Simona Arena, Anna Maria Salzano, Giovanni Renzone, and Chiara D'Ambrosio contributed equally to this work.
Non-enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies
Article first published online: 24 SEP 2013
© 2013 Wiley Periodicals, Inc.
Mass Spectrometry Reviews
Special Issue: Special Issue on Redox Proteomics Part 1
Volume 33, Issue 1, pages 49–77, January/February 2014
How to Cite
Arena, S., Salzano, A. M., Renzone, G., D'Ambrosio, C. and Scaloni, A. (2014), Non-enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies. Mass Spectrom. Rev., 33: 49–77. doi: 10.1002/mas.21378
- Issue published online: 27 NOV 2013
- Article first published online: 24 SEP 2013
- Manuscript Revised: 9 MAR 2013
- Manuscript Accepted: 9 MAR 2013
- Manuscript Received: 10 DEC 2012
- Italian MEF (Innovazione e sviluppo del Mezzogiorno-Conoscenze Integrate per Sostenibilità ed Innovazione del Made in Italy Agroalimentare-Legge n.191/2009)
- mass spectrometry
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. © 2013 Wiley Periodicals, Inc. Mass Spec Rev 33: 49–77, 2014.