中国科技核心期刊
CN:31-1600/Q
ISSN:1004-0374
“健康与疾病的免疫”国际学术研讨会通知      关于有网站冒充本刊网站的声明
《生命科学》 2008, 20(2): 246-
未折叠蛋白反应的信号转导
李 明1,2,丁 健1,缪泽鸿1*
1 中国科学院上海药物研究所新药研究国家重点实验室,上海 201203; 2 中国科学院研究生院,北京 100049
摘 要:在内质网中,分泌性蛋白、跨膜蛋白和内质网驻留蛋白折叠成天然构象,经过修饰后,形成有活性的功能性蛋白质。如果蛋白质在内质网内的折叠受到抑制,造成未折叠蛋白聚集,将引起内质网应激, 激活未折叠蛋白反应(unfolded protein response, UPR),使蛋白质的生物合成减少,内质网的降解功能增强,从而降低内质网负担,维持细胞内的稳态。如果内质网应激持续存在,则可能诱发细胞凋亡。研究表明,未折叠蛋白反应能在多种肿瘤细胞中发生,并能促进肿瘤细胞的生长。本文对未折叠蛋白反应与肿瘤研究的最新进展进行综述。
关键词:内质网应激;未折叠蛋白反应;肿瘤
中图分类号:Q51;R73.23  文献标识码:A
 
The signal transduction of unfolded protein response
LI Ming1,2, DING Jian1 , MIAO Ze-hong1*
(1 State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China; 2 Graduate School of Chinese Academy of Sciences, Beijing 100049, China)
Abstract: In the endoplasmic reticulum(ER), secretory, transmembrane and ER-resident proteins are folded into their native conformation,undergo posttranslational modifications  and are finally transformed into their corresponding functional forms. Disruption of protein folding causes ER stress and activates a signaling network called the unfolded proteins response (UPR). UPR increases the biosynthesis capacity of ER chaperones and foldases, and relieves the biosynthetic burden of the secretory pathway by down-regulating expression of genes encoding secreted proteins. Defects in protein folding if not corrected timely, could lead to cell apoptosis. It has been revealed that UPR is highly activated in a variety of tumors types and could contribute to tumor survival and growth.
Key words:  ER stress; unfold protein response; cancer
 
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