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

Ms., Bharathi and Indi, S. S. and Rao, K. S. J. (2007) Copper- and iron-induced differential fibril formation in alpha-synuclein: TEM study. Neuroscience letters, 424 (2). pp. 78-82. ISSN 0304-3940

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Abstract

alpha-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 alpha-synuclein affect dramatically the kinetics of fibrillation. Currently, we have investigated the influence of Cu(II) and Fe(III) on alpha-synuclein fibril formation. Cu(II) and Fe(III) selectively and differentially induced the formation of discrete alpha-synuclein fibrillar species. Transmission electron microscopy was used to monitor the aggregation state of alpha-synuclein (wild-type, A30P, A53T, and E46K) after 60h with stirring at 37 degrees C in the presence and absence of metal ions. Cu(II) has induced thin long network-like fibrils with the wild-type of alpha-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 alpha-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.

Item Type: Article
Uncontrolled Keywords: alpha-Synuclein; Copper; Iron; Electron microscopy; Fibrils; Parkinson’s disease
Subjects: 600 Technology > 01 Medical sciences > 09 Human Physiology
600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 18 Aug 2008 11:42
Last Modified: 11 May 2012 03:47
URI: http://ir.cftri.com/id/eprint/1845

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