메뉴 건너뛰기




Volumn 126, Issue 12, 2005, Pages 1292-1299

Amyloid peptide attenuates the proteasome activity in neuronal cells

Author keywords

Amyloid peptide; Chymotrypsin like activity; Proteasome; Tg2576

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; PROTEASOME; UBIQUITIN;

EID: 27644522515     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mad.2005.07.006     Document Type: Article
Times cited : (141)

References (43)
  • 1
    • 0027444952 scopus 로고
    • Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis
    • V. Askanas, R.B. Alvarez, and W.K. Engel Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis Ann. Neurol. 34 1993 551 560
    • (1993) Ann. Neurol. , vol.34 , pp. 551-560
    • Askanas, V.1    Alvarez, R.B.2    Engel, W.K.3
  • 2
    • 0032551528 scopus 로고    scopus 로고
    • Amyloid beta protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein
    • B.A. Bahr, K.B. Hoffman, A.J. Yang, U.S. Hess, C.G. Glabe, and G. Lynch Amyloid beta protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein J. Comp. Neurol. 397 1998 139 147
    • (1998) J. Comp. Neurol. , vol.397 , pp. 139-147
    • Bahr, B.A.1    Hoffman, K.B.2    Yang, A.J.3    Hess, U.S.4    Glabe, C.G.5    Lynch, G.6
  • 3
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • N.F. Bence, R.M. Sampat, and R.R. Kopito Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 4
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • X. Bi, C.M. Gall, J. Zhou, and G. Lynch Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists Neuroscience 112 2002 827 840
    • (2002) Neuroscience , vol.112 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3    Lynch, G.4
  • 6
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • A. Ciechanover, A. Orian, and A.L. Schwartz Ubiquitin-mediated proteolysis: biological regulation via destruction Bioessays 22 2000 442 451
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 7
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • O. Coux, K. Tanaka, and A.L. Goldberg Structure and functions of the 20S and 26S proteasomes Annu. Rev. Biochem. 65 1996 801 847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 8
    • 0033845065 scopus 로고    scopus 로고
    • Prevention of beta-amyloid neurotoxicity by blockade of the ubiquitin-proteasome proteolytic pathway
    • A. Favit, M. Grimaldi, and D.L. Alkon Prevention of beta-amyloid neurotoxicity by blockade of the ubiquitin-proteasome proteolytic pathway J. Neurochem. 75 2000 1258 1263
    • (2000) J. Neurochem. , vol.75 , pp. 1258-1263
    • Favit, A.1    Grimaldi, M.2    Alkon, D.L.3
  • 9
    • 25144472262 scopus 로고    scopus 로고
    • Phospho-beta-catenin accumulation in Alzheimer's disease and in aggresomes attributable to proteasome dysfunction
    • M. Ghanevati, and C.A. Miller Phospho-beta-catenin accumulation in Alzheimer's disease and in aggresomes attributable to proteasome dysfunction J. Mol. Neurosci. 25 2005 79 94
    • (2005) J. Mol. Neurosci. , vol.25 , pp. 79-94
    • Ghanevati, M.1    Miller, C.A.2
  • 10
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • T. Gilon, O. Chomsky, and R.G. Kulka Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae EMBO J. 17 1998 2759 2766
    • (1998) EMBO J. , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 13
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • M. Groettrup, A. Soza, U. Kuckelkorn, and P.M. Kloetzel Peptide antigen production by the proteasome: complexity provides efficiency Immunol. Today 17 1996 429 435
    • (1996) Immunol. Today , vol.17 , pp. 429-435
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.M.4
  • 15
    • 0027333557 scopus 로고
    • Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide
    • C. Haass, and D.J. Selkoe Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide Cell 75 1993 1039 1042
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 16
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • W. Heinemeyer, J.A. Kleinschmidt, J. Saidowskym, C. Escherm, and D.H. Wolf Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival EMBO J. 10 1991 555 562
    • (1991) EMBO J. , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowskym, J.3    Escherm, C.4    Wolf, D.H.5
  • 18
    • 0030607177 scopus 로고    scopus 로고
