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Volumn 275, Issue 23, 2008, Pages 5982-5993

Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin

Author keywords

Alzheimer's disease; Amyloid ; Molecular chaperone; Prefoldin; Soluble oligomers

Indexed keywords

ACTIN; AMYLOID BETA PROTEIN; CHAPERONE; OLIGOMER; PREFOLDIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 55949096479     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06727.x     Document Type: Article
Times cited : (56)

References (55)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81, 741 766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 0002080057 scopus 로고    scopus 로고
    • The neuropathology of Alzheimer disease and the structural basis of its cognitive alterations
    • In. Terry, R.D., Katzman, R., Bick, K.L. Sisodia, S.S., eds. pp. Lipponcott Williams and Wilikins, Philadelphia, PA.
    • Terry RD, Maslia E Hansen LA (1999) The neuropathology of Alzheimer disease and the structural basis of its cognitive alterations. In Alzheimer Disease (Terry RD, Katzman R, Bick KL Sisodia SS, eds pp. 187 206. Lipponcott Williams and Wilikins, Philadelphia, PA.
    • (1999) Alzheimer Disease , pp. 187-206
    • Terry, R.D.1    Maslia, E.2    Hansen, L.A.3
  • 3
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein WL, Krafft GA Finch CE (2001) Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 24, 219 224.
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353 356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass C Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8, 101 112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • Walsh DM Selkoe DJ (2007) Aβ oligomers - a decade of discovery. J Neurochem 101, 1172 1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 9
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26, 267 298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 12
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ Selkoe DJ (2002) Naturally secreted oligomers of amyloid β 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
  • 13
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • Laferla FM, Green KN Oddo S (2007) Intracellular amyloid-β in Alzheimer's disease. Nat Rev Neurosci 8, 499 509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 14
    • 0036772311 scopus 로고    scopus 로고
    • Intracellular A-beta amyloid, a sign for worse things to come?
    • Echeverria V Cuello AC (2002) Intracellular A-beta amyloid, a sign for worse things to come? Mol Neurobiol 26, 299 316.
    • (2002) Mol Neurobiol , vol.26 , pp. 299-316
    • Echeverria, V.1    Cuello, A.C.2
  • 15
    • 0036550597 scopus 로고    scopus 로고
    • Significance of intracellular Aβ42 accumulation in Alzheimer's disease
    • Tabira T, Chui DH Kuroda S (2002) Significance of intracellular Aβ42 accumulation in Alzheimer's disease. Front Biosci 7, a44 49.
    • (2002) Front Biosci , vol.7
    • Tabira, T.1    Chui, D.H.2    Kuroda, S.3
  • 16
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • Walsh DM, Tseng BP, Rydel RE, Podlisny MB Selkoe DJ (2000) The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 39, 10831 10839.
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 17
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi RH, Almeida CG, Kearney PF, Yu F, Lin MT, Milner TA Gouras GK (2004) Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J Neurosci 24, 3592 3599.
    • (2004) J Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 18
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed β-amyloid in neurons
    • Magrane J, Smith RC, Walsh K Querfurth HW (2004) Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed β-amyloid in neurons. J Neurosci 24, 1700 1706.
    • (2004) J Neurosci , vol.24 , pp. 1700-1706
    • Magrane, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 19
    • 7244236841 scopus 로고    scopus 로고
    • A modified β-amyloid hypothesis: Intraneuronal accumulation of the β-amyloid peptide - The first step of a fatal cascade
    • Wirths O, Multhaup G Bayer TA (2004) A modified β-amyloid hypothesis: intraneuronal accumulation of the β-amyloid peptide - the first step of a fatal cascade. J Neurochem 91, 513 520.
    • (2004) J Neurochem , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 22
    • 33646461282 scopus 로고    scopus 로고
    • β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida CG, Takahashi RH Gouras GK (2006) β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci 26, 4277 4288.
    • (2006) J Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 24
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852 1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 25
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J Horwich A (2006) Molecular chaperones and protein quality control. Cell 125, 443 451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 26
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6, 11 22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 27
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro
    • Evans CG, Wisen S Gestwicki JE (2006) Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro. J Biol Chem 281, 33182 33191.
    • (2006) J Biol Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 28
    • 14144252923 scopus 로고    scopus 로고
    • Hsp20, a novel α-crystallin, prevents Aβ fibril formation and toxicity
    • Lee S, Carson K, Rice-Ficht A Good T (2005) Hsp20, a novel α-crystallin, prevents Aβ fibril formation and toxicity. Protein Sci 14, 593 601.
    • (2005) Protein Sci , vol.14 , pp. 593-601
    • Lee, S.1    Carson, K.2    Rice-Ficht, A.3    Good, T.4
  • 31
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • Hansen WJ, Cowan NJ Welch WJ (1999) Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J Cell Biol 145, 265 277.
