Glutathione peroxidase 1 (GPX1) (GPX1)

Glutathione peroxidase 1 (GPX1) is a ubiquitous antioxidant enzyme and the most abundant selenoprotein in mammals, characterized by a critical selenocysteine residue at its catalytic site (UniProt: P07203). It plays a fundamental role in cellular defense by catalyzing the reduction of hydrogen peroxide and organic hydroperoxides into water and alcohols, respectively, using reduced glutathione as an electron donor (PubMed: 22503688). This enzymatic activity is essential for protecting cellular components from oxidative damage and modulating redox-sensitive signaling pathways. GPX1 deficiency is linked to increased susceptibility to atherosclerosis and neurodegeneration, while its overexpression or high activity can contribute to insulin resistance or protect cancer cells from oxidative stress (PubMed: 18505688). Pharmacological intervention includes GPX1 mimetics like Ebselen, which are investigated for treating stroke and hearing loss, and inhibitors that aim to increase oxidative stress in tumor environments (PubChem: CID 3194).

Other names

GPX-1GSHPx-1Cellular glutathione peroxidaseSelenoprotein GPX1

GPX1 mimetics catalyze the reduction of hydroperoxides using glutathione as a reducing agent to mitigate oxidative stress, while inhibitors target the selenocysteine residue to increase reactive oxygen species for therapeutic benefit in specific contexts like oncology.