메뉴 건너뛰기




Volumn 2, Issue 1, 2014, Pages

Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies

Author keywords

Conformational disease; Misfolding; Neurodegeneration; Prion; Protein aggregation

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); ANTIBODY; DROSOPHILA PROTEIN; PEPTIDE FRAGMENT; PROTEIN BINDING;

EID: 84908021295     PISSN: None     EISSN: 20515960     Source Type: Journal    
DOI: 10.1186/2051-5960-2-43     Document Type: Article
Times cited : (10)

References (56)
  • 1
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M: The amyloid state of proteins in human diseases. Cell 2012, 148: 1188-1203. 10.1016/j.cell.2012.02.022
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 2
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • Bellotti V, Mangione P, Merlini G: Molecular mechanisms of amyloidosis. N Engl J Med 2003, 349: 583-596. 10.1056/NEJMra023144
    • (2003) N Engl J Med , vol.349 , pp. 583-596
    • Bellotti, V.1    Mangione, P.2    Merlini, G.3
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM: Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006, 75: 333-366. 10.1146/annurev.biochem.75.101304.123901
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner T, Radford SE: A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 2011, 43: 8-18. 10.1016/j.molcel.2011.05.012
    • (2011) Mol Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 5
    • 0038044258 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease
    • Dodel RC, Hampel H, Du YS: Immunotherapy for Alzheimer's disease. Lancet Neurol 2003, 2: 215-220. 10.1016/S1474-4422(03)00349-1
    • (2003) Lancet Neurol , vol.2 , pp. 215-220
    • Dodel, R.C.1    Hampel, H.2    Du, Y.S.3
  • 6
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid bold beta-peptide
    • Haass C, Selkoe DJ: Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid bold beta-peptide. Nat Rev Mol Cell Biol 2007, 8: 101-112. 10.1038/nrm2101
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 7
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-β and tau-a toxic pas de deux in Alzheimer's disease
    • Ittner LM, Götz J: Amyloid-β and tau-a toxic pas de deux in Alzheimer's disease. Nat Rev Neurosci 2011, 12: 65-72.
    • (2011) Nat Rev Neurosci , vol.12 , pp. 65-72
    • Ittner, L.M.1    Götz, J.2
  • 8
    • 84859610500 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid β protein
    • Walsh DM, Teplow DB: Alzheimer's disease and the amyloid β protein. Prog Mol Biol Tranls 2012, 107: 101-124.
    • (2012) Prog Mol Biol Tranls , vol.107 , pp. 101-124
    • Walsh, D.M.1    Teplow, D.B.2
  • 9
    • 84855795920 scopus 로고    scopus 로고
    • Review: assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils
    • Morgado I, Fändrich M: Review: assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils. Curr Opin Colloid In 2011, 16: 508-514. 10.1016/j.cocis.2011.06.016
    • (2011) Curr Opin Colloid In , vol.16 , pp. 508-514
    • Morgado, I.1    Fändrich, M.2
  • 12
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel HA, Lansbury PT Jr: Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 2006, 39: 167-201. 10.1017/S0033583506004422
    • (2006) Q Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 13
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: not only pathological agents but also ordered nanomaterials
    • Cherny I, Gazit E: Amyloids: not only pathological agents but also ordered nanomaterials. Angew Chem Int Edit 2008, 47: 4062-4069. 10.1002/anie.200703133
    • (2008) Angew Chem Int Edit , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 14
    • 84863986886 scopus 로고    scopus 로고
    • Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity
    • Fändrich M: Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity. J Mol Biol 2012, 421: 427-440. 10.1016/j.jmb.2012.01.006
    • (2012) J Mol Biol , vol.421 , pp. 427-440
    • Fändrich, M.1
  • 16
    • 38049056730 scopus 로고    scopus 로고
    • Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice
    • Martins IC, Kuperstein I, Wilkinson H, Maes E, Vanbrabant M: Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J 2008, 27: 224-233. 10.1038/sj.emboj.7601953
    • (2008) EMBO J , vol.27 , pp. 224-233
    • Martins, I.C.1    Kuperstein, I.2    Wilkinson, H.3    Maes, E.4    Vanbrabant, M.5
  • 17
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • Glabe CG: Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem Sci 2004, 29: 542-547. 10.1016/j.tibs.2004.08.009
