 6
    • 0025838381 scopus 로고
    • pH-dependent structural transitions of Alzheimer amyloid peptides
    • 6 Fraser PE, Nguyen JT, Surewicz WK, Kirschner DA (1991) pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys J 60:1190-1201
    • (1991) Biophys. J. , vol.60 , pp. 1190-1201
    • Fraser, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.A.4
  • 9
    • 0033526118 scopus 로고    scopus 로고
    • Synthesis, aggregation, and neurotoxicity of the Alzheimer's Abeta 1-42 amyloid peptide and its isoaspartyl isomers
    • Fukuda H, Shimizu T, Nakajima M, Mori H, Shirasawa T (1999) Synthesis, aggregation, and neurotoxicity of the Alzheimer's Abeta 1-42 amyloid peptide and its isoaspartyl isomers. Bioorg Med Chem Lett 9:953-956
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 953-956
    • Fukuda, H.1    Shimizu, T.2    Nakajima, M.3    Mori, H.4    Shirasawa, T.5
  • 10
    • 0033615250 scopus 로고    scopus 로고
    • Primary cultures of neuronal and non-neuronal rat brain cells secrete similar proportions of amyloid β peptides ending at Aβ40 and Aβ42
    • Fukumoto H, Tomita T, Matsunaga H, Ishibashi Y, Saido TC, Iwatsubo T (1999) Primary cultures of neuronal and non-neuronal rat brain cells secrete similar proportions of amyloid β peptides ending at Aβ40 and Aβ42. NeuroReport 10:2965-2969
    • (1999) NeuroReport , vol.10 , pp. 2965-2969
    • Fukumoto, H.1    Tomita, T.2    Matsunaga, H.3    Ishibashi, Y.4    Saido, T.C.5    Iwatsubo, T.6
  • 11
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 12
  • 13
    • 0028915895 scopus 로고
    • Amyloid beta protein (Abeta) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Abeta 40 or Abeta 42(43)
    • Gravina SA, Ho L, Eckman CB, Long KE, Otvos LJ, Younkin LH, Suzuki N, Younkin SG (1995) Amyloid beta protein (Abeta) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Abeta 40 or Abeta 42(43). J Biol Chem 270:7013-7016
    • (1995) J. Biol. Chem. , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3    Long, K.E.4    Otvos, L.J.5    Younkin, L.H.6    Suzuki, N.7    Younkin, S.G.8
  • 14
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor
    • Haass C, Hung AY, Selkoe DJ, Teplow DB (1994) Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-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
  • 15
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J, Allsop D (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci 12:383-388
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 19
    • 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
    • Jarrett JT, Berger EP, Lansbury PTJ (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.J.3
  • 21
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
    • Kirkitadze MD, Condron MM, Teplow DB (2001) Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis. J Mol Biol 312:1103-1119
    • (2001) J. Mol. Biol. , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 23
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid β-peptides and APO E in Down syndrome: Implications for initial events in amyloid plaque formation
    • Lemere CA, Blusztajn JK, Yamaguchi H, Wisniewski T, Saido TC, Selkoe DJ (1996) Sequence of deposition of heterogeneous amyloid β-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
  • 25
    • 0034975365 scopus 로고    scopus 로고
    • Amyloid angiopathy and variability in amyloid β deposition is determined by mutation position in presenilin-1-linked Alzheimer disease
    • Mann DMA, Pickering-Brown SM, Takeuchi A, Iwatsubo T (2001) Amyloid angiopathy and variability in amyloid β deposition is determined by mutation position in presenilin-1-linked Alzheimer disease. Am J Pathol 158:2165-2175
    • (2001) Am. J. Pathol. , vol.158 , pp. 2165-2175
    • Mann, D.M.A.1    Pickering-Brown, S.M.2    Takeuchi, A.3    Iwatsubo, T.4
  • 27
    • 0034049538 scopus 로고    scopus 로고
    • Charge alterations of E22 enhance the pathogenic properties of the amyloid β-protein
    • Melchor JP, McVoy L, Van Nostrand WE (2000) Charge alterations of E22 enhance the pathogenic properties of the amyloid β-protein. J Neurochem 74:2209-2212
