α-突触核蛋白促进原代神经元及转基因小鼠神经细胞表面NMDA受体的内在化  

Alpha-synuclein promotes internalization of surface N-methyl-D-aspartate receptors in primary neurons and transgenic mice

作　　者：陈予东[1] 杨巍巍[1] 李昕[1] 王鹏[1] 李旭冉[1] 于顺[1] 

机构地区：[1]首都医科大学宣武医院神经生物学研究室北京市老年病医疗研究中心分子诊断实验室教育部神经变性病重点实验室,北京100053

出　　处：《首都医科大学学报》2014年第5期596-600,共5页Journal of Capital Medical University

基　　金：国家重点基础研究发展计划(2011CB504101);国家自然科学基金(81071014;81371200);国家科技支撑计划课题(2012BAI10B03);首都卫生发展科研专项课题(2011-4001-01);北京市自然科学基金(7122035)~~

摘　　要：目的在原代培养神经元及转基因动物水平上,研究α-突触核蛋白(α-synuclein,α-Syn)对神经细胞表面N-甲基-D-天门冬氨酸(N-methyl-D-aspartate,NMDA)受体的影响及其机制。方法免疫荧光标记法和Western blotting测定NMDA受体(NMDA receptor,NMDAR)和Rab5B质量分数。Rab5B反义寡核苷酸抑制Rab5B基因表达。以原代培养神经细胞及转基因小鼠为模型,观察α-Syn蛋白增多对细胞膜NMDAR质量分数的影响以及Rab5B的作用。结果在细胞及动物水平,α-Syn明显上调Rab5B表达,促进NMDAR的内在化。而抑制Rab5B表达可消除α-Syn致NMDAR的内在化。结论α-Syn通过上调Rab5B的表达促进NMDAR的内在化。Objective To investigate the effect of α-synuclein（ α-Syn） on surface N-methyl-D-aspartate（ NMDA） receptors on the primary neurons and transgenic mice. Methods Immunofluorescent labeling and Western blotting analysis were used to measure the alterations of NMDA receptors and Rab5 B proteins. Rab5 B antisense oligonucleotides were applied to suppress Rab5 B expression. The primary neurons and transgenic mice were used as models to observe the effect of α-Syn on the surface NMDAR expression. Results α-Syn triggered a significant decrease of the surface NMDAR expression. This effect of α-Syn was blocked by suppression of Rab5 B expression. Conclusion α-Syn promotes internalization of surface NMDA receptors by increasing Rab5 B expression.

关 键 词：Α-突触核蛋白 转基因小鼠 原代神经元 N-甲基-D-天门冬氨酸 内在化 

分 类 号：Q189[生物学—神经生物学]