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J Biol Chem. 2017 Sep 22;292(38):15758-15776. doi: 10.1074/jbc.M117.794537. Epub 2017 Jun 13.

Global proteomic analysis of advanced glycation end products in the Arabidopsis proteome provides evidence for age-related glycation hot spots.

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From the Departments of Bioorganic Chemistry and
the Faculty of Chemistry and Mineralogy, Universität Leipzig, D-04103 Leipzig, Germany.
the Departments of Plant Physiology and Biochemistry and.
From the Departments of Bioorganic Chemistry and.
Biochemistry, Faculty of Biology, Saint-Petersburg State University, 199034 Saint Petersburg, Russia.
the Institute of Pharmacy, Martin-Luther Universität Halle-Wittenberg, D-06099 Halle (Saale), Germany, and.
the Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), D-06466 Stadt Seeland, Germany.
Cell and Metabolic Biology, Leibniz Institute of Plant Biochemistry (IPB), D-06120 Halle (Saale), Germany.
From the Departments of Bioorganic Chemistry and


Glycation is a post-translational modification resulting from the interaction of protein amino and guanidino groups with carbonyl compounds. Initially, amino groups react with reducing carbohydrates, yielding Amadori and Heyns compounds. Their further degradation results in formation of advanced glycation end products (AGEs), also originating from α-dicarbonyl products of monosaccharide autoxidation and primary metabolism. In mammals, AGEs are continuously formed during the life of the organism, accumulate in tissues, are well-known markers of aging, and impact age-related tissue stiffening and atherosclerotic changes. However, the role of AGEs in age-related molecular alterations in plants is still unknown. To fill this gap, we present here a comprehensive study of the age-related changes in the Arabidopsis thaliana glycated proteome, including the proteins affected and specific glycation sites therein. We also consider the qualitative and quantitative changes in glycation patterns in terms of the general metabolic background, pathways of AGE formation, and the status of plant anti-oxidative/anti-glycative defense. Although the patterns of glycated proteins were only minimally influenced by plant age, the abundance of 96 AGE sites in 71 proteins was significantly affected in an age-dependent manner and clearly indicated the existence of age-related glycation hot spots in the plant proteome. Homology modeling revealed glutamyl and aspartyl residues in close proximity (less than 5 Å) to these sites in three aging-specific and eight differentially glycated proteins, four of which were modified in catalytic domains. Thus, the sites of glycation hot spots might be defined by protein structure that indicates, at least partly, site-specific character of glycation.


Arabidopsis thaliana; advanced glycation end products (AGEs); aging; glycation; homology modeling; hot spots of glycation; metabolomics; oxidative stress; post-translational modification (PTM); proteomics

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