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Volumn 1814, Issue 12, 2011, Pages 1703-1712

Conformation-dependent scFv antibodies specifically recognize the oligomers assembled from various amyloids and show colocalization of amyloid fibrils with oligomers in patients with amyloidoses

Author keywords

Amyloid; Amyloidosis; Fibril deposit; Single chain variable fragment antibody

Indexed keywords

ALPHA SYNUCLEIN; AMYLIN; AMYLOID; AMYLOID BETA PROTEIN[1-40]; INSULIN; LYSOZYME; OLIGOMER; PRION PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

EID: 80054754517     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.09.005     Document Type: Article
Times cited : (28)

References (54)
  • 1
    • 28244446220 scopus 로고    scopus 로고
    • Aspects on human amyloid forms and their fibril polypeptides
    • DOI 10.1111/j.1742-4658.2005.05024.x
    • P. Westermark Aspects on human amyloid forms and their fibril polypeptides FEBS J. 272 2005 5942 5949 (Pubitemid 41713686)
    • (2005) FEBS Journal , vol.272 , Issue.23 , pp. 5942-5949
    • Westermark, P.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 77951767673 scopus 로고    scopus 로고
    • The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism
    • S.B. Nielsen, K. Wilhelm, B. Vad, J. Schleucher, L.A. Morozova-Roche, and D. Otzen The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism J. Mol. Biol. 398 2010 351 361
    • (2010) J. Mol. Biol. , vol.398 , pp. 351-361
    • Nielsen, S.B.1    Wilhelm, K.2    Vad, B.3    Schleucher, J.4    Morozova-Roche, L.A.5    Otzen, D.6
  • 4
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • D.J. Selkoe Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease Annu. Rev. Cell Biol. 10 1994 373 403 (Pubitemid 24372824)
    • (1994) Annual Review of Cell Biology , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 6
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • DOI 10.1038/35081564
    • M. Goedert Alpha-synuclein and neurodegenerative diseases Nat. Rev. Neurosci. 2 2001 492 501 (Pubitemid 33676584)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.7 , pp. 492-501
    • Goedert, M.1
  • 12
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • DOI 10.1038/nrn1007
    • C. Soto Unfolding the role of protein misfolding in neurodegenerative diseases Nat. Rev. Neurosci. 4 2003 49 60 (Pubitemid 37271088)
    • (2003) Nature Reviews Neuroscience , vol.4 , Issue.1 , pp. 49-60
    • Soto, C.1
  • 13
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • C.G. Glabe Structural classification of toxic amyloid oligomers J. Biol. Chem. 283 2008 29639 29643
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 14
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 15
    • 78049290389 scopus 로고    scopus 로고
    • Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    • M. Stefani Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity FEBS J. 277 2010 4602 4613
    • (2010) FEBS J. , vol.277 , pp. 4602-4613
    • Stefani, M.1
  • 16
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid {beta}-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • M. Jin, N. Shepardson, T. Yang, G. Chen, D. Walsh, and D.J. Selkoe Soluble amyloid {beta}-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration Proc. Natl. Acad. Sci. U. S. A. 108 2011 5819 5824
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 19
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • R. Kayed, E. Head, J.L. Thompson, T.M. McIntire, S.C. Milton, C.W. Cotman, and C.G. Glabe Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , 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    Glabel, C.G.7
  • 23
    • 66449097646 scopus 로고    scopus 로고
    • Detecting morphologically distinct oligomeric forms of alpha-synuclein
    • S. Emadi, S. Kasturirangan, M.S. Wang, P. Schulz, and M.R. Sierks Detecting morphologically distinct oligomeric forms of alpha-synuclein J. Biol. Chem. 284 2009 11048 11058
    • (2009) J. Biol. Chem. , vol.284 , pp. 11048-11058
    • Emadi, S.1    Kasturirangan, S.2    Wang, M.S.3    Schulz, P.4    Sierks, M.R.5
  • 25
    • 34547672881 scopus 로고    scopus 로고
    • Methylene blue inhibits amyloid Aβ oligomerization by promoting fibrillization
    • DOI 10.1021/bi700411k
    • M. Necula, L. Breydo, S. Milton, R. Kayed, W.E. van der Veer, P. Tone, and C.G. Glabe Methylene blue inhibits amyloid Abeta oligomerization by promoting fibrillization Biochemistry 46 2007 8850 8860 (Pubitemid 47208418)