    • (2004) Trends Biochem Sci , vol.29 , pp. 542-547
    • Glabe, C.G.1
  • 18
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Ronald Wetzel R: Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci U S A 2002, 99: 1485-1490. 10.1073/pnas.022662599
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Ronald Wetzel, R.2
  • 19
    • 84855987854 scopus 로고    scopus 로고
    • Structure-based design of conformation- and sequence-specific antibodies against amyloid β
    • Perchiacca JM, Ladiwala AR, Bhattacharya M, Tessier PM: Structure-based design of conformation- and sequence-specific antibodies against amyloid β. Proc Natl Acad Sci U S A 2012, 109: 84-89. 10.1073/pnas.1111232108
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 84-89
    • Perchiacca, J.M.1    Ladiwala, A.R.2    Bhattacharya, M.3    Tessier, P.M.4
  • 21
    • 66449106372 scopus 로고    scopus 로고
    • Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity
    • Kvam E, Nannenga BL, Wang MS, Jia Z, Sierks MR, Messer A: Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity. PLoS ONE 2009, 4(5):e5727. doi:10.1371/journal.pone.0005727 10.1371/journal.pone.0005727
    • (2009) PLoS ONE , vol.4 , Issue.5
    • Kvam, E.1    Nannenga, B.L.2    Wang, M.S.3    Jia, Z.4    Sierks, M.R.5    Messer, A.6
  • 22
    • 15044339964 scopus 로고    scopus 로고
    • Intraneuronal Abeta, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease
    • Crowther DC, Kinghorn KJ, Miranda E, Page R, Curry JA, Duthie FA, Gubb DC, Lomas DA: Intraneuronal Abeta, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease. Neuroscience 2005, 132: 123-135. 10.1016/j.neuroscience.2004.12.025
    • (2005) Neuroscience , vol.132 , pp. 123-135
    • Crowther, D.C.1    Kinghorn, K.J.2    Miranda, E.3    Page, R.4    Curry, J.A.5    Duthie, F.A.6    Gubb, D.C.7    Lomas, D.A.8
  • 26
    • 78049427560 scopus 로고    scopus 로고
    • Inhibition of GSK-3 ameliorates Aβ pathology in an adult-onset Drosophila model of Alzheimer's disease
    • Sofola O, Kerr F, RogersI KK, Augustin H, Gandy C, Allen MJ, Hardy J, Lovestone S, Partridge L: Inhibition of GSK-3 ameliorates Aβ pathology in an adult-onset Drosophila model of Alzheimer's disease. PLoS Genet 2010, 6(9):e1001087. doi:10.1371/journal.pgen.1001087 10.1371/journal.pgen.1001087
    • (2010) PLoS Genet , vol.6 , Issue.9
    • Sofola, O.1    Kerr, F.2    RogersI, K.K.3    Augustin, H.4    Gandy, C.5    Allen, M.J.6    Hardy, J.7    Lovestone, S.8    Partridge, L.9
  • 27
    • 77958449984 scopus 로고    scopus 로고
    • α-Synuclein: membrane interactions and toxicity in Parkinson's disease
    • Auluck PK, Caraveo G, Lindquist S: α-Synuclein: membrane interactions and toxicity in Parkinson's disease. Annu Rev Cell Dev Biol 2010, 26: 211-233. 10.1146/annurev.cellbio.042308.113313
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 33
    • 84856353669 scopus 로고    scopus 로고
    • High-molecular weight Aβ oligomers and protofibrils are the predominant Aβ species in the native soluble protein fraction of the AD brain
    • Upadhaya AR, Lungrin I, Yamaguchi H, Fändrich M, Thal DR: High-molecular weight Aβ oligomers and protofibrils are the predominant Aβ species in the native soluble protein fraction of the AD brain. J Cell Mol Med 2012, 16: 287-295. 10.1111/j.1582-4934.2011.01306.x
    • (2012) J Cell Mol Med , vol.16 , pp. 287-295
    • Upadhaya, A.R.1    Lungrin, I.2    Yamaguchi, H.3    Fändrich, M.4    Thal, D.R.5
  • 34
    • 79955872891 scopus 로고    scopus 로고
    • PTAA and B10: new approaches to amyloid detection in tissue-evaluation of amyloid detection in tissue with a conjugated polyelectrolyte and a fibril-specific antibody fragment
    • Kieninger B, Gioeva Z, Krüger S, Westermark GT, Friedrich RP, Fändrich M, Röcken C: PTAA and B10: new approaches to amyloid detection in tissue-evaluation of amyloid detection in tissue with a conjugated polyelectrolyte and a fibril-specific antibody fragment. Amyloid 2011, 18: 47-52. 10.3109/13506129.2011.560623
    • (2011) Amyloid , vol.18 , pp. 47-52
    • Kieninger, B.1    Gioeva, Z.2    Krüger, S.3    Westermark, G.T.4    Friedrich, R.P.5    Fändrich, M.6    Röcken, C.7
  • 35
    • 79952498441 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopic investigation of Aβ protofibrils: implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils
