메뉴 건너뛰기




Volumn 152, Issue 4, 1998, Pages 983-992

Astrocytes containing amyloid β-protein (Aβ)-positive granules are associated with aβ40-positive diffuse plaques in the aged human brain

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; ANTIBODY;

EID: 0031922062     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (148)

References (50)
  • 1
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y: Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron 1994, 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
  • 2
    • 0028919919 scopus 로고
    • Amyloid β-protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down's syndrome
    • Iwatsubo T, Mann DMA, Odaka A, Suzuki N, Ihara Y: Amyloid β-protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down's syndrome. Ann Neurol 1995, 37:294-299
    • (1995) Ann Neurol , vol.37 , pp. 294-299
    • Iwatsubo, T.1    Mann, D.M.A.2    Odaka, A.3    Suzuki, N.4    Ihara, Y.5
  • 3
    • 0028979854 scopus 로고
    • Amyloid β-proteins (Aβ)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: Amyloid β-proteins (Aβ)1-40, and 1-42(43) in the soluble fraction of extra-and intracranial blood vessels. Ann Neurol 1995, 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
  • 4
    • 0027261525 scopus 로고
    • Migration of perivascular cells into the neuropil and their involvement in β-amyloid plaque formation
    • Berl
    • Wisniewski HM, Weigel J: Migration of perivascular cells into the neuropil and their involvement in β-amyloid plaque formation. Acta Neuropathol (Berl) 1993, 85:586-595
    • (1993) Acta Neuropathol , vol.85 , pp. 586-595
    • Wisniewski, H.M.1    Weigel, J.2
  • 6
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor
    • Paresce DM, Ghosh RN, Maxfield FR: Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor. Neuron 1996, 17:553-565
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 8
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein
    • Knauer MF, Soreghan B, Burdick D, Kosmoski J, Glabe CG: Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein. Proc Natl Acad Sci USA 1992, 89:7437-7441
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 9
    • 0028172208 scopus 로고
    • The Alzheimer Aβ peptide develops protease resistance in association with its polymerization into fibrils
    • Nordstedt C, Naslund J, Tjernberg LO, Karlstrom AR, Thyberg J, Terenius L: The Alzheimer Aβ peptide develops protease resistance in association with its polymerization into fibrils. J Biol Chem 1994, 269:30773-30776
    • (1994) J Biol Chem , vol.269 , pp. 30773-30776
    • Nordstedt, C.1    Naslund, J.2    Tjernberg, L.O.3    Karlstrom, A.R.4    Thyberg, J.5    Terenius, L.6
  • 11
    • 0029998346 scopus 로고    scopus 로고
    • The serpin-enzyme complex receptor recognizes soluble, nontoxic amyloid-β peptide but not aggregated, cytotoxic amyloid-β peptide
    • Boland K, Behrens M, Choi D, Manias K, Perlmutter DH: The serpin-enzyme complex receptor recognizes soluble, nontoxic amyloid-β peptide but not aggregated, cytotoxic amyloid-β peptide. J Biol Chem 1996, 271:18032-18044
    • (1996) J Biol Chem , vol.271 , pp. 18032-18044
    • Boland, K.1    Behrens, M.2    Choi, D.3    Manias, K.4    Perlmutter, D.H.5
  • 13
    • 0013642132 scopus 로고    scopus 로고
    • Degradation of amyloid β-protein by a serine protease-α2-macroglobulin complex
    • Qiu WQ, Borth W, Ye Z, Haass C, Teplow DB, Selkoe DJ: Degradation of amyloid β-protein by a serine protease-α2-macroglobulin complex. J Biol Chem 1996, 271:8443-8451
    • (1996) J Biol Chem , vol.271 , pp. 8443-8451
    • Qiu, W.Q.1    Borth, W.2    Ye, Z.3    Haass, C.4    Teplow, D.B.5    Selkoe, D.J.6
  • 14
    • 0028985061 scopus 로고
    • β-Amyloid peptide produced in vitro is degraded by proteinases released by cultured cells
    • Naidu A, Quon D, Cordell B: β-Amyloid peptide produced in vitro is degraded by proteinases released by cultured cells. J Biol Chem 1995, 270:1369-1374
    • (1995) J Biol Chem , vol.270 , pp. 1369-1374
    • Naidu, A.1    Quon, D.2    Cordell, B.3
