Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/117741
Title: Maillard proteomics : opening new pages
Author(s): Soboleva, Alena
Schmidt, Rico
Vikhnina, Maria
Grishina, Tatiana
Frolov, AndrejLook up in the Integrated Authority File of the German National Library
Issue Date: 2017
Type: Article
Language: English
Abstract: Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress.
URI: https://opendata.uni-halle.de//handle/1981185920/119701
http://dx.doi.org/10.25673/117741
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
Journal Title: International journal of molecular sciences
Publisher: Molecular Diversity Preservation International
Publisher Place: Basel
Volume: 18
Issue: 12
Original Publication: 10.3390/ijms18122677
Page Start: 1
Page End: 45
Appears in Collections:Open Access Publikationen der MLU

Files in This Item:
File Description SizeFormat 
ijms-18-02677.pdf3.69 MBAdobe PDFThumbnail
View/Open