内质网
自噬
内质网相关蛋白降解
未折叠蛋白反应
蛋白酶体
脂肪肝
细胞生物学
慢性肝病
癌症研究
蛋白质降解
泛素
肝病
化学
医学
细胞凋亡
生物
疾病
肝硬化
内科学
生物化学
基因
作者
Siwei Xia,Zhimin Wang,Sumin Sun,Ying Su,Zhanghao Li,Jiangjuan Shao,Shanzhong Tan,Anping Chen,Shijun Wang,Zili Zhang,Feng Zhang,Shizhong Zheng
标识
DOI:10.1016/j.phrs.2020.105218
摘要
Endoplasmic reticulum (ER) stress is easily observed in chronic liver disease, which often causes accumulation of unfolded or misfolded proteins in the ER, leading to unfolded protein response (UPR). Regulating protein degradation is an integral part of UPR to relieve ER stress. The major protein degradation system includes the ubiquitin-proteasome system (UPS) and autophagy. All three arms of UPR triggered in response to ER stress can regulate UPS and autophagy. Accumulated misfolded proteins could activate these arms, and then generate various transcription factors to regulate the expression of UPS-related and autophagy-related genes. The protein degradation process regulated by UPR has great significance in many chronic liver diseases, including non-alcoholic fatty liver disease (NAFLD), alcoholic liver disease (ALD), viral hepatitis, liver fibrosis, and hepatocellular carcinoma(HCC). In most instances, the degradation of excessive proteins protects cells with ER stress survival from apoptosis. According to the specific functions of protein degradation in chronic liver disease, choosing to promote or inhibit this process is promising as a potential method for treating chronic liver disease.
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