    • Scheidt HA, Morgado I, Rothemund S, Huster D, Fändrich M: Solid-state NMR spectroscopic investigation of Aβ protofibrils: implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils. Angew Chem Int Ed Engl 2011, 50: 2837-2840. 10.1002/anie.201007265
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 2837-2840
    • Scheidt, H.A.1    Morgado, I.2    Rothemund, S.3    Huster, D.4    Fändrich, M.5
  • 36
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation
    • Hortschansky P, Schroeckh V, Christopeit T, Zandomeneghi G, Fändrich M: The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation. Prot Sci 2005, 14: 1753-1759. 10.1110/ps.041266605
    • (2005) Prot Sci , vol.14 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fändrich, M.5
  • 38
    • 33847660443 scopus 로고    scopus 로고
    • An optimized transgenesis system for Drosophila using germ-line-specific φC31 integrases
    • Bischof K: An optimized transgenesis system for Drosophila using germ-line-specific φC31 integrases. Proc Natl Acad Sci U S A 2007, 104: 3312-3317. 10.1073/pnas.0611511104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3312-3317
    • Bischof, K.1
  • 39
    • 0033762437 scopus 로고    scopus 로고
    • The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2
    • Green C, Levashina E, McKimmie C, Dafforn T, Reichhart JM, Gubb D: The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2. Genetics 2000, 156: 1117-1127.
    • (2000) Genetics , vol.156 , pp. 1117-1127
    • Green, C.1    Levashina, E.2    McKimmie, C.3    Dafforn, T.4    Reichhart, J.M.5    Gubb, D.6
  • 40
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N: Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 1993, 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 42
    • 0003455528 scopus 로고    scopus 로고
    • Drosophila: a laboratory handbook
    • 2nd edition. Cold Spring Harbor, New York: Cold Spring Harbor Laborators Press. XXVIII
    • Ashburner M, Golic KG, Hawley RS: Drosophila: a laboratory handbook. 2nd edition. Cold Spring Harbor, New York: Cold Spring Harbor Laborators Press; 2005. XXVIII 1408pp
    • (2005) , pp. 1408
    • Ashburner, M.1    Golic, K.G.2    Hawley, R.S.3
  • 44
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH: Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 1989, 182: 319-326. 10.1016/0003-2697(89)90602-7
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 46
    • 52449104067 scopus 로고    scopus 로고
    • Abeta mediated diminution of MTT reduction-an artefact of single cell culture?
    • Rönicke R, Klemm A, Meinhardt J, Schröder UH, Fändrich M, Reymann KG: Abeta mediated diminution of MTT reduction-an artefact of single cell culture? PLoS ONE 2008, 3(9):e3236. doi:10.1371/journal.pone.0003236 10.1371/journal.pone.0003236
    • (2008) PLoS ONE , vol.3 , Issue.9
    • Rönicke, R.1    Klemm, A.2    Meinhardt, J.3    Schröder, U.H.4    Fändrich, M.5    Reymann, K.G.6
  • 52
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300: 486-489. 10.1126/science.1079469
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 53
    • 33645220400 scopus 로고    scopus 로고
    • Targeting amyloid-beta peptide (Abeta) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Abeta precursor protein (APP) transgenic mice
    • Lee EB, Leng LZ, Zhang B, Kwong L, Trojanowski JQ, Abel T, Lee VM: Targeting amyloid-beta peptide (Abeta) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Abeta precursor protein (APP) transgenic mice. J Biol Chem 2006, 281: 4292-4299. 10.1074/jbc. M511018200
    • (2006) J Biol Chem , vol.281 , pp. 4292-4299
    • Lee, E.B.1    Leng, L.Z.2    Zhang, B.3    Kwong, L.4    Trojanowski, J.Q.5    Abel, T.6    Lee, V.M.7
  • 54
    • 78149424228 scopus 로고    scopus 로고
    • Immunomodulation targeting abnormal protein conformation reduces pathology in a mouse model of Alzheimer's disease
    • Goñi F, Prelli F, Ji Y, Scholtzova H, Yang J, Sun Y, Liang FX, Kascsak R, Kascsak R, Mehta P, Wisniewski T: Immunomodulation targeting abnormal protein conformation reduces pathology in a mouse model of Alzheimer's disease. PLoS ONE 2010, 5(10):e13391. doi:10.1371/journal.pone.0013391 10.1371/journal.pone.0013391
    • (2010) PLoS ONE , vol.5 , Issue.10
    • Goñi, F.1    Prelli, F.2    Ji, Y.3    Scholtzova, H.4    Yang, J.5    Sun, Y.6    Liang, F.X.7    Kascsak, R.8    Kascsak, R.9    Mehta, P.10    Wisniewski, T.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.