  • 15
    • 0002541877 scopus 로고
    • The consortium to establish a registry for Alzheimer's disease (CERAD). II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKee D, Sumi SM, Crain BJ, Brownlee LM, Vogel FS, Hughes JP, van Belle G, Berg L, participating CERAD neuropathologists: the consortium to establish a registry for Alzheimer's disease (CERAD). II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991, 42:1681-1689
    • (1991) Neurology , vol.42 , pp. 1681-1689
    • Mirra, S.S.1    Heyman, A.2    McKee, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    Van Belle, G.9    Berg, L.10
  • 16
    • 0023833603 scopus 로고
    • The NICDS-ADRDA Work Group criteria for the clinical diagnosis of probable Alzheimer's disease: Clinicopathological study of 57 cases
    • Tierney MC, Fisher H, Lewis AJ: The NICDS-ADRDA Work Group criteria for the clinical diagnosis of probable Alzheimer's disease: clinicopathological study of 57 cases. Neurology 1988, 38:356-364
    • (1988) Neurology , vol.38 , pp. 356-364
    • Tierney, M.C.1    Fisher, H.2    Lewis, A.J.3
  • 17
    • 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: Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells Biochemistry 1995, 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
  • 18
    • 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. Nature Med 1995, 1:1062-1066
    • (1995) Nature Med , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 20
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain
    • Saido TC, Yamao-Harigaya W, Iwatsubo T, Kawashima S: Amino-and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain. Neurosci Lett 1996, 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
  • 21
    • 0029849644 scopus 로고    scopus 로고
    • Full-length amyloid-β (1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques
    • Iwatsubo T, Saido TC, Mann DMA, Lee VM-Y, Trojanowski JQ: Full-length amyloid-β (1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques. Am J Pathol 1996, 149:1823-1830
    • (1996) Am J Pathol , vol.149 , pp. 1823-1830
    • Iwatsubo, T.1    Saido, T.C.2    Mann, D.M.A.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5
  • 22
    • 0023131373 scopus 로고
    • Alzheimer's neurofibrillary tangles are penetrated by astroglial processes and appear eosinophilic in their final stages
    • Yamaguchi H, Morimatsu M, Hirai S, Takahashi K: Alzheimer's neurofibrillary tangles are penetrated by astroglial processes and appear eosinophilic in their final stages. Acta Neuropathol 1987, 72:214-217
    • (1987) Acta Neuropathol , vol.72 , pp. 214-217
    • Yamaguchi, H.1    Morimatsu, M.2    Hirai, S.3    Takahashi, K.4
  • 23
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida Y, Takio K, Titani K, Ihara Y, Tomonaga M: The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron 1991, 7:337-347
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 24
    • 0029096205 scopus 로고
    • Immunoreactivity of growth inhibitory factor in normal rat brain and after stab wounds: An immunocytochemical study using confocal laser scan microscope
    • Hozumi I, Inuzuka T, Hiraiwa M, Uchida Y, Anezaki T, Ishiguro H, Kobayashi H, Uda Y, Miyatake T, Tsuji S: Immunoreactivity of growth inhibitory factor in normal rat brain and after stab wounds: an immunocytochemical study using confocal laser scan microscope. Brain Res 1995, 688:143-148
    • (1995) Brain Res , vol.688 , pp. 143-148
    • Hozumi, I.1    Inuzuka, T.2    Hiraiwa, M.3    Uchida, Y.4    Anezaki, T.5    Ishiguro, H.6    Kobayashi, H.7    Uda, Y.8    Miyatake, T.9    Tsuji, S.10
  • 26
    • 0022907623 scopus 로고
    • A specific histochemical marker (lectin Ricinus communis agglutinin-1) for normal human microglia and application to routine histopathology
    • Berl
    • Mannoji H, Yeger H, Becker LE: A specific histochemical marker (lectin Ricinus communis agglutinin-1) for normal human microglia and application to routine histopathology. Acta Neuropathol (Berl) 1986, 71:341-343
