GPX8, a member of the Glutathione Peroxidases (GPXs) family, is located in the endoplasmic reticulum lumen. It is involved in redox homoeostasis, and its active site contains cysteine residues instead of selenocysteine [5,10]. It may also be involved in protein folding and regulation of Ca2+ in the endoplasmic reticulum [10].

In gliomas, GPX8 acts as a tumor accelerator, facilitating cell contact between tumor cells and macrophages and promoting microglial migration [1]. In clear cell renal cell carcinoma, GPX8 promotes lipogenesis through the NNMT, regulating tumorigenesis [2]. In hepatocellular carcinoma, downregulation of GPX8 enhances the stemness and migration ability of HCC cells [3]. In oral cancer cells, GPX8 deficiency-induced oxidative stress reprograms the m6A epitranscriptome [4]. In esophageal squamous cell carcinoma, GPX8 regulates apoptosis and autophagy through the IRE1/JNK pathway [6]. In primary glioma and glioblastoma, GPX8 is associated with poor prognosis and may be a therapeutic target [7,8]. In non-small cell lung cancer, GPX8 promotes migration and invasion by regulating epithelial characteristics [9].

In conclusion, GPX8 plays diverse roles in various biological processes and disease conditions, especially in multiple types of cancers. Functional studies, including gene knockout-related models, have revealed its significance in tumorigenesis, metastasis, and redox-related regulation, providing potential therapeutic targets for cancer treatment.