Challenges and complexities of alpha-synuclein toxicity: new postulates in unfolding the mystery associated with Parkinson's disease.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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http://ir.cftri.com/2052/
ABB-01-03 |
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| Title |
Challenges and complexities of alpha-synuclein toxicity: new postulates in unfolding the mystery associated with Parkinson's disease.
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| Creator |
Muralidhar, L. Hegde
Jagannatha Rao, K. S. |
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| Subject |
17 Toxicology
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| Description |
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.
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| Date |
2003
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Article
PeerReviewed |
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| Format |
application/pdf
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| Language |
en
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| Rights |
—
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| Identifier |
http://ir.cftri.com/2052/1/Archives_of_Biochemistry_and_Biophysics%2C_Volume_418%2C_Issue_2%2C_15_October_2003%2C_Pages_169-178.pdf
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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