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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 (ER) stress initiates the non-folded protein reaction, which separates the three endoplasmic reticulum PERK, IRE1 and ATF6 in the endoplasmic reticulum from the endoplasmic reticulum chaperone, thereby activating the three pathways and activating the apoptotic pathways. Using single-prolonged stress (SPS) in an animal model of post-traumatic stress disorder, we found that endoplasmic reticulum stress initiates endoplasmic reticulum chaperone protein during early and endoplasmic reticulum stress, which plays a protective role on nerve cells. However, in the later period, as the endoplasmic reticulum chaperone protein reduces the ability of the non-folded protein to correct, accelerating the activation of the three pathways and initiating apoptosis.