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目的研究α-突触核蛋白(α-Syn)和氧化应激的相互作用关系。方法用200μmol/LH2O2处理多巴胺能MES23·5神经细胞作为氧化应激的细胞模型。采用免疫荧光、硫磺素S组织化学染色和免疫印迹技术检测细胞氧化应激反应中α-突触核蛋白的表达状态和亚细胞定位。结果200μmol/LH2O2处理可诱导α-突触核蛋白从细胞浆转位到细胞核内,而且转位到细胞核内的是约10kD的α-突触核蛋白C-末端片段,而存在于细胞浆内的是完整的α-突触核蛋白。硫磺素S染色显示,转位到细胞核内的α-突触核蛋白C-末端片段呈非聚集状态。结论氧化应激可诱导多巴胺能MES23·5神经细胞α-突触核蛋白C末端约10kD的片段核转位。
Objective To study the interaction between α-synuclein (α-Syn) and oxidative stress. Methods Dopaminergic MES23.5 cells were treated with 200μmol / L H2O2 as cell model of oxidative stress. Immunofluorescence, Thioflavin S histochemical staining and Western blotting were used to detect the expression and subcellular location of α-synuclein in cell oxidative stress. Results Treatment with 200μmol / LH 2 O 2 induced the translocation of α-synuclein from the cytoplasm into the nucleus and translocated to the nucleus about 10kD of α-synuclein C-terminal fragment, which was present in the cytoplasm Is the complete α-synuclein. Thioflavin S staining showed that the C-terminal fragment of [alpha] -synuclein translocated into the nucleus was non-aggregated. Conclusion Oxidative stress induces nuclear translocation of about 10 kD at the C-terminus of α-synuclein in dopaminergic neuronal cells.