Nikoletopoulou Vassiliki, Tavernarakis Nektarios
Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Hellas, Greece.
Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Hellas, Greece; Department of Basic Sciences, Faculty of Medicine, University of Crete Heraklion 71110, Crete, Greece.
Neurosci Lett. 2018 Jan 10;663:66-71. doi: 10.1016/j.neulet.2017.08.006. Epub 2017 Aug 2.
Proteinopathies constitute a diverse group of devastating neurodegenerative disorders, characterized by aberrant aggregation of specific proteins within neurons and in the brain parenchyma. Parkinson's disease (PD) is among the most common proteinopathies, caused by the accumulation of different species of α-synuclein and the formation of protein inclusions known as Lewy bodies. Although several mutations in the α-synuclein gene have been linked to PD, the mechanisms mediating the aggregation and toxicity of α-synuclein are not fully understood. Here, we review recent evidence that highlight an intricate interplay between α-synuclein and ionostasis, focusing on the PMR1 pump, a Golgi resident Ca/Mn P-type ATPase, which plays a pivotal role in regulating the intracellular levels of calcium and manganese ions.
蛋白质病是一组多样的毁灭性神经退行性疾病，其特征是特定蛋白质在神经元和脑实质内异常聚集。帕金森病（PD）是最常见的蛋白质病之一，由不同种类的α-突触核蛋白积累以及称为路易小体的蛋白质内含物形成所致。尽管α-突触核蛋白基因中的几个突变已与PD相关联，但介导α-突触核蛋白聚集和毒性的机制尚未完全了解。在此，我们综述了最近的证据，这些证据突出了α-突触核蛋白与离子稳态之间的复杂相互作用，重点关注PMR1泵，一种驻留在高尔基体的Ca/Mn P型ATP酶，它在调节细胞内钙和锰离子水平方面起着关键作用。
