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Plant Protein Glycation

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Plant Sciences".

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 8989

Special Issue Editor


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Guest Editor
1. Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, 06120 Halle, Germany
2. Department of Biochemistry, St. Petersburg State University, 199034 St. Petersburg, Russia
Interests: bioanalytical chemistry; mass spectrometry; chromatography; proteomics; metabolomics; food chemistry; nutrition; metabolic diseases; biomarkers; Maillard reaction; glycation; environmental stress; stress tolerance in plants; plant-derived natural products as anti-inflammatory and neuroprotective drugs
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Special Issue Information

Dear Colleagues,

Protein glycation is a ubiquitous post-translational modification characterized by the interaction of reduced carbohydrates or dicarbonyl products from their degradation with amino and guanidino functionalities of a polypeptide chain. The reaction of reducing sugars, aldoses, and ketoses, readily yields corresponding keto- and aldimines, known as Amadori and Heyns compounds, respectively. Their subsequent degradation and direct interaction with α-dicarbonyl compounds ultimately result in the formation of advanced glycation end products (AGEs)—a wide group of structurally diverse compounds with distinct pro-inflammatory effects in mammals. The formation of AGEs affects the development of metabolic pathologies (such as diabetes mellitus and Alzheimer disease) and accompanies the thermal processing of foods. Recently, the formation of AGEs was demonstrated also in plants in association with plant tissues ageing and response to environmental stress, like drought, high temperature, or intense light. Moreover, protein glycation is known as a marker of seed maturation and of the development of legume–rhizobial symbiosis. However, the effects of AGEs in planta and their biological role still remain unknown.

Thus, the scope of this Special Issue will cover all plant-related aspects of plant protein glycation. These aspects can be disclosed in original research papers or critical reviews (both in short and comprehensive format). Thereby, AGE formation can be addressed in vivo in different models and crop plants, including seeds, targeting both structural and functional (physiological) aspects. On the other hand, the glycation of plant proteins can be considered in the context of food chemistry, i.e., during thermal processing of plant-derived protein-rich foods. Works addressing the responses of animal and human cells and/or organisms to natural or food-derived plant protein glycation products (i.e., nutritional aspect) are also welcomed. To summarize, the main idea of this Special Issue is to present different views of the plant glycation phenomenon, covering biological, physiological, biochemical, chemical, nutritional, and food aspects of the Maillard reaction in plants. Thus, this Special Issue will be of interest to a broad community of biologists, biochemists, plant physiologists, chemists, and medical scientists.

Dr. Andrej Frolov
Guest Editor

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Keywords

  • advanced glycation end products (AGEs)
  • food chemistry
  • Maillard reaction
  • metabolomics
  • nutrition
  • plant biology
  • plant biochemistry
  • plant physiology
  • protein glycation
  • proteomics

Published Papers (2 papers)

