摘 要：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
Abstract: 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
