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目的:研究儿茶酚异喹啉类物质1-甲基-6,7-二羟基-1,2,3,4-四氢异喹啉(salsolinol,Sal)对帕金森病关键蛋白α突触核蛋白(α-syulcein,α-syn)纤维化程度的影响。方法:将重组人源α-Syn蛋白与不同浓度的Sal共同孵育,通过Th T染色对α-Syn成纤维状况进行监测。同时,利用扫描电镜和激光共聚焦显微镜观察α-Syn与Sal共孵育后的形态变化。结果结论:实验结果表明Sal具有将α-Syn稳定在寡聚体或者原纤维状态的能力,且呈浓度依赖性,Sal浓度越大,α-Syn纤维化进程越缓慢。这一发现为进一步研究α-Syn和儿茶酚异喹啉类物质在PD发生和发展过程中起到的作用提供了一定的实验依据。
AIM: To investigate the effect of salsolinol (Sal), a catechol isoquinoline substance, on the synapse of Parkinson’s disease Effect of α-synuclein (α-syn) fibrosis. Methods: Recombinant human α-Syn protein was incubated with different concentrations of Sal and the status of α-Syn fibrils was monitored by Th T staining. At the same time, morphological changes of α-Syn and Sal were observed by scanning electron microscopy and laser confocal microscopy. Results Conclusion: The experimental results show that Sal has the ability to stabilize α-Syn in oligomers or fibrils in a concentration-dependent manner. The greater Sal concentration, the slower the progress of α-Syn fibrosis. This finding provides some experimental evidence for further study of the role of α-Syn and catechol isoquinolines in the occurrence and development of PD.