Oueslati Abid, Ximerakis Methodios, Vekrellis Kostas
Centre de Recherche du Centre Hospitalier de Québec, Axe Neuroscience et Département de Médecine Moléculaire de l'Université Laval, Québec G1V4G2, Canada.
Center for Neurosciences, Biomedical Research Foundation, Academy of Athens, Athens 11526, Greece.
Exp Neurobiol. 2014 Dec;23(4):324-36. doi: 10.5607/en.2014.23.4.324. Epub 2014 Dec 12.
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.
越来越多的证据表明，细胞间传播和致病性淀粉样蛋白的自我传播在几种神经退行性疾病的发生和发展中起着核心作用。最近有报道称，这种“类朊病毒”假说是针对α-突触核蛋白的，α-突触核蛋白是一种与帕金森病（PD）及相关疾病发病机制有关的突触前蛋白。这篇综述总结了关于α-突触核蛋白类朊病毒样传播的最新发现，重点关注其传播、种子形成和降解，并讨论了一些有待探索的关键问题。了解α-突触核蛋白如何离开细胞并从一个脑区传播到另一个脑区，将有助于开发治疗PD的新治疗策略，旨在减缓或阻止疾病进展。
