ALS小鼠脊髓组织GFAP蛋白赖氨酸的乙酰化修饰  

Glial fibrillary acid protein lysine acetylated modification in ALS mouse

作　　者：李俊强[1] 郭继生 王小岳[1] 王道光[1] 赵作辉[2] 杨静华[1] 

机构地区：[1]山东大学医学院癌症研究中心,济南250012 [2]山东大学附属省立医院泌尿外科,济南250021

出　　处：《山东大学学报（医学版）》2013年第10期15-18,共4页Journal of Shandong University:Health Sciences

摘　　要：目的探讨肌萎缩脊髓硬化症(ALS)模型小鼠脊髓组织胶质纤维酸性蛋白(GFAP)中赖氨酸的乙酰化修饰。方法对4个月左右的ALS模型小鼠进行麻醉处死,提取小鼠脊髓组织总蛋白,通过GFAP抗体和乙酰化抗体,运用免疫沉淀和免疫蛋白印迹技术鉴定GFAP蛋白的表达与GFAP蛋白赖氨酸的乙酰化修饰,通过液相二级质谱连用(LC-MS/MS)检测ALS模型小鼠脊髓组织中GFAP赖氨酸的乙酰化修饰位点。结果免疫沉淀和免疫蛋白印迹方法发现ALS模型小鼠脊髓组织中GFAP蛋白存在赖氨酸乙酰化修饰;LC-MS/MS发现GFAP的394位和402位赖氨酸位点发生乙酰化修饰。结论 ALS小鼠模型脊髓组织中,GFAP的赖氨酸位点能被乙酰化修饰,该修饰可能参与了ALS的发生。Objective To investigate glial fibrillary acidic protein （GFAP） lysine acetylated modification in the spinal cord tissue of amyotrophic lateral sclerosis （ALS） model mouse. Methods After 3 ALS mice about 4 months old were sacrificed with anesthesia, total protein was extracted by RIPA lysis buffer; GFAP and Pan-AC protein expression were identified by immunoprecipitation and western blotting. Then IP-purified GFAP protein was analyzed using liquid chromatography-tandem mass spectrometry （LC-MS/MS）. Results IP-purified GFAP protein from ALS mice was acetylated in lysine residues, and the GFAP 394 and 402 lysine residues were confirmed by LC-MS/MS. Conclusion The lysine residue of GFAP can be modified by acetylation, which may participate in the occurrence of ALS.

关 键 词：胶质纤维酸性蛋白 乙酰化修饰 肌萎缩脊髓硬化症 液相二级质谱连用 

分 类 号：R34[医药卫生—基础医学]