溶酶体自噬途径降解α-synuclein蛋白作用研究  

Role of lysosomal autophagy pathway in α-synuclein degradation

作　　者：王润青[1] 赵杰[1] 张晓曼[2] 刘威[1] 赵松耀[1] 秦晓明[1] 赵美英[1] 孟宏音[1] 

机构地区：[1]郑州市中心医院神经内科,郑州450007 [2]郑州市第一人民医院神经内科,郑州450006

出　　处：《中国实用神经疾病杂志》2010年第24期3-5,共3页Chinese Journal of Practical Nervous Diseases

基　　金：郑科计(2009)15号;项目编号:096SYJH33116

摘　　要：目的探讨α-synuclein蛋白细胞内溶酶体途径降解机制。方法用神经生长因子NGF诱导分化PC12细胞作为研究多巴胺能神经元的细胞载体,应用鱼藤酮处理PC12细胞建立α-synuclein蛋白细胞模型。使用溶酶体途径降解抑制剂E64处理神经元样分化的PC12细胞,应用免疫荧光双标方法观察PC12细胞内硫黄素S、α-synuclein蛋白阳性聚集包涵体形成情况,比较各组的差异。结果用E64处理鱼藤酮预处理过的PC12细胞后α-synuclein蛋白聚集且较多包涵体形成(15.36±0.85)%,与对照组相比差异有统计学意义(P<0.05)。结论溶酶体自噬途径可能在α-synuclein蛋白降解、聚集和多巴胺神经元死亡过程中发挥重要作用。Objective To investigate the pathway and mechanism of α-synuclein in lysosomal degradation path way. Methods PC12 cells as dopaminergic neurons, differentiated by nerve growth factor. PCI2 cell5 were treated by rotenone to make α-synuclein model. Then PCI2 cells were treated by lysosomal inhibitors E64. Protein aggregation was detected by the double labeling of thioflavine S and α-synuelein for imunofluoreseenee staining. Results E64 induced α-synuelein protein aggre gate and lead to the formation of eosinophilic intracytoplasmic inclusions, which was immunoreactive to α-synuclein and thioflavine S with （ 15.36 ± 0. 85 ）%（ P〈 0. 05 ）. Conclusion The autophagy pathway plays an important role in the metabolism of a-synuclein, inclusions formation and dopaminergic neuro- nal death.

关 键 词：溶酶体 α—synuclein 帕金森病 自噬 

分 类 号：R-33[医药卫生]