Glutathione peroxidase and related selenoproteins (GPx)

Glutathione peroxidases (GPxs) and related selenoproteins are a group of enzymes that incorporate the trace element selenium as selenocysteine in their active sites. These enzymes play a critical role in cellular antioxidant defense by reducing hydrogen peroxide and organic hydroperoxides to water or alcohols, thereby protecting cells from oxidative damage (nih.gov, 2022). Among the family, GPx4 is particularly notable for its unique ability to reduce phospholipid hydroperoxides, making it a master regulator of ferroptosis, an iron-dependent form of regulated cell death (nih.gov, 2025). Other selenoproteins, such as thioredoxin reductases (TrxRs) and iodothyronine deiodinases (DIOs), are involved in redox signaling and thyroid hormone metabolism, respectively (nih.gov, 2009). Dysregulation of these proteins is linked to various pathologies, including cancer, neurodegeneration, and cardiovascular diseases (medchemexpress.com). Consequently, they have emerged as significant therapeutic targets, with GPx4 inhibitors being explored for cancer therapy and GPx mimics or activators for neuroprotection and anti-inflammatory applications (patsnap.com, 2024).

Other names

Glutathione peroxidase familySelenoenzymesSelenoprotein familyGPx family

Modulation of cellular redox state through the reduction of hydroperoxides or inhibition of antioxidant enzymes to induce ferroptosis.