| Literature DB >> 31794946 |
Zeyu Wang1, Hao Zhang1, Quan Cheng2.
Abstract
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.Entities:
Keywords: ERp72; Endoplasmic reticulum stress response; PDI family; PDIA4; Platelet; Tumor
Year: 2019 PMID： 31794946 DOI： 10.1016/j.biopha.2019.109688
Source DB: PubMed Journal: Biomed Pharmacother ISSN： 0753-3322 Impact factor: 6.529