Glycation of Plant Proteins: Regulatory Roles and Interplay with Sugar Signalling?

Glycation can be defined as an array of non-enzymatic post-translational modifications of proteins formed by their interaction with reducing carbohydrates and carbonyl products of their degradation. Initial steps of this process rely on reducing sugars and result in the formation of early glycation...

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Published in: International journal of molecular sciences Vol. 20; no. 9; p. 2366
Main Authors: Shumilina, Julia, Kusnetsova, Alena, Tsarev, Alexander, Janse van Rensburg, Henry C, Medvedev, Sergei, Demidchik, Vadim, Van den Ende, Wim, Frolov, Andrej
Format: Journal Article
Language: English
Published: Switzerland MDPI 05-13-2019
MDPI AG
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Summary: Glycation can be defined as an array of non-enzymatic post-translational modifications of proteins formed by their interaction with reducing carbohydrates and carbonyl products of their degradation. Initial steps of this process rely on reducing sugars and result in the formation of early glycation products-Amadori and Heyns compounds via Schiff base intermediates, whereas their oxidative degradation or reactions of proteins with α-dicarbonyl compounds yield a heterogeneous group of advanced glycation end products (AGEs). These compounds accompany thermal processing of protein-containing foods and are known to impact on ageing, pathogenesis of diabetes mellitus and Alzheimer's disease in mammals. Surprisingly, despite high tissue carbohydrate contents, glycation of plant proteins was addressed only recently and its physiological role in plants is still not understood. Therefore, here we summarize and critically discuss the first steps done in the field of plant protein glycation during the last decade. We consider the main features of plant glycated proteome and discuss them in the context of characteristic metabolic background. Further, we address the possible role of protein glycation in plants and consider its probable contribution to protein degradation, methylglyoxal and sugar signalling, as well as interplay with antioxidant defense.
ISSN: 1422-0067
1422-0067
DOI: 10.3390/ijms20092366