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Challenges and complexities of alpha-synuclein toxicity: new postulates in unfolding the mystery associated with Parkinson's disease.

Muralidhar, L. Hegde and Jagannatha Rao, K. S. (2003) Challenges and complexities of alpha-synuclein toxicity: new postulates in unfolding the mystery associated with Parkinson's disease. Archives of Biochemistry and Biophysics, 418 (2). pp. 169-78. ISSN 0003-9861

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Abstract

The discovery of two missense mutations in alpha-synuclein gene and the identification of the alpha-synuclein as the major component of Lewy bodies and Lewy neurites have imparted a new direction in understanding Parkinson's disease. Now that alpha-synuclein has been implicated in several neurodegenerative disorders makes it increasingly clear that aggregation of alpha-synuclein is a hallmark feature in neurodegeneration. Although little has been learned about its normal function, alpha-synuclein appears to be associated with membrane phospholipids and may therefore participate in a number of cell signaling pathways. Here, we review the localization, structure, and function of alpha-synuclein and provide a new hypothesis on, (a) the disruption in the membrane binding ability of synuclein which may be the major culprit leading to the alpha-synuclein aggregation and (b) the complexity associated with nuclear localization of alpha-synuclein and its possible binding property to DNA. Further, we postulated the three possible mechanisms of synuclein induced neuronal degeneration in Parkinson's disease.

Item Type: Article
Uncontrolled Keywords: a-Synuclein; Parkinson�s disease; Neurodegeneration; Protein aggregation; Membrane binding; Neuronal plasticity
Subjects: 600 Technology > 01 Medical sciences > 17 Toxicology
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 26 Jun 2009 05:18
Last Modified: 22 Jun 2012 06:31
URI: http://ir.cftri.com/id/eprint/2052

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