2. Academic Validation
  3. Protein disulfide isomerase family mediated redox regulation in cancer

Protein disulfide isomerase family mediated redox regulation in cancer

  • Adv Cancer Res. 2023:160:83-106. doi: 10.1016/bs.acr.2023.06.001.
Zhi-Wei Ye 1,  Jie Zhang 2,  Muhammad Aslam 2,  Anna Blumental-Perry 3,  Kenneth D Tew 2,  Danyelle M Townsend 4
Affiliations

Affiliations

  • 1 Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, United States. Electronic address: tezzh@musc.edu.
  • 2 Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, United States.
  • 3 Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, NY, United States.
  • 4 Department of Drug Discovery and Biomedical Sciences, Medical University of South Carolina, Charleston, SC, United States.
PMID: 37704292 DOI: 10.1016/bs.acr.2023.06.001
Abstract

Protein disulfide isomerase (PDI) and its superfamilies are mainly endoplasmic reticulum (ER) resident proteins with essential roles in maintaining cellular homeostasis, via thiol oxidation/reduction cycles, chaperoning, and isomerization of client proteins. Since PDIs play an important role in ER homeostasis, their upregulation supports cell survival and they are found in a variety of Cancer types. Despite the fact that the importance of PDI to tumorigenesis remains to be understood, it is emerging as a new therapeutic target in Cancer. During the past decade, several PDI inhibitors has been developed and commercialized, but none has been approved for clinical use. In this review, we discuss the properties and redox regulation of PDIs within the ER and provide an overview of the last 5 years of advances regarding PDI inhibitors.

Keywords

Cancer; ER stress; Inhibitors; Protein disulfide isomerase; Redox regualtion.

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