摘要
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 Growing evidence suggests that oxidative stress is involved in the neuronal degeneration and can promote the aggregation of α-synuclein. However, the role of α-synuclein under physiologic and pathological conditions remains poorly understood. We set to study the relationship between α-synuclein and oxidative stress. Methods Dopaminergic neuronal cell line was treated with 200 μmol/L H2O2. Immunofluorescence, Thioflavine S histochemistry and Western blot analysis were used to investigate the status, expression and location in neuronal cells. Results Our study shows that the 200 μmol/L H2O2 treatment can induce the translocation of α-synuclein from cytoplasm to nuclei in dopaminergic MES23.5 ceils. Further study indicates that the protein translocated into nucleus is a C-terminal fragment of α-synuclein and the size of the fragment is about 10 kD. Conclusion Our data indicate that oxidative stress can induce the intranuclear accumulation of the C terminal fragment of α- synuclein in dopaminergic neurons, but further study is needed to reveal the exact role of the translocation of C-terminus of α- synuclein in response to oxidative stress in dopaminergic neuron.
出处
《解剖学报》
CAS
CSCD
北大核心
2005年第4期337-341,共5页
Acta Anatomica Sinica
基金
国家自然科学基金(30371574
30430280)
国家973重点基础研究发展规划项目(001CB510104)
北京市卫生局重点学科基金(卫科扶字12号
1998)资助
