Microbiology and Virology Unit, Department of Biomedical Sciences, University of Cagliari, 09042 Cagliari, Italy.
Int J Mol Sci. 2021 Jul 27;22(15):8022. doi: 10.3390/ijms22158022.
The principal pathogenic event in Parkinson's disease is characterized by the conformational change of α-synuclein, which form pathological aggregates of misfolded proteins, and then accumulate in intraneuronal inclusions causing dopaminergic neuronal loss in specific brain regions. Over the last few years, a revolutionary theory has correlated Parkinson's disease and other neurological disorders with a shared mechanism, which determines α-synuclein aggregates and progresses in the host in a prion-like manner. In this review, the main characteristics shared between α-synuclein and prion protein are compared and the cofactors that influence the remodeling of native protein structures and pathogenetic mechanisms underlying neurodegeneration are discussed.
帕金森病的主要致病事件的特征是α-突触核蛋白的构象改变，导致错误折叠的蛋白质形成病理性聚集物，然后在神经元内积累，导致特定脑区的多巴胺能神经元丧失。在过去的几年中，一个革命性的理论将帕金森病和其他神经退行性疾病与一种共同的机制联系起来，这种机制决定了朊病毒样的α-突触核蛋白聚集和在宿主中的进展。在这篇综述中，比较了α-突触核蛋白和朊病毒蛋白之间的主要共同特征，并讨论了影响天然蛋白质结构重塑和神经退行性变发病机制的协同因子。
