Crosstalk between ER stress, NLRP3 inflammasome, and inflammation
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MINI-REVIEW
Crosstalk between ER stress, NLRP3 inflammasome, and inflammation Wei Li 1 & Ting Cao 1 & Chunyi Luo 1 & Jialun Cai 1 & Xiangping Zhou 1 & Xinhua Xiao 2 & Shuangquan Liu 1 Received: 4 February 2020 / Revised: 31 March 2020 / Accepted: 5 April 2020 # Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Endoplasmic reticulum stress (ERS) is a protective response to restore protein homeostasis by activating the unfolded protein response (UPR). However, UPR can trigger cell death under severe and/or persistently high ERS. The NLRP3 inflammasome is a complex of multiple proteins that activates the secretion of the proinflammatory cytokine IL-1β in a caspase-1-dependent manner to participate in the regulation of inflammation. The NLRP3 inflammasome involvement in ERS-induced inflammation has not been completely described. The intersection of ERS with multiple inflammatory pathways can initiate and aggravate chronic diseases. Accumulating evidence suggests that ERS-induced activation of NLRP3 inflammasome is the pathological basis of various inflammatory diseases. In this review, we have discussed the networks between ERS and NLRP3 inflammasome, with the view to identifying novel therapeutic targets in inflammatory diseases. Key points • Endoplasmic reticulum stress (ERS) is an important factor for the activation of the NLRP3 inflammasomes that results in pathological processes. • ERS can activate the NLRP3 inflammasome to induce inflammatory responses via oxidative stress, calcium homeostasis, and NF-κB activation. • The interactions between ERS and NLRP3 inflammasome are associated with inflammation, which represent a potential therapeutic opportunity of inflammatory diseases. Keywords Endoplasmic reticulum stress . NLRP3 inflammasome . Inflammation . Reactive oxygen species . NF-κB
Introduction Endoplasmic reticulum (ER) is a specialized organelle in eukaryotic cells involved in protein synthesis, modification, integration and quality control, calcium homeostasis, and lipid biosynthesis (Saito and Imaizumi 2018). Dysregulated protein processing can lead to the accumulation of misfolded proteins Wei Li and Ting Cao contributed equally to this work. * Xinhua Xiao [email protected] * Shuangquan Liu [email protected] 1
Department of Clinical Laboratory, The First Affiliated Hospital of University of South China, Hengyang, Hunan, China
2
Department of Endocrinology, The First Affiliated Hospital of University of South China, Hengyang, Hunan, China
in the ER, resulting in hypoxia, protein overloading, calcium metabolic disorders, low intracellular ATP levels, and oxidative stress. When the accumulation of protein aggregates exceeds ER loading capacity, it leads to the ERS (Namgaladze et al. 2019) that is mediated by the unfolded protein response (UPR), endoplasmic reticulum overload response (EOR), and sterol regulatory element–binding protein (SREBP). While transient ERS restores protein homeostasis by activating the UPR and reducing protein aggregates, long-term or severe ERS can trigger
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