Niwa Toshimitsu
Department of Clinical Preventive Medicine, Nagoya University Hospital, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8560, Japan.
Mass Spectrom Rev. 2006 Sep-Oct;25(5):713-23. doi: 10.1002/mas.20089.
The structural elucidation of advanced glycation end-product (AGE)-modified proteins and quantitative analysis of free AGEs have been successfully performed, by use of mass spectrometry (MS) in plasma and tissues of patients with AGE-related diseases, such as diabetes mellitus, uremia, cataract, and liver cirrhosis. Matrix-assisted laser desorption/ionization (MALDI)-MS made it possible to directly analyze the AGE-modified proteins such as albumin and IgG. However, because the direct structural analysis of intact AGE-modified proteins is often not easy due to the formation of broad and poorly resolved peaks, peptide mapping after enzymatic hydrolysis was introduced into the analysis of AGE-modified proteins and the site-specific analysis of defined AGEs by MALDI-MS. Liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS) has been employed not only for the structural elucidation of enzymatically hydrolyzed AGEs-modified peptides but also for simultaneous quantification of free AGEs in plasma and tissues of patients. Based on many studies that use MS for the analysis of AGEs, there is no doubt as to the important role of protein-linked AGEs in several diseases.
通过质谱（MS）技术，已成功实现了对晚期糖基化终产物（AGE）修饰蛋白的结构解析以及游离AGEs的定量分析，该技术应用于患有AGE相关疾病（如糖尿病、尿毒症、白内障和肝硬化）患者的血浆和组织中。基质辅助激光解吸/电离（MALDI）-MS使得直接分析如白蛋白和IgG等AGE修饰蛋白成为可能。然而，由于完整AGE修饰蛋白的直接结构分析往往因形成宽峰且分辨率差而不易进行，因此酶解后的肽图谱分析被引入到AGE修饰蛋白的分析以及通过MALDI-MS对特定AGEs进行位点特异性分析中。液相色谱/电喷雾电离质谱（LC/ESI-MS）不仅用于酶解AGE修饰肽的结构解析，还用于同时定量患者血浆和组织中的游离AGEs。基于许多使用MS分析AGEs的研究，蛋白质连接的AGEs在多种疾病中的重要作用毋庸置疑。
