Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/191006
Title: | Could alpha-Synuclein Amyloid-like aggregates trigger a prionic neuronal invasion? |
Author: | Espargaró Colomé, Alba Busquets i Viñas, Ma. Antonia Estelrich i Latràs, Joan Sabaté Lagunas, Raimon |
Keywords: | Amiloïdosi Malaltia de Parkinson Proteïnes Amyloidosis Parkinson's disease Proteins |
Issue Date: | 2015 |
Publisher: | Hindawi |
Abstract: | Parkinson's disease (PD), a progressive neurodegenerative disease primarily affecting voluntary and controlled movement, is characterized by abnormal accumulations of 𝛼-synuclein (𝛼-syn) in intraneuronal Lewy bodies. In the last years, the increased number of evidences from both the in vitro and in vivo studies has shown the ability of 𝛼-syn to misfold in amyloid conformations and to spread via neuron-to-neuron transmission, suggesting a prion-like behaviour. However, in contrast to prion protein (PrP), 𝛼-syn transmission is far from neuronal invasion. The high neuronal toxicity of both mature fibres and oligomeric species, as well as the intracellular localization of the protein and the difficulty to be secreted, could be key factors impeding the prion ability of 𝛼-syn aggregates. |
Note: | Reproducció del document publicat a: https://doi.org/10.1155/2015/172018 |
It is part of: | BioMed Research International, 2015, vol. 2015, p. 7 pp |
URI: | http://hdl.handle.net/2445/191006 |
Related resource: | https://doi.org/10.1155/2015/172018 |
ISSN: | 2314-6133 |
Appears in Collections: | Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
646257.pdf | 1.17 MB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License