    • (2000) J. Neurochem. , vol.74 , pp. 2209-2212
    • Melchor, J.P.1    McVoy, L.2    Van Nostrand, W.E.3
  • 29
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimer's Abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
    • Miravelle L, Tokuda T, Chiarle R, Giaccone G, Bugiani O, Tagliavini F, Frangione B, Ghiso J (2000) Substitutions at codon 22 of Alzheimer's Abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J Biol Chem 275:27110-27116
    • (2000) J. Biol. Chem. , vol.275 , pp. 27110-27116
    • Miravelle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5    Tagliavini, F.6    Frangione, B.7    Ghiso, J.8
  • 30
    • 0036227489 scopus 로고    scopus 로고
    • Substitution at codon 22 reduces clearance of Alzheimer's amyloid-β peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood
    • Monro OR, Mackic JB, Yamada S, Segal MB, Ghiso J, Maurer C, Calero M, Frangione B, Zlokovic BV (2002) Substitution at codon 22 reduces clearance of Alzheimer's amyloid-β peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood. Neurobiol Aging 23:405-412
    • (2002) Neurobiol. Aging , vol.23 , pp. 405-412
    • Monro, O.R.1    Mackic, J.B.2    Yamada, S.3    Segal, M.B.4    Ghiso, J.5    Maurer, C.6    Calero, M.7    Frangione, B.8    Zlokovic, B.V.9
  • 34
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe DJ (1994) Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu Rev Cell Biol 10:373-403
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 37
    • 0037010294 scopus 로고    scopus 로고
    • Isoaspartate formation at position 23 of amyloid beta peptide enhanced fibril formation and deposited onto senile plaques and vascular amyloids in Alzheimer's disease
    • (in press)
    • Shimizu T, Fukuda H, Murayama S, Izumiyama N, Shirasawa T (2002) Isoaspartate formation at position 23 of amyloid beta peptide enhanced fibril formation and deposited onto senile plaques and vascular amyloids in Alzheimer's disease. J Neurosci Res (in press)
    • (2002) J. Neurosci. Res.
    • Shimizu, T.1    Fukuda, H.2    Murayama, S.3    Izumiyama, N.4    Shirasawa, T.5
  • 38
    • 0028979854 scopus 로고
    • Amyloid β-proteins 1-40 and 1-42(43) in the soluble fraction of extra- and intracranial blood vessels
    • Shinkai Y, Yoshimura M, Ito Y, Odaka A, Suzuki N, Yanagisawa K, Ihara Y (1995) Amyloid β-proteins 1-40 and 1-42(43) in the soluble fraction of extra- and intracranial blood vessels. Ann Neurol 38:421-428
    • (1995) Ann. Neurol. , vol.38 , pp. 421-428
    • Shinkai, Y.1    Yoshimura, M.2    Ito, Y.3    Odaka, A.4    Suzuki, N.5    Yanagisawa, K.6    Ihara, Y.7
  • 40
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanisms of β-amyloid production and secretion
    • Sinha S, Lieberburg I (1999) Cellular mechanisms of β-amyloid production and secretion. Proc Natl Acad Sci USA 96: 11049-11053
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 45
    • 0028177534 scopus 로고
    • Racemization and Asp23 residue affects the aggregation properties of Alzheimer amyloid β protein analogues
    • Tomiyama T, Asano S, Furiya Y, Shirasawa T, Endo N, Mori H (1994) Racemization and Asp23 residue affects the aggregation properties of Alzheimer amyloid β protein analogues. J Biol Chem 269:10205-10208
    • (1994) J. Biol. Chem. , vol.269 , pp. 10205-10208
    • Tomiyama, T.1    Asano, S.2    Furiya, Y.3    Shirasawa, T.4    Endo, N.5    Mori, H.6
  • 46
    • 0030833577 scopus 로고    scopus 로고
    • Cerebrovascular smooth muscle cells internalize Alzheimer amyloid beta protein via a lipoprotein pathway: Implications for cerebral amyloid angiopathy
    • Urmoneit B, Prikulis I, Wihl G, D'Urso D, Frank R, Heeren J, Beisiegel U, Prior R (1997) Cerebrovascular smooth muscle cells internalize Alzheimer amyloid beta protein via a lipoprotein pathway: implications for cerebral amyloid angiopathy. Lab Invest 77:157-166
    • (1997) Lab. Invest. , vol.77 , pp. 157-166
    • Urmoneit, B.1    Prikulis, I.2    Wihl, G.3    D'Urso, D.4    Frank, R.5    Heeren, J.6    Beisiegel, U.7    Prior, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.