蛋白质组学方法研究葡萄糖对人血清白蛋白的修饰作用  

Study on Human Serum Albumin Modified by Glucose with Proteomic Technique

作　　者：李浡[1] 彭博[1] 胡定煜[1] 邓玉林[1] 

机构地区：[1]北京理工大学生命科学与技术学院,北京100081

出　　处：《化学通报》2008年第6期425-429,共5页Chemistry

基　　金：国家自然科学基金项目(20435020和20275005)资助

摘　　要：晚期糖基化终产物是一组由不同种类物质组成的复杂混合物,其与很多疾病相关,如糖尿病及其并发症、肾衰竭以及与老龄化相关等疾病。人血清白蛋白(HSA)是血清中含量最丰富的蛋白质。葡萄糖对血液中的HSA和其它蛋白质的结构具有修饰作用,发生糖基化反应。本文利用LC/MS联用技术,通过蛋白质组学方法,寻找差异肽段,研究糖基化HSA的修饰位点以及修饰种类,对于进一步寻找临床诊断糖尿病以及与老龄化相关疾病的肽类生物标志物具有重要意义。Advanced glycation end products （AGEs） are a heterogeneous group of complex compounds which may play a role in the pathogenesis of chronic complications associated with diabetes complications, renal failure and aging. Human Serum Albumin （HSA） is the most abundant protein in blood serum. Glucose has the ability to modify HSA and other proteins through glycation. This study was carried out on glycated HSA which was analyzed by LC/MS with the aim of identifying specific peptides. Analysis of the LC/MS data showed that there were differences between peptides of glycated and normal HSA. Modification sites of glycated peptides were also studied. These typical peptides were considered as biomarkers for clinical diagnose of diabetes and aging.

关 键 词：糖基化反应 人血清白 蛋白LC/MS 修饰位点 

分 类 号：R341[医药卫生—基础医学]