相关实验视频

Updated: Jun 28, 2025

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity

Published on: June 14, 2024

细胞内膜网膜应激会诱导肝血管的血管扩张,而这种扩张并非由未折叠的蛋白质反应介导

Sergejs Zavadskis¹, Anna Shiganyan¹, Andrea Müllebner²

¹Ludwig Boltzmann Institute for Traumatology, The Research Center in Cooperation with AUVA, Austrian Cluster for Tissue Regeneration, Donaueschingenstraße 13, 1200 Vienna, Austria.

International journal of molecular sciences

|April 13, 2024

概括

细胞内膜网膜 (ER) 的压力通过氧化 (NO) 以一种独立于未折叠蛋白质响应 (UPR) 途径的方式诱导肝脏血管扩张. 这种NO释放源于细胞内储存,而不是内皮NO合成酶 (eNOS).

科学领域:

血管生物学血管生物学
细胞应激反应细胞应激反应
肝病学肝病学是一种肝病学.

背景情况:

细胞内膜网膜 (ER) 应激和未展开的蛋白质反应 (UPR) 与各种疾病有关.
在肝脏疾病中,ER压力和肝脏输液受损经常同时存在,但它们之间的确切关系尚不清楚.

研究的目的:

为了研究ER压力和UPR对肝血管大小的影响.
确定对细胞内 (Ca2+) 和氧化 (NO) 水平的影响,这是血管度的关键调节剂.

主要方法:

实验是在精确切割的肝脏组织切片上进行的.
孔焦显微镜和激光扫描显微镜 (LSM) 用于3D成像和分析NO和Ca2+水平.
还使用NO分析仪测量了NO度.

主要成果:

突尼卡米辛是一种ER压力诱导剂,引起显著的血管扩张,类似于血管扩张剂乙胆.
图尼卡米辛和乙胆都增加了NO和Ca2+水平.
血管扩张即使在个人UPR通路 (ATF-6,PERK,IRE1) 被抑制时也持续存在,这证实了UPR激活.
在HUVEC细胞中NO水平升高并非源于内皮NO合成酶 (eNOS) 的激活.

结论:

图尼卡米辛诱导的ER压力促进了NO依赖性肝血管扩张.
这种血管扩张是由平滑肌细胞中的细胞内缩剂可激活NO储存 (NANOS) 介导的,而不是eNOS.
ER压力通过一种独立于规范UPR通路的新NO依赖机制影响肝输液.

关键词:

在Ca2+中.没有,没有,没有,没有.细胞内膜网膜的压力应激活体外模型模型的模型缩剂是一种缩剂.不折叠的蛋白质反应反应血管度血管度

更多相关视频

Measurements of Physiological Stress Responses in C. Elegans

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

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...

The Unfolded Protein Response

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

Role of ER in the Secretory Pathway

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

Smooth Endoplasmic Reticulum

Smooth Endoplasmic Reticulum

Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...