Klucken, Jochen and Outeiro, Tiago F. and Nguyen, Paul and McLean, Pamela J. and Hyman, Bradley T. (2006) Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging. FASEB JOURNAL, 20 (12). pp. 2050-2057. ISSN 0892-6638, 1530-6860
Full text not available from this repository. (Request a copy)Abstract
Oligomerization and aggregation of alpha-synuclein molecules are believed to play a major role in neuronal dysfunction and loss in Parkinson's disease (PD) and dementia with Lewy bodies. However, alpha-synuclein oligomerization and aggregation have been detected only indirectly in cells using detergent extraction methods. Here, we show for the first time intracellular alpha-synuclein oligomerization using fluorescence lifetime imaging (FLIM). Two forms of alpha-synuclein homomeric interactions were detected: an antiparallel amino terminus-carboxyl terminus interaction between alpha-synuclein molecules, and a close amino terminus-carboxy terminus interaction within single alpha-synuclein molecules. Coexpression of the chaperone protein Hsp70, which can block alpha-synuclein toxicity in several systems, causes alpha-synuclein to adopt a different, open conformation, but Hsp70 does not alter alpha-synuclein-alpha-synuclein interactions. Thus, the neuroprotective effect of Hsp70 can be explained by its chaperone activity on alpha-synuclein molecules, rather than alteration of alpha-synuclein-alpha-synuclein interactions.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PARKINSONS-DISEASE; DROSOPHILA MODEL; IN-VITRO; PROTEIN; AGGREGATION; DYNAMICS; SUPPRESSION; PHOSPHOLIPIDS; NEUROTOXICITY; GELDANAMYCIN; Parkinson's disease; Lewy body disease; chaperone; protein aggregation |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Neurologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 Jan 2021 07:36 |
| Last Modified: | 25 Jan 2021 07:36 |
| URI: | https://pred.uni-regensburg.de/id/eprint/33923 |
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