Inhibition of Methylglyoxal-Induced Histone H1 Nε -Carboxymethyllysine Formation by (+)-Catechin

Journal of Agricultural and Food Chemistry
Lijun YangQiang Dong

Abstract

Reactive dicarbonyl species (RCS) such as methylglyoxal (MGO) and glyoxal (GO) are common intermediates in protein damage, leading to the formation of advanced glycation end products (AGEs) through nonenzymatic glycation. (+)-Catechin, a natural plant extract from tea, has been evaluated for its ability in trapping GO and MGO. However, (+)-catechin is also reported to have both antioxidant ability and pro-oxidant properties. Until now, whether (+)-catechin can inhibit the formation of nonenzymatic glycation and the mechanism of the inhibition in nucleoprotein nonenzymatic glycation is still unclear. In the present study, histone H1 and MGO were used to establish an in vitro (100 mM phosphate buffer solution (PBS), pH 7.4, 37 °C) protein glycation model to study the trapping ability of (+)-catechin. Our data show that MGO caused dose-dependent protein damage, and the content of MGO-induced Schiff base formation was inhibited by (+)-catechin when the molecular ratio of catechin:MGO was 1:6. The formation of Nε-carboxymethyllysine (CML) was reduced significantly when the ratio of (+)-catechin and MGO was 1:1, which was similar to the inhibition effect of aminoguanidine (AG). The formation of CML under in vitro conditions can be in...Continue Reading

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Citations

Apr 21, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Yuzhen WangBaoguo Sun
Feb 9, 2021·Glycobiology·Abdul Rouf MirMoin Uddin
Nov 30, 2021·Journal of Biomolecular Structure & Dynamics·Akhlas TarannumKhursheed Alam
Dec 30, 2021·Journal of Agricultural and Food Chemistry·Rui PengXu Zhang

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