Targeting the Endoplasmic Reticulum Oxidoreductin-1 Alpha–Protein Disulfide Isomerase Redox Interface as a Therapeutic Strategy in Cancer

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Authors: Kamilla Khojayeva, Aiym Zhussipbekkyzy, Dilbara Balkybayeva, Karakat Sabit, Lucia Rossetti Lopes, Kamila Sagatbekova, Assem Zhakupova, Mohamad Aljofan
Cited by: 3
References: 85

Abstract

The endoplasmic reticulum (ER) is critical in aiding cells in ensuring that proteins are folded and processed correctly, particularly during stressful situations. ER oxidoreductin-1 alpha (ERO1α) is an enzyme that is responsible for the formation of disulfide bonds during protein folding, along with protein disulfide isomerase (PDI). This redox pathway is often highly upregulated in cancer cells, allowing tumors to survive harsh conditions such as hypoxia and nutrient deprivation. This review discusses the role of the ERO1α-PDI system in cancer development through the regulation of oxidative stress, redox homeostasis, and tumor plasticity. It further shows the therapeutic potential of interrupting the ERO1α-PDI axis, which could lead to protein misfolding; enhanced generation of reactive oxygen species (ROS); and, eventually, cancer cell death.

Fields of Study & Subjects

Endoplasmic Reticulum Stress and Disease Redox biology and oxidative stress Cellular transport and secretion

Publication details

Journal / source
Biomedicines
Publisher
MDPI AG
Volume
14
Issue
2
Pages
263–263
Publication date
23 January 2026
Language
EN