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Mass spectrometry for the study of protein glycation in disease

✍ Scribed by Toshimitsu Niwa

Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
192 KB
Volume
25
Category
Article
ISSN
0277-7037

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✦ Synopsis

Abstract

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. © 2006 Wiley‐Liss, Inc.

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