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• W2912622904 abstract "Event Abstract Back to Event In vivo characterization of different alpha-synuclein variants Anke Van Der Perren1*, Géraldine Gelders1, Nikol Shakhbazyan1, Francesca Macchi1, Chris Van Den Haute1, 2 and Veerle Baekelandt1, 2 1 KU Leuven, Neurosciences, Belgium 2 KU Leuven, Belgium Alpha-synuclein (α-SYN) is a key player in Parkinson’s disease, but the exact relationship between α-SYN aggregation and the pathogenesis remains unresolved. There is emerging evidence that α-SYN can adopt distinct conformations that are characterized by noticeable differences in structural and phenotypic features (Peelaerts et al. Nature, 2015). In addition, it has been shown that neuroinflammatory processes are closely linked to dopaminergic neurodegeneration. We presume that immune alterations in response to different α-SYN conformations may play a critical role in modulating the progression as well as the outcome of the disease. In this study, we aim to analyze the effect of different α-SYN mutants (different propensity to form oligomeric or fibrillar aggregates) in terms of aggregation, neurodegeneration and neuroinflammation in vivo. More specifically, we will compare the aggregation prone A53T clinical mutant which we have previously characterized in detail (Van der Perren et al. Neurobiology of aging, 2014, 2015) with WT α-SYN, the 1-110 truncation promoting α-SYN aggregation and the artificial E57K, E35K and A56P α-SYN mutants that were shown to induce oligomers but not fibrils. We overexpressed the different α-SYN mutants in the substantia nigra (SN) of the rat using rAAV2/7 viral vectors. To assess motor deficits the rats were subjected to the cylinder test. Two and four weeks post injection a significant difference was observed in the use of the left forepaw between the groups with the 1-110 truncation and the oligomeric mutants (E57K, E35K, A56P). Thioflavin S staining and oligomer-specific antibodies were used to discern fibrillar and oligomeric α-SYN as well as biochemical analysis using sarkosyl treatment. The level of neurodegeneration was assessed in the SN and the striatum by immunohistochemical staining. This revealed clear differences between fibrillary and oligomeric α-SYN. Characterization of neuroinflammatory markers is ongoing. These results support our hypothesis that distinct α-SYN conformations may play a critical role in the progression of Parkinson’s disease. Keywords: alpha-Synuclein, Parkinson’s disease, neurodegeneration, Neuroinflammation, vector-based model Conference: 12th National Congress of the Belgian Society for Neuroscience, Gent, Belgium, 22 May - 22 May, 2017. Presentation Type: Poster Presentation Topic: Disorders of the Nervous System Citation: Van Der Perren A, Gelders G, Shakhbazyan N, Macchi F, Van Den Haute C and Baekelandt V (2019). In vivo characterization of different alpha-synuclein variants. Front. Neurosci. Conference Abstract: 12th National Congress of the Belgian Society for Neuroscience. doi: 10.3389/conf.fnins.2017.94.00052 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 22 Apr 2017; Published Online: 25 Jan 2019. * Correspondence: Dr. Anke Van Der Perren, KU Leuven, Neurosciences, Leuven, Vlaams-Brabant, 3000, Belgium, anke.vanderperren@kuleuven.be Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Anke Van Der Perren Géraldine Gelders Nikol Shakhbazyan Francesca Macchi Chris Van Den Haute Veerle Baekelandt Google Anke Van Der Perren Géraldine Gelders Nikol Shakhbazyan Francesca Macchi Chris Van Den Haute Veerle Baekelandt Google Scholar Anke Van Der Perren Géraldine Gelders Nikol Shakhbazyan Francesca Macchi Chris Van Den Haute Veerle Baekelandt PubMed Anke Van Der Perren Géraldine Gelders Nikol Shakhbazyan Francesca Macchi Chris Van Den Haute Veerle Baekelandt Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page." @default.
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• W2912622904 title "In vivo characterization of different alpha-synuclein variants" @default.
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