相关实验视频

Updated: Jun 17, 2025

Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells

Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells

Published on: May 22, 2014

NLRP3炎症酶激活介导肝炎E病毒诱导的神经炎症

Bingyan Wei¹, Huopeng Li¹, Minheng Cheng²

¹Laboratory of Animal Pathology and Public Health, National Key Laboratory of Veterinary Public Health and Safety, College of Veterinary Medicine, China Agricultural University, Beijing, China.

Journal of viral hepatitis

|August 13, 2024

概括

肝炎E病毒 (HEV) 通过激活NLRP3炎症体,引发神经炎症,导致脑损伤. 针对这种途径为HEV诱导的神经疾病提供了潜在的治疗方法.

科学领域:

神经科学是一个神经科学.
免疫学免疫学免疫学
病毒学病毒学

背景情况:

肝炎E病毒 (HEV) 是急性病毒性肝炎的常见原因之一.
高血压病毒感染越来越多地与神经系统疾病有关,高血压病毒穿越血脑屏障 (BBB).
引起HEV的神经炎症和脑损伤的确切机制尚不清楚.

研究的目的:

研究NLRP3炎症酶激活在HEV诱导的神经炎症中的作用.
探索HEV对大脑微血管内皮细胞 (BMEC) 和BBB的影响.
评估针对NLRP3炎症酶的治疗潜力.

主要方法:

在Gerbil模型中的HEV感染.
脑组织的组织病理学检查.
在大脑和人类BMEC (hBMEC) 中分析NLRP3炎症组分 (NLRP3,caspase-1,IL-1β,IL-18).
用NLRP3抑制剂MCC950进行治疗.

主要成果:

HEV感染导致大脑组织病理变化,如化和鼠神经元损伤.
在受感染的大脑和hBMEC中观察到NLRP3,caspase-1,IL-1β和IL-18的高表达.
在hBMEC中检测到HEV粒子,这表明BBB妥协.
MCC950治疗减少了NLRP3炎症酶激活,线粒体损伤和VE-cadherin降解.

结论:

HEV感染激活NLRP3炎症酶,导致神经炎症和脑损伤.
BBB易受HEV感染,这可能导致神经系统并发症.
向NLRP3炎症酶组为HEV相关的神经疾病提供了一个有前途的治疗策略.

关键词:

在NLRP3炎症酶体中,NLRP3炎症大脑大脑大脑的大脑大脑 hBMECs 的使用情况.乙型肝炎病毒的感染.

更多相关视频

Detection of Inflammasome Activation and Pyroptotic Cell Death in Murine Bone Marrow-derived Macrophages

Detection of Inflammasome Activation and Pyroptotic Cell Death in Murine Bone Marrow-derived Macrophages

Published on: May 21, 2018

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

相关概念视频

Regulation of the Unfolded Protein Response

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...