Glutathione peroxidase 7 (GPX7)

Glutathione peroxidase 7 is a non-selenocysteine containing peroxidase enzyme predominantly localized in the endoplasmic reticulum in mammalian cells[2]. Unlike classic glutathione peroxidases, GPX7 does not contain a GSH-binding domain and uses cysteine residues (Cys57, Cys86) for redox catalysis[2]. Its main function is to promote protein oxidative folding by detoxifying hydrogen peroxide generated by Ero1α and efficiently transferring oxidizing equivalents to protein disulfide isomerase (PDI), thereby accelerating the maturation and folding of secreted and membrane proteins[1][2]. GPX7 also interacts with and enhances the activity of chaperone proteins such as GRP78/BIP during ER stress, contributing to cellular protection against oxidative stress, inflammation, and potentially protecting against cancer progression and metabolic disorders[1][2]. Deficiencies or dysregulation of GPX7 can lead to elevated ROS, improper protein folding, and are implicated in the pathology of liver diseases, cancer, and other ER stress-related conditions[2].

Other names

Non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidaseGPx-7GSHPx-7NPGPxGlutathione peroxidase 6 (limited evidence—may refer to a related protein but not identical; confirm when extracting structured data)FLJ14777UNQ469/PRO828CL683

Antioxidant effect (potential mechanism if targeted: restoration of redox homeostasis, reduction of ROS, improvement of protein folding efficiency[1][2]); Modulation of oxidative protein folding pathways (methodologically, drugs could enhance or inhibit GPX7 activity to alter ER stress or oxidative folding, especially in disease contexts[2])