메뉴 건너뛰기




Volumn 464, Issue 1, 2015, Pages 342-347

Cu(II) promotes amyloid pore formation

Author keywords

Amyloid; Heavy metal; Parkinson's disease; Protofibril; synuclein

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; BAICALEIN; CUPRIC ION; COPPER; DIVALENT CATION; FLAVANONE DERIVATIVE; PROTEIN AGGREGATE; RECOMBINANT PROTEIN; THIAZOLE DERIVATIVE; THIOFLAVINE;

EID: 84937637686     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.06.156     Document Type: Article
Times cited : (7)

References (42)
  • 1
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • A.L. Fink The aggregation and fibrillation of alpha-synuclein Acc. Chem. Res. 39 2006 628 634
    • (2006) Acc. Chem. Res. , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 2
    • 77953575526 scopus 로고    scopus 로고
    • Oligomeric alpha-synuclein and its role in neuronal death
    • D.R. Brown Oligomeric alpha-synuclein and its role in neuronal death IUBMB Life 62 2010 334 339
    • (2010) IUBMB Life , vol.62 , pp. 334-339
    • Brown, D.R.1
  • 3
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain
    • C.A. Lasagna-Reeves, C.G. Glabe, and R. Kayed Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain J. Biol. Chem. 286 2011 22122 22130
    • (2011) J. Biol. Chem. , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 6
    • 84864538288 scopus 로고    scopus 로고
    • Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-Synuclein oligomers in lipid membranes
    • F. Schmidt, J. Levin, F. Kamp, H. Kretzschmar, A. Giese, and K. Bötzel Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-Synuclein oligomers in lipid membranes PLoS One 7 2012 e42545
    • (2012) PLoS One , vol.7
    • Schmidt, F.1    Levin, J.2    Kamp, F.3    Kretzschmar, H.4    Giese, A.5    Bötzel, K.6
  • 8
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease - Amyloid pores from pathogenic mutations
    • 291
    • H.A. Lashuel, D. Hartley, B.M. Petre, T. Walz, and P.T. Lansbury Neurodegenerative disease - amyloid pores from pathogenic mutations Nature 418 2002 291-291
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 9
    • 0037072284 scopus 로고    scopus 로고
    • Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • T.T. Ding, S.J. Lee, J.C. Rochet, and P.T. Lansbury Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes Biochemistry 41 2002 10209 10217
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury, P.T.4
  • 10
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • M.J. Volles, S.J. Lee, J.C. Rochet, M.D. Shtilerman, T.T. Ding, J.C. Kessler, and P.T. Lansbury Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease Biochemistry 40 2001 7812 7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury, P.T.7
  • 11
    • 78650763561 scopus 로고    scopus 로고
    • Membrane permeabilization by oligomeric alpha-Synuclein: In search of the mechanism
    • B.D. van Rooijen, M.M.A.E. Claessens, and V. Subramaniam Membrane permeabilization by oligomeric alpha-Synuclein: in search of the mechanism PLoS One 5 2010
    • (2010) PLoS One , vol.5
    • Van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 12
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • H.A. Lashuel, and P.T. Lansbury Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys. 39 2006 167 201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 14
    • 84879229182 scopus 로고    scopus 로고
    • In vitro study of α-Synuclein protofibrils by Cryo-EM suggests a Cu2+-dependent aggregation pathway
    • H. Zhang, A. Griggs, J.-C. Rochet, and Lia A. Stanciu In vitro study of α-Synuclein protofibrils by Cryo-EM suggests a Cu2+-dependent aggregation pathway Biophys. J. 104 2013 2706 2713
    • (2013) Biophys. J. , vol.104 , pp. 2706-2713
    • Zhang, H.1    Griggs, A.2    Rochet, J.-C.3    Stanciu, L.A.4
  • 16
    • 43049150678 scopus 로고    scopus 로고
    • Metals in Alzheimer's and Parkinson's diseases
    • K.J. Barnham, and A.I. Bush Metals in Alzheimer's and Parkinson's diseases Curr. Opin. Chem. Biol. 12 2008 222 228
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 18
    • 79954642381 scopus 로고    scopus 로고
    • Advances in metal-induced oxidative stress and human disease
    • K. Jomova, and M. Valko Advances in metal-induced oxidative stress and human disease Toxicology 283 2011 65 87
    • (2011) Toxicology , vol.283 , pp. 65-87
    • Jomova, K.1    Valko, M.2
  • 20
    • 72949084639 scopus 로고    scopus 로고
    • Interaction between α-Synuclein and metal ions, still looking for a role in the pathogenesis of Parkinson's disease
    • M. Bisaglia, I. Tessari, S. Mammi, and L. Bubacco Interaction between α-Synuclein and metal ions, still looking for a role in the pathogenesis of Parkinson's disease NeuroMolecular Med. 11 2009 239 251
    • (2009) NeuroMolecular Med , vol.11 , pp. 239-251
    • Bisaglia, M.1    Tessari, I.2    Mammi, S.3    Bubacco, L.4
  • 21
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein: A possible molecular link between Parkinson's disease and heavy metal exposure
    • V.N. Uversky, J. Li, and A.L. Fink Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein: a possible molecular link between Parkinson's disease and heavy metal exposure J. Biol. Chem. 276 2001 44284 44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 23
    • 79952780867 scopus 로고    scopus 로고
    • Coordination features and affinity of the Cu2+ site in the α-Synuclein protein of Parkinson's disease
