目的研究帕金森病(PD)患者血清对外源性α-突触核蛋白(α-Synuclein,α-Syn)寡聚体形成的影响,初步分析血清促进α-Syn寡聚体形成的机制。方法将重组人α-Syn加入PD患者和对照组血清中,37℃振荡孵育,用免疫印迹方法鉴定α-Syn寡聚体的形成情况,用ELISA分析α-Syn寡聚体的形成量。结果α-Syn在血清中振荡孵育后主要形成二聚体和十四聚体。与对照组血清相比较,PD患者血清具有促进α-Syn寡聚体形成的作用。在血清中加入还原性谷胱甘肽可明显减弱PD患者血清促进α-Syn寡聚体形成的作用。结论PD患者血清促进α-Syn寡聚体的形成,其机制可能与α-Syn的氧化修饰有关。
Objective To study the oligomerization of α-Synuclein (ct-Syn) in the sera of patients with Parkinson' s disease (PD) and the potential mechanism for this oligomerization. Methods Recombinant α-Syn was incubated in the sera of PD patients and of normal subjects. Immunoblot analysis was used to identify the formation of α-Syn oligomers. A special ELISA method was used to evaluate the amount of α-Syn oligomers in PD and control sera. Results The oligomeric forms of α-Syn formed in the serum were dimers, trimers, tetramers, and fourteen-polymers, Compared with control sera, the sera of PD patients significantly enhanced the oligomerization of α-Syn. Reduced glutathione significantly decreased the amount of α-Syn oligomers in the sera of PD patients. Conclusion α-Syn can form different forms of oligomers in the serum. Compared with control, sera from PD patients enhance the oligomerization of α-Syn, which may be mediated by oxidization of α-Syn.