    • (1986) Acta Neuropathol , vol.71 , pp. 341-343
    • Mannoji, H.1    Yeger, H.2    Becker, L.E.3
  • 27
    • 0025786986 scopus 로고
    • Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and Alzheimer's disease brain tissues
    • Shin RW, Iwaki T, Kitamoto T, Tateishi J: Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and Alzheimer's disease brain tissues. Lab Invest 1991, 64:693-702
    • (1991) Lab Invest , vol.64 , pp. 693-702
    • Shin, R.W.1    Iwaki, T.2    Kitamoto, T.3    Tateishi, J.4
  • 31
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct β-amyloid peptide species, AβN3(pE), in senile plaques
    • Saido TC, Iwatsubo T, Mann DMA, Shimada H, Ihara Y, Kawashima S: Dominant and differential deposition of distinct β-amyloid peptide species, AβN3(pE), in senile plaques. Neuron 1995, 14:457-466
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.A.3    Shimada, H.4    Ihara, Y.5    Kawashima, S.6
  • 32
    • 0024391157 scopus 로고
    • Immunoreactivity of neuronal lipofuscin with monoclonal antibodies to the amyloid β-protein
    • Bancher C, Grundke-Iqbal I, Iqbal K, Kim KS, Wisniewski HM: Immunoreactivity of neuronal lipofuscin with monoclonal antibodies to the amyloid β-protein. Neurobiol Aging 1989, 10:125-132
    • (1989) Neurobiol Aging , vol.10 , pp. 125-132
    • Bancher, C.1    Grundke-Iqbal, I.2    Iqbal, K.3    Kim, K.S.4    Wisniewski, H.M.5
  • 34
    • 0027512262 scopus 로고
    • Monoclonal antibody to β peptide, recognizing amyloid deposits, neuronal cells and lipofuscin pigments in systemic organs
    • Takahashi H, Utsuyama M, Kurashima C, Mori H, Hirokawa K: Monoclonal antibody to β peptide, recognizing amyloid deposits, neuronal cells and lipofuscin pigments in systemic organs. Acta Neuropathol 1993, 85:159-166
    • (1993) Acta Neuropathol , vol.85 , pp. 159-166
    • Takahashi, H.1    Utsuyama, M.2    Kurashima, C.3    Mori, H.4    Hirokawa, K.5
  • 35
    • 0024349528 scopus 로고
    • Monoclonal antibodies to a synthetic peptide homologous with the first 28 amino acids of Alzheimer's disease β-protein recognize amyloid and diverse glial and neuronal cell types in the central nervous system
    • Stern RA, Otvos L, Trojanowski JQ, Lee VM-Y: Monoclonal antibodies to a synthetic peptide homologous with the first 28 amino acids of Alzheimer's disease β-protein recognize amyloid and diverse glial and neuronal cell types in the central nervous system. Am J Pathol 1989, 134:973-978
    • (1989) Am J Pathol , vol.134 , pp. 973-978
    • Stern, R.A.1    Otvos, L.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 37
    • 0025274691 scopus 로고
    • Antibodies to the β-amyloid peptide cross-react with conformational epitopes in human fibrinogen subunits from peripheral blood
    • Stern RA, Trojanowski JQ, Lee VM-Y: Antibodies to the β-amyloid peptide cross-react with conformational epitopes in human fibrinogen subunits from peripheral blood. FEBS Lett 1990, 264:43-47
    • (1990) FEBS Lett , vol.264 , pp. 43-47
    • Stern, R.A.1    Trojanowski, J.Q.2    Lee, V.M.-Y.3
  • 38
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ: Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 1992, 357:500-503
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 39
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde TE, Estus S, Younkin LH, Selkoe DJ, Younkin SG: Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 1992, 255:728-730
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 40
    • 0028277270 scopus 로고
    • Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-β by cathepsin D
    • Ladror US, Snyder SW, Wang GT, Holzman TF, Krafft GA: Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-β by cathepsin D. J Biol Chem 1994, 269:18422-18428
    • (1994) J Biol Chem , vol.269 , pp. 18422-18428
    • Ladror, U.S.1    Snyder, S.W.2    Wang, G.T.3    Holzman, T.F.4    Krafft, G.A.5
  • 41
    • 0028971529 scopus 로고
    • Candidate γ-secretases in the generation of the carboxyl terminus of the Alzheimer's disease β A4 amyloid: Possible involvement of cathepsin D
