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α-Synuclein and Neurodegenerative Disorders:
Formation of Pathological Protein Aggregates
- Date/Time : Thu September 18., 2003
- Speaker : 백승렬 교수
- 인하대 의대 생화학교실
- Place : Life Science Bldg. #104
- For inquires : Professor Kwan Yong Choi Dept. of Life Science
생명과학과 최관용 교수 (☎279-2295)
- Abstract -
Amyloidosis defining a condition that generates insoluble fibrous protein aggregates from innocuous soluble proteins is the common pathological phenomenon observed in various neurodegenerative disorders. α-Synuclein is a pathological component of Parkinsons disease by participating in the Lewy body formation as the major filamentous constituent. The protein is also related to other degenerative disorders such as Alzheimers disease, Dementia with Lewy bodies, and multiple system atrophy. In this presentation, pathologically relevant mechanisms for the protein aggregation of α-synuclein will be addressed by analyzing biochemically specific phenomenon of the protein self-oligomerization observed under various conditions including metal-catalyzed oxidation. The ligand-induced protein self-oligomerization has been demonstrated to have potential for screening α-synuclein interactive small molecules which could act lead compounds for the eventual drug development. In conclusion,α-asynuclein is introduced as a structurally versatile molecule which could generate various forms of protein aggregates with corresponding physiological/pathological functions, if any. This talk will end up with an open question concerning cause-and-effect relationship of α-ynuclein for the Parkinsons disease by introducing toxic intermediate hypothesis .