Journal
BIOMEDICINE & PHARMACOTHERAPY
Volume 122, Issue -, Pages -Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biopha.2019.109688
Keywords
PDI family; PDIA4; ERp72; Platelet; Tumor; Endoplasmic reticulum stress response
Funding
- National Nature Science Foundation of China [81703622]
- China Postdoctoral Science Foundation [2018M63302]
- Natural Science Foundation of Hunan Province of China [2018JJ3838]
- Hunan Provincial Health Committee Foundation of China [C2019186]
Ask authors/readers for more resources
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 alpha II beta 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
