蛋白质二硫键异构酶
内质网
肿瘤进展
细胞生物学
蛋白质折叠
细胞凋亡
未折叠蛋白反应
折叠(DSP实现)
化学
生物
生物化学
基因
工程类
电气工程
作者
Zeyu Wang,Hao Zhang,Quan Cheng
标识
DOI:10.1016/j.biopha.2019.109688
摘要
Disulfide bond formation is catalyzed by the protein disulfide Isomerases (PDI) family. This is a critical step in protein folding which occurs within the endoplasmic reticulum. PDIA4, as a member of the PDI family, can cause the adjustment of αIIβ 3 affinities which activate platelet and promote thrombosis formation. Endoplasmic reticulum response is triggered by accumulation of abnormal folding proteins concomitant with increasing PDIA4 expression. Besides, current researches indicate that activated platelets and ERS response affect tumor progression. And PDIA4, as previous reported, also participates in tumor progression by affecting cell apoptosis and DNA repair machinery without specific mechanisms revealed.Therefore, PDI inhibitor might possess great potential value in against tumor progression. In this review, we summarize information on PDIA4 including its the basic characteristics and its implication on tumor.
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