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Glutathione peroxidase 2 is a selenium-dependent enzyme predominantly expressed in the epithelial cells of the gastrointestinal tract (and in the liver in humans). It reduces hydrogen peroxide and organic hydroperoxides to less reactive molecules using glutathione, thereby protecting cells against oxidative damage and maintaining redox balance. GPX2 is transcriptionally regulated by the Wnt and Nrf2 pathways and plays a critical role in mucosal homeostasis, limiting inflammation, and supporting cell differentiation and proliferation in crypt cells. It is implicated as a protective factor in early tumorigenesis but may also support the growth of established tumors, resulting in complex "Janus-faced" roles in cancer biology. GPX2-deficient animals show heightened sensitivity to oxidative stress and inflammation. While no drugs selectively target GPX2, its activity is sensitive to selenium levels and could serve as a biomarker for diseases of oxidative stress or gut inflammation.
If hypothetically targeted: inhibition or upregulation would modulate cellular redox state, apoptosis, inflammation, and cancer cell proliferation
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