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Mass spectrometry for the study of protein glycation in disease
Author(s) -
Niwa Toshimitsu
Publication year - 2006
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.20089
Subject(s) - chemistry , glycation , mass spectrometry , chromatography , electrospray ionization , matrix assisted laser desorption/ionization , blood proteins , advanced glycation end product , protein mass spectrometry , biochemistry , desorption , organic chemistry , receptor , adsorption
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.