    • C.G. Dudzik, E.D. Walter, and G.L. Millhauser Coordination features and affinity of the Cu2+ site in the α-Synuclein protein of Parkinson's disease Biochemistry 50 2011 1771 1777
    • (2011) Biochemistry , vol.50 , pp. 1771-1777
    • Dudzik, C.G.1    Walter, E.D.2    Millhauser, G.L.3
  • 25
    • 84884769320 scopus 로고    scopus 로고
    • Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases
    • B. Cheng, H. Gong, H.W. Xiao, R.B. Petersen, L. Zheng, and K. Huang Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases Biochim. Biophys. Acta-General Subj. 1830 2013 4860 4871
    • (2013) Biochim. Biophys. Acta-General Subj. , vol.1830 , pp. 4860-4871
    • Cheng, B.1    Gong, H.2    Xiao, H.W.3    Petersen, R.B.4    Zheng, L.5    Huang, K.6
  • 27
    • 84862815814 scopus 로고    scopus 로고
    • Pharmacokinetic study of baicalein after oral administration in monkeys
    • S. Tian, G.R. He, J.K. Song, S.B. Wang, W.Y. Xin, D. Zhang, and G.H. Du Pharmacokinetic study of baicalein after oral administration in monkeys Fitoterapia 83 2012 532 540
    • (2012) Fitoterapia , vol.83 , pp. 532-540
    • Tian, S.1    He, G.R.2    Song, J.K.3    Wang, S.B.4    Xin, W.Y.5    Zhang, D.6    Du, G.H.7
  • 29
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of alpha-Synuclein oligomers stabilized by the flavonoid baicalein
    • D.P. Hong, A.L. Fink, and V.N. Uversky Structural characteristics of alpha-Synuclein oligomers stabilized by the flavonoid baicalein J. Mol. Biol. 383 2008 214 223
    • (2008) J. Mol. Biol. , vol.383 , pp. 214-223
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3
  • 30
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of α-Synuclein and disaggregates existing fibrils
    • M. Zhu, S. Rajamani, J. Kaylor, S. Han, F. Zhou, and A.L. Fink The flavonoid baicalein inhibits fibrillation of α-Synuclein and disaggregates existing fibrils J. Biol. Chem. 279 2004 26846 26857
    • (2004) J. Biol. Chem. , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 32
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of α-Synuclein oligomers stabilized by the flavonoid baicalein
    • D.-P. Hong, A.L. Fink, and V.N. Uversky Structural characteristics of α-Synuclein oligomers stabilized by the flavonoid baicalein J. Mol. Biol. 383 2008 214 223
    • (2008) J. Mol. Biol. , vol.383 , pp. 214-223
    • Hong, D.-P.1    Fink, A.L.2    Uversky, V.N.3
  • 33
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim. Biophys. Sinica 39 2007 549 559
    • (2007) Acta Biochim. Biophys. Sinica , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 35
    • 68849102707 scopus 로고    scopus 로고
    • Unique copper-induced oligomers mediate alpha-synuclein toxicity
    • J.A. Wright, X.Y. Wang, and D.R. Brown Unique copper-induced oligomers mediate alpha-synuclein toxicity FASEB J. 23 2009 2384 2393
    • (2009) FASEB J. , vol.23 , pp. 2384-2393
    • Wright, J.A.1    Wang, X.Y.2    Brown, D.R.3
  • 37
    • 79960694577 scopus 로고    scopus 로고
    • Cu(II) mediates kinetically distinct, Non-amyloidogenic aggregation of amyloid-beta peptides
    • J.T. Pedersen, J. Ostergaard, N. Rozlosnik, B. Gammelgaard, and N.H.H. Heegaard Cu(II) mediates kinetically distinct, Non-amyloidogenic aggregation of amyloid-beta peptides J. Biol. Chem. 286 2011 26952 26963
    • (2011) J. Biol. Chem. , vol.286 , pp. 26952-26963
    • Pedersen, J.T.1    Ostergaard, J.2    Rozlosnik, N.3    Gammelgaard, B.4    Heegaard, N.H.H.5
  • 38
    • 60349093075 scopus 로고    scopus 로고
    • Metal binding to alpha-synuclein peptides and its contribution to toxicity
    • D.R. Brown Metal binding to alpha-synuclein peptides and its contribution to toxicity Biochem. Biophys. Res. Commun. 380 2009 377 381
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 377-381
    • Brown, D.R.1
  • 39
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II)-induced self-oligomerization of alpha-synuclein
    • S.R. Paik, H.J. Shin, J.H. Lee, C.S. Chang, and J. Kim Copper(II)-induced self-oligomerization of alpha-synuclein Biochem. J. 340 1999 821 828
    • (1999) Biochem. J. , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, C.S.4    Kim, J.5
  • 40
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • K.A. Conway, S.J. Lee, J.C. Rochet, T.T. Ding, R.E. Williamson, and P.T. Lansbury Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy Proc. Natl. Acad. Sci. U. S. A. 97 2000 571 576
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 41
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • H.A. Lashuel, B.M. Petre, J. Wall, M. Simon, R.J. Nowak, T. Walz, and P.T. Lansbury alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils J. Mol. Biol. 322 2002 1089 1102
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury, P.T.7
  • 42
    • 67349270928 scopus 로고    scopus 로고
    • Baicalein exerts neuroprotective effects in 6-hydroxydopamine-induced experimental parkinsonism in vivo and in vitro
    • X. Mu, G. He, Y. Cheng, X. Li, B. Xu, and G. Du Baicalein exerts neuroprotective effects in 6-hydroxydopamine-induced experimental parkinsonism in vivo and in vitro Pharmacol. Biochem. Behav. 92 2009 642 648
    • (2009) Pharmacol. Biochem. Behav. , vol.92 , pp. 642-648
    • Mu, X.1    He, G.2    Cheng, Y.3    Li, X.4    Xu, B.5    Du, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.