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BioMed Research International
Volume 2015, Article ID 172018, 7 pages
Review Article

Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?

Department of Physical Chemistry, Faculty of Pharmacy, University of Barcelona, and Institute of Nanoscience and Nanotechnology of the University of Barcelona (IN2UB), Avenue Joan XXIII 27-31, Barcelona, 08028 Catalonia, Spain

Received 22 May 2014; Accepted 18 July 2014

Academic Editor: Beom S. Jeon

Copyright © 2015 Maria Antònia Busquets et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.