    • Rapid cellular uptake of Alzheimer amyloid betaA4 peptide by cultured human neuroblastoma cells
    • N. Ida, C.L. Masters, and K. Beyreuther Rapid cellular uptake of Alzheimer amyloid betaA4 peptide by cultured human neuroblastoma cells FEBS Lett. 394 1996 174 178
    • (1996) FEBS Lett. , vol.394 , pp. 174-178
    • Ida, N.1    Masters, C.L.2    Beyreuther, K.3
  • 19
    • 0033167947 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications in cell-based assays for drug discovery
    • S.R. Kain Green fluorescent protein (GFP): applications in cell-based assays for drug discovery Drug Discov. Today 4 1999 304 312
    • (1999) Drug Discov. Today , vol.4 , pp. 304-312
    • Kain, S.R.1
  • 20
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • S. Keck, R. Nitsch, T. Grune, and O. Ullrich Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease J. Neurochem. 85 2003 115 122
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 21
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • J.N. Keller, K.B. Hanni, and W.R. Markesbery Impaired proteasome function in Alzheimer's disease J. Neurochem. 75 2000 436 439
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 22
    • 0035853576 scopus 로고    scopus 로고
    • Neuroprotective effects of estrogen against beta-amyloid toxicity are mediated by estrogen receptors in cultured neuronal cells
    • H. Kim, O.Y. Bang, M.W. Jung, S.D. Ha, H.S. Hong, K. Huh, S.U. Kim, and I. Mook-Jung Neuroprotective effects of estrogen against beta-amyloid toxicity are mediated by estrogen receptors in cultured neuronal cells Neurosci. Lett. 302 2001 58 62
    • (2001) Neurosci. Lett. , vol.302 , pp. 58-62
    • Kim, H.1    Bang, O.Y.2    Jung, M.W.3    Ha, S.D.4    Hong, H.S.5    Huh, K.6    Kim, S.U.7    Mook-Jung, I.8
  • 23
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes: Implications for understanding the degradative mechanism and antigen presentation
    • A.F. Kisselev, T.N. Akopian, K.M. Woo, and A.L. Goldberg The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes: implications for understanding the degradative mechanism and antigen presentation J. Biol. Chem. 274 1999 3363 3371
    • (1999) J. Biol. Chem. , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 24
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein
    • M.F. Knauer, B. Soreghan, D. Burdick, J. Kosmoski, and C.G. Glabe Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein Proc. Natl. Acad. Sci. U.S.A. 89 1992 7437 7441
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 25
    • 0037383052 scopus 로고    scopus 로고
    • Relationship between beta-amyloid degradation and the 26S proteasome in neuroal cells
    • M. Lopez Salon, L. Pasquini, M. Besio Moreno, J.M. Pasquini, and E. Soto Relationship between beta-amyloid degradation and the 26S proteasome in neuroal cells Exp. Neurol. 180 2003 131 143
    • (2003) Exp. Neurol. , vol.180 , pp. 131-143
    • Lopez Salon, M.1    Pasquini, L.2    Besio Moreno, M.3    Pasquini, J.M.4    Soto, E.5
  • 26
    • 0024992208 scopus 로고
    • Ubiquitin, cell stress and diseases of the nervous system
    • J. Lowe, and R.J. Mayer Ubiquitin, cell stress and diseases of the nervous system Neuropathol. Appl. Neurobiol. 16 1990 281 291
    • (1990) Neuropathol. Appl. Neurobiol. , vol.16 , pp. 281-291
    • Lowe, J.1    Mayer, R.J.2
  • 27
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • H. Mori, J. Kondo, and Y. Ihara Ubiquitin is a component of paired helical filaments in Alzheimer's disease Science 235 1987 1641 1644
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 28
    • 0028303123 scopus 로고
    • Development of a monoclonal antibody specific for the COOH-terminal of beta-amyloid 1-42 and its immunohistochemical reactivity in Alzheimer's disease and related disorders
    • G.M. Murphy Jr., L.S. Forno, L. Higgins, J.M. Scardina, L.F. Eng, and B. Cordell Development of a monoclonal antibody specific for the COOH-terminal of beta-amyloid 1-42 and its immunohistochemical reactivity in Alzheimer's disease and related disorders Am. J. Pathol. 144 1994 1082 1088
    • (1994) Am. J. Pathol. , vol.144 , pp. 1082-1088
    • Murphy Jr., G.M.1    Forno, L.S.2    Higgins, L.3    Scardina, J.M.4    Eng, L.F.5    Cordell, B.6
  • 29
    • 0029051233 scopus 로고
    • Cyclin ubiquitination: The destructive end of mitosis
