Journal
MASS SPECTROMETRY REVIEWS
Volume 33, Issue 1, Pages 49-77Publisher
WILEY
DOI: 10.1002/mas.21378
Keywords
glycation; glycoxidation; proteomics; mass spectrometry
Categories
Funding
- Italian MEF (Innovazione e sviluppo del Mezzogiorno-Conoscenze Integrate per Sostenibilita ed Innovazione del Made in Italy Agroalimentare-Legge) [191/2009]
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The Maillard reaction includes a complex network of processes affecting food and biopharmaceutical products; it also occurs in living organisms and has been strictly related to cell aging, to the pathogenesis of several (chronic) diseases, such as diabetes, uremia, cataract, liver cirrhosis and various neurodegenerative pathologies, as well as to peritoneal dialysis treatment. Dozens of compounds are involved in this process, among which a number of protein-adducted derivatives that have been simplistically defined as early, intermediate and advanced glycation end-products. In the last decade, various bottom-up proteomic approaches have been successfully used for the identification of glycation/glycoxidation protein targets as well as for the characterization of the corresponding adducts, including assignment of the modified amino acids. This article provides an updated overview of the mass spectrometry-based procedures developed to this purpose, emphasizing their partial limits with respect to current proteomic approaches for the analysis of other post-translational modifications. These limitations are mainly related to the concomitant sheer diversity, chemical complexity, and variable abundance of the various derivatives to be characterized. Some challenges to scientists are finally proposed for future proteomic investigations to solve main drawbacks in this research field. (c) 2013 Wiley Periodicals, Inc. Mass Spec Rev 33: 49-77, 2014.
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