Abstract
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.
Highlights
Protein glycation is usually referred to as a non-enzymatic reaction of protein lysyl and arginyl residues with reducing carbohydrates and carbonyl products of their oxidative and non-oxidative degradation [1]
Despite high contents of such lysine advanced glycation end products (AGEs) as Nε-(carboxymethyl)- and -(carboxyethyl)lysine (CML and CEL), only 21.3% of the total lysyl residue numbers were modified with Amadori and Heyns moieties—early glycation products
We demonstrated that drought contributes to accumulation of AGEs in Arabidopsis thaliana leaves [67]
Summary
Protein glycation is usually referred to as a non-enzymatic reaction of protein lysyl and arginyl residues with reducing carbohydrates and carbonyl products of their oxidative and non-oxidative degradation [1]. The glycation process, initially believed to be acting in a rather random and non-specific way, usually involves lysine and arginine [2,3] and, to a lesser extent, cysteine and tryptophan residues [4]. These reactions, known as Maillard reaction of proteins, are strongly enhanced by temperature increases [5]. Despite significant progress in the evaluation of formation pathways, structural analysis and physiological effects of dietary and clinically relevant AGEs in humans, animals and yeast [45], for plants, this information is still mostly unknown. We discuss possible physiological roles of plant protein glycation in the context of future perspectives and new directions in the field of plant glycation research
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