    • Evin G, Cappai R, Li QX, Culvenor JG, Small DH, Beyreuther K, Masters CL: Candidate γ-secretases in the generation of the carboxyl terminus of the Alzheimer's disease β A4 amyloid: possible involvement of cathepsin D. Biochemistry 1995, 34:14185-14192
    • (1995) Biochemistry , vol.34 , pp. 14185-14192
    • Evin, G.1    Cappai, R.2    Li, Q.X.3    Culvenor, J.G.4    Small, D.H.5    Beyreuther, K.6    Masters, C.L.7
  • 42
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • Cataldo AM, Nixon RA: Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc Natl Acad Sci USA 1990, 87:3861-3865
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 43
    • 0026354082 scopus 로고
    • Rapid appearance of β-amyloid precursor immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury
    • Otsuka N, Tomonaga M, Ikeda K: Rapid appearance of β-amyloid precursor immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury. Brain Res 1991, 568:335-338
    • (1991) Brain Res , vol.568 , pp. 335-338
    • Otsuka, N.1    Tomonaga, M.2    Ikeda, K.3
  • 44
    • 0029970783 scopus 로고    scopus 로고
    • Amyloidogenic processing of human amyloid precursor protein in hippocampal neurons devoid of cathepsin D
    • Saftig P, Peters C, von Figura K, Craessaerts K, Van Leuven F, De Strooper B: Amyloidogenic processing of human amyloid precursor protein in hippocampal neurons devoid of cathepsin D. J Biol Chem 1996, 271:27241-27244
    • (1996) J Biol Chem , vol.271 , pp. 27241-27244
    • Saftig, P.1    Peters, C.2    Von Figura, K.3    Craessaerts, K.4    Van Leuven, F.5    De Strooper, B.6
  • 45
    • 0027475753 scopus 로고
    • Phagocytosis of myelin by astrocytes in explants of adult rabbit cerebral white matter maintained on Gelfoam matrix
    • Vinores SA, Herman MM: Phagocytosis of myelin by astrocytes in explants of adult rabbit cerebral white matter maintained on Gelfoam matrix. J Neuroimmunol 1993, 43:169-176
    • (1993) J Neuroimmunol , vol.43 , pp. 169-176
    • Vinores, S.A.1    Herman, M.M.2
  • 46
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • Dickson DW: The pathogenesis of senile plaques. J Neuropathol Exp Neurol 1997, 56:321-339
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 321-339
    • Dickson, D.W.1
  • 47
    • 0030598393 scopus 로고    scopus 로고
    • The amino-terminally truncated forms of amyloid β-protein in brain macrophages in the ischemic lesions of Alzheimer's disease patients
    • Akiyama H, Kondo H, Mori H, Kametani F, Nishimura T, Ikeda K, Kato M, McGeer PL: The amino-terminally truncated forms of amyloid β-protein in brain macrophages in the ischemic lesions of Alzheimer's disease patients. Neurosci Lett 1996, 219:115-118
    • (1996) Neurosci Lett , vol.219 , pp. 115-118
    • Akiyama, H.1    Kondo, H.2    Mori, H.3    Kametani, F.4    Nishimura, T.5    Ikeda, K.6    Kato, M.7    McGeer, P.L.8
  • 48
    • 0030003487 scopus 로고    scopus 로고
    • Granules in glial cells of patients with Alzheimer's disease are immunoreactive for C-terminal sequence of β-amyloid protein
    • Akiyama H, Schwab C, Kondo H, Mori H, Kametani F, Ikeda K, McGeer PL: Granules in glial cells of patients with Alzheimer's disease are immunoreactive for C-terminal sequence of β-amyloid protein. Neurosci Lett 1996, 206:169-172
    • (1996) Neurosci Lett , vol.206 , pp. 169-172
    • Akiyama, H.1    Schwab, C.2    Kondo, H.3    Mori, H.4    Kametani, F.5    Ikeda, K.6    McGeer, P.L.7
  • 49
    • 0028113719 scopus 로고
    • Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex
    • Martin LJ, Pardo CA, Cork LC, Price DC: Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex. Am J Pathol 1994, 145:1358-1381
    • (1994) Am J Pathol , vol.145 , pp. 1358-1381
    • Martin, L.J.1    Pardo, C.A.2    Cork, L.C.3    Price, D.C.4
  • 50
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro
    • Pike CJ, Overman MJ, Cotman CW: Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro. J Biol Chem 1995, 270:23895-23898
    • (1995) J Biol Chem , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.