TY - JOUR

T1 - Glycation of plant proteins

T2 - Regulatory roles and interplay with sugar signalling?

AU - Shumilina, Julia

AU - Kusnetsova, Alena

AU - Tsarev, Alexander

AU - Janse van Rensburg, Henry C.

AU - Medvedev, Sergei

AU - Demidchik, Vadim

AU - Van den Ende, Wim

AU - Frolov, Andrej

PY - 2019/5/1

Y1 - 2019/5/1

N2 - 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.

AB - 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.

KW - Advanced glycation end products (ages)

KW - Methylglyoxal

KW - Plant glycation

KW - Protein degradation

KW - Protein glycation

KW - Sugar signalling

KW - Thermal processing of foods

KW - OXIDATIVE STRESS

KW - GLUCOSE AUTOXIDATION

KW - advanced glycation end products (AGEs)

KW - thermal processing of foods

KW - protein glycation

KW - sugar signalling

KW - MASS-SPECTROMETRY

KW - DIABETES-MELLITUS

KW - methylglyoxal

KW - REACTIVE OXYGEN

KW - ADVANCED GLYCOXIDATION

KW - END-PRODUCTS AGES

KW - plant glycation

KW - protein degradation

KW - ELECTRON-TRANSPORT

KW - MAILLARD REACTIONS

KW - SOLUBLE RECEPTOR

UR - http://www.scopus.com/inward/record.url?scp=85066845670&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/glycation-plant-proteins-regulatory-roles-interplay-sugar-signalling

U2 - 10.3390/ijms20092366

DO - 10.3390/ijms20092366

M3 - Review article

C2 - 31086058

AN - SCOPUS:85066845670

VL - 20

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 9

M1 - 2366

ER -