    • (2007) Biochemistry , vol.46 , Issue.30 , pp. 8850-8860
    • Necula, M.1    Breydo, L.2    Milton, S.3    Kayed, R.4    Van Der Veer, W.E.5    Tone, P.6    Glabe, C.G.7
  • 26
    • 20444412385 scopus 로고    scopus 로고
    • A new method for purification of recombinant human α-synuclein in Escherichia coli
    • DOI 10.1016/j.pep.2005.02.014, PII S1046592805000719
    • C. Huang, G. Ren, H. Zhou, and C.C. Wang A new method for purification of recombinant human alpha-synuclein in Escherichia coli Protein Expr. Purif. 42 2005 173 177 (Pubitemid 40793408)
    • (2005) Protein Expression and Purification , vol.42 , Issue.1 , pp. 173-177
    • Huang, C.1    Ren, G.2    Zhou, H.3    Wang, C.-C.4
  • 27
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • J.W. Kelly Mechanisms of amyloidogenesis Nat. Struct. Biol. 7 2000 824 826
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 28
    • 33846005437 scopus 로고    scopus 로고
    • Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
    • DOI 10.1016/j.jmb.2006.11.009, PII S0022283606015385
    • M. Fandrich Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils J. Mol. Biol. 365 2007 1266 1270 (Pubitemid 46048846)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1266-1270
    • Fandrich, M.1
  • 29
    • 34547947641 scopus 로고    scopus 로고
    • Conversion of non-fibrillar β-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation
    • DOI 10.1016/j.bbrc.2007.07.082, PII S0006291X07015707
    • N. Benseny-Cases, M. Cocera, and J. Cladera Conversion of non-fibrillar beta-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation Biochem. Biophys. Res. Commun. 361 2007 916 921 (Pubitemid 47263455)
    • (2007) Biochemical and Biophysical Research Communications , vol.361 , Issue.4 , pp. 916-921
    • Benseny-Cases, N.1    Cocera, M.2    Cladera, J.3
  • 30
    • 33749251222 scopus 로고    scopus 로고
    • Kinetics and Thermodynamics of Amyloid Assembly Using a High-Performance Liquid Chromatography-Based Sedimentation Assay
    • DOI 10.1016/S0076-6879(06)13003-7, PII S0076687906130037, Amyloid, Prions, and Other Protein Aggregates, Part C
    • B. O'Nuallain, A.K. Thakur, A.D. Williams, A.M. Bhattacharyya, S. Chen, G. Thiagarajan, and R. Wetzel Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay Methods Enzymol. 413 2006 34 74 (Pubitemid 44528684)
    • (2006) Methods in Enzymology , vol.413 , pp. 34-74
    • O'Nuallain, B.1    Thakur, A.K.2    Williams, A.D.3    Bhattacharyya, A.M.4    Chen, S.5    Thiagarajan, G.6    Wetzel, R.7
  • 32
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis
    • DOI 10.1210/er.2007-0037
    • L. Haataja, T. Gurlo, C.J. Huang, and P.C. Butler Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis Endocr. Rev. 29 2008 303 316 (Pubitemid 351679701)
    • (2008) Endocrine Reviews , vol.29 , Issue.3 , pp. 303-316
    • Haataja, L.1    Gurlo, T.2    Huang, C.J.3    Butler, P.C.4
  • 34
    • 41549105851 scopus 로고    scopus 로고
    • Modulation of amyloid-β aggregation and toxicity by inosose stereoisomers
    • DOI 10.1111/j.1742-4658.2008.06321.x
    • M. Nitz, D. Fenili, A.A. Darabie, L. Wu, J.E. Cousins, and J. McLaurin Modulation of amyloid-beta aggregation and toxicity by inosose stereoisomers FEBS J. 275 2008 1663 1674 (Pubitemid 351463985)
    • (2008) FEBS Journal , vol.275 , Issue.8 , pp. 1663-1674
    • Nitz, M.1    Fenili, D.2    Darabie, A.A.3    Wu, L.4    Cousins, J.E.5    McLaurin, J.6
  • 37
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • DOI 10.1016/j.tibs.2004.08.009, PII S0968000404002105
    • C.G. Glabe Conformation-dependent antibodies target diseases of protein misfolding Trends Biochem. Sci. 29 2004 542 547 (Pubitemid 39265171)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.10 , pp. 542-547
    • Glabe, C.G.1
  • 38
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
    • DOI 10.1038/nsmb1345, PII NSMB1345
    • S. Chimon, M.A. Shaibat, C.R. Jones, D.C. Calero, B. Aizezi, and Y. Ishii Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid Nat. Struct. Mol. Biol. 14 2007 1157 1164 (Pubitemid 350223342)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 41
    • 62049083728 scopus 로고    scopus 로고
    • Direct in vivo intracellular selection of conformation-sensitive antibody domains targeting Alzheimer's amyloid-beta oligomers
