Copper- and iron-induced differential fibril formation in α-synuclein: TEM study

α-Synuclein filaments are the central component of intracytoplasmic inclusion bodies characteristic of Parkinson's disease (PD) and related disorders. Metals are the significant etiological factors in PD, and their interaction with α-synuclein affect dramatically the kinetics of fibrillation. C...

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Bibliographic Details
Published in:Neuroscience letters 2007-09, Vol.424 (2), p.78-82
Main Authors: Bharathi, Indi, S.S., Rao, K.S.J.
Format: Article
Language:English
Subjects:
alpha-Synuclein - chemistry
alpha-Synuclein - genetics
alpha-Synuclein - ultrastructure
Biological and medical sciences
Copper
Copper - chemistry
Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
Electron microscopy
Fibrils
Fundamental and applied biological sciences. Psychology
Humans
Iron
Iron - chemistry
Medical sciences
Microscopy, Electron, Transmission - methods
Mutation - physiology
Neurology
Parkinson's disease
Protein Binding
Time Factors
Vertebrates: nervous system and sense organs
α-Synuclein
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Summary:α-Synuclein filaments are the central component of intracytoplasmic inclusion bodies characteristic of Parkinson's disease (PD) and related disorders. Metals are the significant etiological factors in PD, and their interaction with α-synuclein affect dramatically the kinetics of fibrillation. Currently, we have investigated the influence of Cu(II) and Fe(III) on α-synuclein fibril formation. Cu(II) and Fe(III) selectively and differentially induced the formation of discrete α-synuclein fibrillar species. Transmission electron microscopy was used to monitor the aggregation state of α-synuclein (wild-type, A30P, A53T, and E46K) after 60 h with stirring at 37 °C in the presence and absence of metal ions. Cu(II) has induced thin long network-like fibrils with the wild-type of α-synuclein, while the mutant, showed amorphous aggregates with no fibrillar forms. Fe(III) induced short and thick fibrils with both wild and mutant forms and were similar to α-synuclein fibrils incubated without metal ion. The present study illustrates the metal-specific fibril morphology, and has relevance in understanding the role of metals in neurodegeneration.
ISSN:0304-3940
1872-7972
DOI:10.1016/j.neulet.2007.06.052