内质网应激与创伤后应激障碍

Endoplasmic reticulum stress and posttraumatic stress disorder

内质网应激启动非折叠蛋白反应,使处于结合状态的内质网三条通路PERK,IRE1及ATF6与内质网伴侣蛋白分离,从而活化三条通路,启动细胞凋亡路径。利用创伤后应激障碍动物模型单程长时刺激(single-prolonged stress,SPS),研究发现SPS早期,内质网应激启动内质网伴侣蛋白,对神经细胞起到保护作用。但是在中后期,随着内质网伴侣蛋白对非折叠蛋白纠正能力的下降,加速活化三条径路,启动细胞凋亡。

Endoplasmic reticulum stress（ERS） induce the protein folding reaction, and then make endoplasmic reticulum three pathway PERK, IRE1 and ATF6 separate from the endoplasmic reticulum chaperone, activate of three pathways and start the apoptosis pathway. We used the animal model of posttraumatic stress disorder： single prolonged stress（SPS） to find endoplasmic reticulum stress cause the endoplasmic reticulum chaperone and protect neurons at the early stage of SPS, but in the later period of SPS, when the ability decreased that endoplasmic reticulum chaperone correct for the folding protein, ERS could accelerate the activation of three path and induce the cell apoptosis.