期刊
GENES
卷 13, 期 11, 页码 -出版社
MDPI
DOI: 10.3390/genes13112033
关键词
peroxiredoxin; endoplasmic reticulum stress; reactive oxygen species; unfolded protein response signaling; apoptosis
资金
- Gachon University Research fund [GCU-2018-0686]
- Ministry of Trade, Industry & Energy (MOTIE, Korea) [20009350]
Prx1 overexpression inhibits nuclear localization of XBP-1 and CHOP expression, reducing apoptosis and ROS production during ER stress. While ROS scavenger inhibits ER stress-induced apoptosis, it does not affect XBP-1 activation and CHOP expression. The biological role of Prx1 in ER stress may have important implications for ER stress-related diseases.
Endoplasmic reticulum (ER) stress activates the unfolded protein response (UPR) signaling via the accumulation of unfolded and misfolded proteins. ER stress leads to the production of reactive oxygen species (ROS), which are necessary to maintain redox homeostasis in the ER. Although peroxiredoxin 1 (Prx1) is an antioxidant enzyme that regulates intracellular ROS levels, the link between Prx1 and ER stress remains unclear. In this study, we investigated the role of Prx1 in X-box binding protein 1 (XBP-1) activation, the C/EBP homologous protein (CHOP) pathway, and apoptosis in response to ER stress. We observed that Prx1 overexpression inhibited the nuclear localization of XBP-1 and the expression of XBP-1 target genes and CHOP after thapsigargin (Tg) treatment to induce ER stress. In addition, Prx1 inhibited apoptosis and ROS production during ER stress. The ROS scavenger inhibited ER stress-induced apoptosis but did not affect XBP-1 activation and CHOP expression. Therefore, the biological role of Prx1 in ER stress may have important implications for ER stress-related diseases.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据