    • G. Meli, M. Visintin, I. Cannistraci, and A. Cattaneo Direct in vivo intracellular selection of conformation-sensitive antibody domains targeting Alzheimer's amyloid-beta oligomers J. Mol. Biol. 387 2009 584 606
    • (2009) J. Mol. Biol. , vol.387 , pp. 584-606
    • Meli, G.1    Visintin, M.2    Cannistraci, I.3    Cattaneo, A.4
  • 42
    • 56249092747 scopus 로고    scopus 로고
    • Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells
    • A. Zameer, S. Kasturirangan, S. Emadi, S.V. Nimmagadda, and M.R. Sierks Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells J. Mol. Biol. 384 2008 917 928
    • (2008) J. Mol. Biol. , vol.384 , pp. 917-928
    • Zameer, A.1    Kasturirangan, S.2    Emadi, S.3    Nimmagadda, S.V.4    Sierks, M.R.5
  • 43
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of amyloid β (1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action
    • DOI 10.1002/cbic.200700427
    • M. Bartolini, C. Bertucci, M.L. Bolognesi, A. Cavalli, C. Melchiorre, and V. Andrisano Insight into the kinetic of amyloid beta (1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action Chembiochem 8 2007 2152 2161 (Pubitemid 350220767)
    • (2007) ChemBioChem , vol.8 , Issue.17 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 44
    • 1542327644 scopus 로고    scopus 로고
    • Ligand-Dependent Inhibition and Reversal of Tau Filament Formation
    • DOI 10.1021/bi036094h
    • C. Chirita, M. Necula, and J. Kuret Ligand-dependent inhibition and reversal of tau filament formation Biochemistry 43 2004 2879 2887 (Pubitemid 38327819)
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2879-2887
    • Chirita, C.1    Necula, M.2    Kuret, J.3
  • 46
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils
    • A.K. Paravastu, R.D. Leapman, W.M. Yau, and R. Tycko Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils Proc. Natl. Acad. Sci. U. S. A. 105 2008 18349 18354
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 47
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • A.T. Petkova, R.D. Leapman, Z. Guo, W.M. Yau, M.P. Mattson, and R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils Science 307 2005 262 265 (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 48
    • 77955045091 scopus 로고    scopus 로고
    • Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies
    • G.T. Debelouchina, G.W. Platt, M.J. Bayro, S.E. Radford, and R.G. Griffin Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies J. Am. Chem. Soc. 132 2010 10414 10423
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10414-10423
    • Debelouchina, G.T.1    Platt, G.W.2    Bayro, M.J.3    Radford, S.E.4    Griffin, R.G.5
  • 49
    • 77955273305 scopus 로고    scopus 로고
    • Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated
    • R. Kodali, A.D. Williams, S. Chemuru, and R. Wetzel Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated J. Mol. Biol. 401 2010 503 517
    • (2010) J. Mol. Biol. , vol.401 , pp. 503-517
    • Kodali, R.1    Williams, A.D.2    Chemuru, S.3    Wetzel, R.4
  • 51
    • 65549131364 scopus 로고    scopus 로고
    • Applications of single-chain variable fragment antibodies in therapeutics and diagnostics
    • N.E. Weisser, and J.C. Hall Applications of single-chain variable fragment antibodies in therapeutics and diagnostics Biotechnol. Adv. 27 2009 502 520
    • (2009) Biotechnol. Adv. , vol.27 , pp. 502-520
    • Weisser, N.E.1    Hall, J.C.2
  • 52
    • 0035969513 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes: From molecular misfolding to islet pathophysiology
    • DOI 10.1016/S0925-4439(01)00078-3, PII S0925443901000783
    • E.T. Jaikaran, and A. Clark Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology Biochim. Biophys. Acta 1537 2001 179 203 (Pubitemid 33139801)
    • (2001) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1537 , Issue.3 , pp. 179-203
    • Jaikaran, E.T.A.S.1    Clark, A.2
  • 54
    • 34248160486 scopus 로고    scopus 로고
    • Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced β-cell apoptosis in h-IAPP transgenic mice
    • DOI 10.2337/db06-1579
    • C.Y. Lin, T. Gurlo, R. Kayed, A.E. Butler, L. Haataja, C.G. Glabe, and P.C. Butler Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced beta-cell apoptosis in h-IAPP transgenic mice Diabetes 56 2007 1324 1332 (Pubitemid 46715613)
    • (2007) Diabetes , vol.56 , Issue.5 , pp. 1324-1332
    • Lin, C.-Y.1    Gurlo, T.2    Kayed, R.3    Butler, A.E.4    Haataja, L.5    Glabe, C.G.6    Butler, P.C.7


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