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病毒感染时黏膜屏障处未折叠蛋白反应的免疫调节

Immune regulation of the unfolded protein response at the mucosal barrier in viral infection.

作者信息

Wang Ran, Moniruzzaman Md, Shuffle Eric, Lourie Rohan, Hasnain Sumaira Z

机构信息

Translational Research Institute Immunopathology Group at Mater Research Institute - The University of Queensland Brisbane QLD Australia.

Faculty of Medicine The University of Queensland Brisbane QLD Australia.

出版信息

Clin Transl Immunology. 2018 Apr 3;7(4):e1014. doi: 10.1002/cti2.1014. eCollection 2018.

DOI:10.1002/cti2.1014
PMID:29632667
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5881172/
Abstract

Protein folding in the endoplasmic reticulum (ER) is subject to stringent quality control. When protein secretion demand exceeds the protein folding capacity of the ER, the unfolded protein response (UPR) is triggered as a consequence of ER stress. Due to the secretory function of epithelial cells, UPR plays an important role in maintaining epithelial barrier function at mucosal sites. ER stress and activation of the UPR are natural mechanisms by which mucosal epithelial cells combat viral infections. In this review, we discuss the important role of UPR in regulating mucosal epithelium homeostasis. In addition, we review current insights into how the UPR is involved in viral infection at mucosal barriers and potential therapeutic strategies that restore epithelial cell integrity following acute viral infections via cytokine and cellular stress manipulation.

摘要

内质网(ER)中的蛋白质折叠受到严格的质量控制。当蛋白质分泌需求超过内质网的蛋白质折叠能力时,内质网应激会引发未折叠蛋白反应(UPR)。由于上皮细胞的分泌功能,UPR在维持黏膜部位的上皮屏障功能中发挥着重要作用。内质网应激和UPR的激活是黏膜上皮细胞对抗病毒感染的天然机制。在本综述中,我们讨论了UPR在调节黏膜上皮细胞稳态中的重要作用。此外,我们还综述了目前关于UPR如何参与黏膜屏障处病毒感染的见解,以及通过细胞因子和细胞应激调控在急性病毒感染后恢复上皮细胞完整性的潜在治疗策略。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/4faa7cb9dc99/CTI2-7-e1014-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/1049b389677d/CTI2-7-e1014-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/360ecba85388/CTI2-7-e1014-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/53dac83384b5/CTI2-7-e1014-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/2deb459db13d/CTI2-7-e1014-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/4faa7cb9dc99/CTI2-7-e1014-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/1049b389677d/CTI2-7-e1014-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/360ecba85388/CTI2-7-e1014-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/53dac83384b5/CTI2-7-e1014-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/2deb459db13d/CTI2-7-e1014-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcb8/5881172/4faa7cb9dc99/CTI2-7-e1014-g005.jpg

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