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α-sylluclein是一种天然非折叠可溶性蛋白。目前发现它与许多神经功能障碍性及退行性中枢系统疾病密切相关,典型之一就是帕金森病(Parkjnson disea8e,PD)。各种复杂因素,都可导致α-syrIuclein错误折叠并改变其正常的功能。在多巴胺(dop啪ine,DA)能体系中,这一改变可最终使得多巴胺能神经细胞数目减少而导致PD。α-synuclein功能不全是PD中普遍存在的一个特征,该物质是如何产生神经细胞毒性作用的机制涉及多个方面。正是因为上述错综复杂的机制使得对α-sylluclein与PD的研究进展缓慢。本文就α-sylluclein基因、α-synuclein蛋白的聚集及其在PD发病机制中作用等方面的研究做一综述。
Alpha-sylluclein is a natural non-folding soluble protein. It is found to be closely associated with many neurodevelopmental and degenerative central nervous system diseases, one of which is Parkinson’s disease (PD). Various complexities can cause alpha-syrIuclein to misfold and alter its normal function. In dopamine (DA) energy system, this change can eventually lead to a decrease in the number of dopaminergic neurons resulting in PD. α-synuclein dysfunction is a common feature of PD, the mechanism of how the substance produces neurotoxicity involves a number of aspects. It is because of the intricacies of these mechanisms that the research on a-sylluclein and PD has been slow. This review summarizes the studies on the aggregation of α-sylluclein and α-synuclein and their roles in the pathogenesis of PD.