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Involvement of Nrf2 and Keap1 in the activation of antioxidant responsive element (ARE) by chemopreventive agent peptides from soft-shelled turtle

文献类型： 外文期刊

作者： Wang, Nan 1 ; Wang, Wei 2 ; Sadiq, Faizan Ahmed 3 ; Wang, Shilei 1 ; Liu Caiqin 1 ; Jin Jianchang 1 ;

作者机构： 1.Zhejiang Shuren Univ, Coll Biol & Environm Engn, Hangzhou 310015, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Qual & Stand Agr Prod, Hangzhou 310021, Peoples R China

3.Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China

关键词： Antioxidant peptides; ARE; Nrf2; Oxidative stress

期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）

ISSN： 1359-5113

年卷期： 2020 年 92 卷

页码：

收录情况： SCI

摘要： The antioxidant response element (ARE) is a cis-acting enhancer sequence located in the region containing genes related to antioxidant and detoxification. Under oxidative stress, the induction of nuclear factor-E2-related factor 2 (Nrf2)/ARE is considered as a fundamental process involved in defending reactive oxygen species (ROS) and providing protection against toxic xenobiotics. In this study, we obtained seven antioxidant peptides from soft-shelled turtle and concluded that Glu-Asp-Tyr-Gly-Ala (EDYGA) is the most potent ARE-luciferase inducer. To gain fundamental insights into the role of EDYGA in oxidative stress, we evaluated the effects of EDYGA on the Nrf2/Keap1 system in HepG 2 cells. The results revealed that EDYGA modulated the Nrf2/ARE pathway by enhancing Nrf2 level through the stabilization of Nrf2, which was accomplished by a decrease in the level of Keapl. These actions eventually led to an increase in nuclear Nrf2 accumulation and ARE-binding activity. Moreover, silencing Nrf2 markedly reduced ARE-driven activity induced by EDYGA. Docking results proved that glutamate residues of peptide EDYGA directly bind to Arg 415 of Kelch domain receptor pocke. The results were helpful in understanding the antioxidant activity of peptides from soft-shelled turtle which have potential to be used in foods and drugs as functional ingredients.

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