    • A. Murry Cyclin ubiquitination: the destructive end of mitosis Cell 81 1995 149 152
    • (1995) Cell , vol.81 , pp. 149-152
    • Murry, A.1
  • 30
    • 0037066072 scopus 로고    scopus 로고
    • Intracellular accumulation of beta-amyloid (1-42) in neurons is facilitated by the alpha 7 nicotinic acetylcholine receptor in Alzheimer's disease
    • R.G. Nagele, M.R. D'Andrea, W.J. Anderson, and H.Y. Wang Intracellular accumulation of beta-amyloid (1-42) in neurons is facilitated by the alpha 7 nicotinic acetylcholine receptor in Alzheimer's disease Neuroscience 110 2002 199 211
    • (2002) Neuroscience , vol.110 , pp. 199-211
    • Nagele, R.G.1    D'Andrea, M.R.2    Anderson, W.J.3    Wang, H.Y.4
  • 31
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • V.J. Palombella, O.J. Rando, A.L. Goldberg, and T. Maniatis The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B Cell 78 1994 773 785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 33
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • K.L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A.L. Goldberg Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules Cell 78 1994 761 771
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 36
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • A.L. Schwartz, and A. Ciechanover The ubiquitin-proteasome pathway and pathogenesis of human diseases Annu. Rev. Med. 50 1999 57 74
    • (1999) Annu. Rev. Med. , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 38
    • 0033712579 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: Possible importance in Alzheimer's disease
    • R. Shringarpure, T. Grune, N. Sitte, and K.J. Davies 4-Hydroxynonenal- modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease Cell. Mol. Life Sci. 57 2000 1802 1809
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1802-1809
    • Shringarpure, R.1    Grune, T.2    Sitte, N.3    Davies, K.J.4
  • 39
    • 0025376092 scopus 로고
    • Different configurational states of beta-amyloid and their distributions relative to plaques and tangles in Alzheimer disease
    • M.G. Spillantini, M. Goedert, R. Jakes, and A. Klug Different configurational states of beta-amyloid and their distributions relative to plaques and tangles in Alzheimer disease Proc. Natl. Acad. Sci. U.S.A. 87 1990 3947 3951
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3947-3951
    • Spillantini, M.G.1    Goedert, M.2    Jakes, R.3    Klug, A.4
  • 40
    • 0027361386 scopus 로고
    • Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular beta-amyloid or A4 peptides
    • A.M. Wertkin, R.S. Turner, S.J. Pleasure, T.E. Golde, S.G. Younkin, J.Q. Trojanowski, and V.M. Lee Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular beta-amyloid or A4 peptides Proc. Natl. Acad. Sci. U.S.A. 90 1993 9513 9517
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9513-9517
    • Wertkin, A.M.1    Turner, R.S.2    Pleasure, S.J.3    Golde, T.E.4    Younkin, S.G.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 41
    • 0029057814 scopus 로고
    • Intracellular a beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • A.J. Yang, M. Knauer, D.A. Burdick, and C. Glabe Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells J. Biol. Chem. 270 1995 14786 14792
    • (1995) J. Biol. Chem. , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 42
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta 1-42 pathogenesis
    • A.J. Yang, D. Chandswangbhuvana, L. Margol, and C.G. Glabe Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta 1-42 pathogenesis J. Neurosci. Res. 52 1998 691 698
    • (1998) J. Neurosci. Res. , vol.52 , pp. 691-698
    • Yang, A.J.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.G.4
  • 43
    • 0035158645 scopus 로고    scopus 로고
    • Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages
    • H. Yazawa, Z.X. Yu, K. Takeda, Y. Le, W. Gong, V.J. Ferrans, J.J. Oppenheim, C.C. Li, and J.M. Wang Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages FASEB J. 15 2001 2454 2462
    • (2001) FASEB J. , vol.15 , pp. 2454-2462
    • Yazawa, H.1    Yu, Z.X.2    Takeda, K.3    Le, Y.4    Gong, W.5    Ferrans, V.J.6    Oppenheim, J.J.7    Li, C.C.8    Wang, J.M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.