    • (1999) J Cell Biol , vol.145 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 32
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers K, Waldmann T, Leroux MR, Grein K, Shevchenko A, Schiebel E Hartl FU (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18, 75 84.
    • (1999) EMBO J , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5    Schiebel, E.6    Hartl, F.U.7
  • 34
    • 3843093899 scopus 로고    scopus 로고
    • Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: Contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin
    • Okochi M, Nomura T, Zako T, Arakawa T, Iizuka R, Ueda H, Funatsu T, Leroux M Yohda M (2004) Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin. J Biol Chem 279, 31788 31795.
    • (2004) J Biol Chem , vol.279 , pp. 31788-31795
    • Okochi, M.1    Nomura, T.2    Zako, T.3    Arakawa, T.4    Iizuka, R.5    Ueda, H.6    Funatsu, T.7    Leroux, M.8    Yohda, M.9
  • 37
    • 33750287973 scopus 로고    scopus 로고
    • Localization of prefoldin interaction sites in the hyperthermophilic group II chaperonin and correlations between binding rate and protein transfer rate
    • Zako T, Murase Y, Iizuka R, Yoshida T, Kanzaki T, Ide N, Maeda M, Funatsu T Yohda M (2006) Localization of prefoldin interaction sites in the hyperthermophilic group II chaperonin and correlations between binding rate and protein transfer rate. J Mol Biol 364, 110 120.
    • (2006) J Mol Biol , vol.364 , pp. 110-120
    • Zako, T.1    Murase, Y.2    Iizuka, R.3    Yoshida, T.4    Kanzaki, T.5    Ide, N.6    Maeda, M.7    Funatsu, T.8    Yohda, M.9
  • 38
    • 0036299118 scopus 로고    scopus 로고
    • Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding
    • Okochi M, Yoshida T, Maruyama T, Kawarabayasi Y, Kikuchi H Yohda M (2002) Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding. Biochem Biophys Res Commun 291, 769 774.
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 769-774
    • Okochi, M.1    Yoshida, T.2    Maruyama, T.3    Kawarabayasi, Y.4    Kikuchi, H.5    Yohda, M.6
  • 39
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert R, Leroux MR, Scheufler C, Hartl FU Moarefi I (2000) Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621 632.
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 42
    • 33745712353 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human prefoldin and SPEC domain protein gene (PFD6L) from the fetal brain
    • Zhang J, Liu L, Zhang X, Jin F, Chen J, Ji C, Gu S, Xie Y Mao Y (2006) Cloning and characterization of a novel human prefoldin and SPEC domain protein gene (PFD6L) from the fetal brain. Biochem Genet 44, 69 74.
    • (2006) Biochem Genet , vol.44 , pp. 69-74
    • Zhang, J.1    Liu, L.2    Zhang, X.3    Jin, F.4    Chen, J.5    Ji, C.6    Gu, S.7    Xie, Y.8    Mao, Y.9
  • 43
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H III. (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2, 404 410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • Levine Iii., H.1
  • 44
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S Glabe CG (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282, 10311 10324.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 45
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, Necula M, Margol L, Wu J, Breydo L, Thompson JL et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2, 18.
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5    Necula, M.6    Margol, L.7    Wu, J.8    Breydo, L.9    Thompson, J.L.10
  • 50
    • 0034660602 scopus 로고    scopus 로고
    • Glutamine synthetase, hemoglobin α-chain, and macrophage migration inhibitory factor binding to amyloid β-protein: Their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation
    • Oyama R, Yamamoto H Titani K (2000) Glutamine synthetase, hemoglobin α-chain, and macrophage migration inhibitory factor binding to amyloid β-protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation. Biochim Biophys Acta 1479, 91 102.
    • (2000) Biochim Biophys Acta , vol.1479 , pp. 91-102
    • Oyama, R.1    Yamamoto, H.2    Titani, K.3
  • 51
    • 39049170168 scopus 로고    scopus 로고
    • Structure and molecular dynamics simulation of archaeal prefoldin: The molecular mechanism for binding and recognition of nonnative substrate proteins
    • Ohtaki A, Kida H, Miyata Y, Ide N, Yonezawa A, Arakawa T, Iizuka R, Noguchi K, Kita A, Odaka M et al. (2008) Structure and molecular dynamics simulation of archaeal prefoldin: the molecular mechanism for binding and recognition of nonnative substrate proteins. J Mol Biol 376, 1130 1141.
    • (2008) J Mol Biol , vol.376 , pp. 1130-1141
    • Ohtaki, A.1    Kida, H.2    Miyata, Y.3    Ide, N.4    Yonezawa, A.5    Arakawa, T.6    Iizuka, R.7    Noguchi, K.8    Kita, A.9    Odaka, M.10
  • 54
    • 40649126526 scopus 로고    scopus 로고
    • Functional characterization of recombinant prefoldin complexes from a hyperthermophilic archaeon, Thermococcus sp. strain KS-1
    • Iizuka R, Sugano Y, Ide N, Ohtaki A, Yoshida T, Fujiwara S, Imanaka T Yohda M (2008) Functional characterization of recombinant prefoldin complexes from a hyperthermophilic archaeon, Thermococcus sp. strain KS-1. J Mol Biol 377, 972 983.
    • (2008) J Mol Biol , vol.377 , pp. 972-983
    • Iizuka, R.1    Sugano, Y.2    Ide, N.3    Ohtaki, A.4    Yoshida, T.5    Fujiwara, S.6    Imanaka, T.7    Yohda, M.8
  • 55
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction
    • Liu Y, Peterson DA, Kimura H Schubert D (1997) Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J Neurochem 69, 581 593.
    • (1997) J Neurochem , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4


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