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Exp Neurobiol 2014; 23(4): 324-336
Published online December 31, 2014
© The Korean Society for Brain and Neural Sciences
Abid Oueslati1#*, Methodios Ximerakis2# and Kostas Vekrellis2
1Centre de Recherche du Centre Hospitalier de Québec, Axe Neuroscience et Département de Médecine Moléculaire
de l'Université Laval, Québec G1V4G2, Canada, 2Center for Neurosciences, Biomedical Research Foundation,
Academy of Athens, Athens 11526, Greece
Correspondence to: #A. O. and M. X. contributed equally to this work.
*To whom correspondence should be addressed.
TEL: 14185254444, Ext 49119, FAX: 14186542125
Converging lines of evidence suggest that cell-to-cell transmission and the self-propagation of pathogenic amyloidogenic proteins play a central role in the initiation and the progression of several neurodegenerative disorders. This "prion-like" hypothesis has been recently reported for α-synuclein, a presynaptic protein implicated in the pathogenesis of Parkinson's disease (PD) and related disorders. This review summarizes recent findings on α-synuclein prion-like propagation, focusing on its transmission, seeding and degradation and discusses some key questions that remain to be explored. Understanding how α-synuclein exits cells and propagates from one brain region to another will lead to the development of new therapeutic strategies for the treatment of PD, aiming at slowing or stopping the disease progression.
Keywords: secretion, seeding, turnover, extracellular proteins, disease propagation