![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
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
![[img]](http://ir.cftri.res.in/style/images/fileicons/application_pdf.png) |
PDF
Archives_of_Biochemistry_and_Biophysics,_Volume_418,_Issue_2,_15_October_2003,_Pages_169-178.pdf Restricted to Registered users only Download (278kB) |
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.res.in/id/eprint/2052 |
Actions (login required)
 |
View Item |