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Research

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29 pages, 2107 KiB  
Article
Does Protein Glycation Impact on the Drought-Related Changes in Metabolism and Nutritional Properties of Mature Pea (Pisum sativum L.) Seeds?
by Tatiana Leonova, Veronika Popova, Alexander Tsarev, Christian Henning, Kristina Antonova, Nadezhda Rogovskaya, Maria Vikhnina, Tim Baldensperger, Alena Soboleva, Ekaterina Dinastia, Mandy Dorn, Olga Shiroglasova, Tatiana Grishina, Gerd U. Balcke, Christian Ihling, Galina Smolikova, Sergei Medvedev, Vladimir A. Zhukov, Vladimir Babakov, Igor A. Tikhonovich, Marcus A. Glomb, Tatiana Bilova and Andrej Frolovadd Show full author list remove Hide full author list
Int. J. Mol. Sci. 2020, 21(2), 567; https://doi.org/10.3390/ijms21020567 - 15 Jan 2020
Cited by 21 | Viewed by 4345
Abstract
Protein glycation is usually referred to as an array of non-enzymatic post-translational modifications formed by reducing sugars and carbonyl products of their degradation. The resulting advanced glycation end products (AGEs) represent a heterogeneous group of covalent adducts, known for their pro-inflammatory effects in [...] Read more.
Protein glycation is usually referred to as an array of non-enzymatic post-translational modifications formed by reducing sugars and carbonyl products of their degradation. The resulting advanced glycation end products (AGEs) represent a heterogeneous group of covalent adducts, known for their pro-inflammatory effects in mammals, and impacting on pathogenesis of metabolic diseases and ageing. In plants, AGEs are the markers of tissue ageing and response to environmental stressors, the most prominent of which is drought. Although water deficit enhances protein glycation in leaves, its effect on seed glycation profiles is still unknown. Moreover, the effect of drought on biological activities of seed protein in mammalian systems is still unstudied with respect to glycation. Therefore, here we address the effects of a short-term drought on the patterns of seed protein-bound AGEs and accompanying alterations in pro-inflammatory properties of seed protein in the context of seed metabolome dynamics. A short-term drought, simulated as polyethylene glycol-induced osmotic stress and applied at the stage of seed filling, resulted in the dramatic suppression of primary seed metabolism, although the secondary metabolome was minimally affected. This was accompanied with significant suppression of NF-kB activation in human SH-SY5Y neuroblastoma cells after a treatment with protein hydrolyzates, isolated from the mature seeds of drought-treated plants. This effect could not be attributed to formation of known AGEs. Most likely, the prospective anti-inflammatory effect of short-term drought is related to antioxidant effect of unknown secondary metabolite protein adducts, or down-regulation of unknown plant-specific AGEs due to suppression of energy metabolism during seed filling. Full article
(This article belongs to the Special Issue Plant Protein Glycation)
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Review

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16 pages, 3030 KiB  
Review
Protein Glycation in Plants—An Under-Researched Field with Much Still to Discover
by Naila Rabbani, Maryam Al-Motawa and Paul J. Thornalley
Int. J. Mol. Sci. 2020, 21(11), 3942; https://doi.org/10.3390/ijms21113942 - 30 May 2020
Cited by 26 | Viewed by 4201
Abstract
Recent research has identified glycation as a non-enzymatic post-translational modification of proteins in plants with a potential contributory role to the functional impairment of the plant proteome. Reducing sugars with a free aldehyde or ketone group such as glucose, fructose and galactose react [...] Read more.
Recent research has identified glycation as a non-enzymatic post-translational modification of proteins in plants with a potential contributory role to the functional impairment of the plant proteome. Reducing sugars with a free aldehyde or ketone group such as glucose, fructose and galactose react with the N-terminal and lysine side chain amino groups of proteins. A common early-stage glycation adduct formed from glucose is Nε-fructosyl-lysine (FL). Saccharide-derived reactive dicarbonyls are arginine residue-directed glycating agents, forming advanced glycation endproducts (AGEs). A dominant dicarbonyl is methylglyoxal—formed mainly by the trace-level degradation of triosephosphates, including through the Calvin cycle of photosynthesis. Methylglyoxal forms the major quantitative AGE, hydroimidazolone MG-H1. Glucose and methylglyoxal concentrations in plants change with the developmental stage, senescence, light and dark cycles and also likely biotic and abiotic stresses. Proteomics analysis indicates that there is an enrichment of the amino acid residue targets of glycation, arginine and lysine residues, in predicted functional sites of the plant proteome, suggesting the susceptibility of proteins to functional inactivation by glycation. In this review, we give a brief introduction to glycation, glycating agents and glycation adducts in plants. We consider dicarbonyl stress, the functional vulnerability of the plant proteome to arginine-directed glycation and the likely role of methylglyoxal-mediated glycation in the activation of the unfolded protein response in plants. The latter is linked to the recent suggestion of protein glycation in sugar signaling in plant metabolism. The overexpression of glyoxalase 1, which suppresses glycation by methylglyoxal and glyoxal, produced plants resistant to high salinity, drought, extreme temperature and other stresses. Further research to decrease protein glycation in plants may lead to improved plant growth and assist the breeding of plant varieties resistant to environmental stress and senescence—including plants of commercial ornamental and crop cultivation value. Full article
(This article belongs to the Special Issue Plant Protein Glycation)
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