GPX1

Glutathione peroxidase 1 (GPX1) is a ubiquitously expressed selenium-dependent antioxidant enzyme located in the cytosol and mitochondria that reduces hydrogen peroxide and soluble hydroperoxides using glutathione, thereby maintaining cellular redox homeostasis and controlling reactive oxygen species (ROS) signaling^[1]. Mechanistically, GPX1 is a selenoprotein whose catalytic activity depends on a redox-active selenocysteine residue and represents a major component of the glutathione peroxidase antioxidant defense network that limits peroxide-mediated cellular damage^[1][2]. Through regulation of intracellular peroxide levels, GPX1 influences thiol redox balance and modulates biological processes linked to oxidative stress, metabolic regulation, vascular function, and cellular survival pathways^[1]. In disease contexts, altered GPX1 expression or activity has been associated with cardiovascular, metabolic, neurological, and cancer-related phenotypes, highlighting its importance in maintaining oxidative stress resilience across tissues^[1][5]. Experimental studies further demonstrate that Gpx1-null mice remain viable but display increased sensitivity to oxidant challenges such as paraquat exposure, establishing GPX1 as a widely used genetic model for investigating oxidative injury and antioxidant defense mechanisms^[3][4]. Compared with related glutathione peroxidase isoforms, GPX1 is the prototypical and most broadly expressed cellular member of the GPX family, whereas other isoforms exhibit distinct tissue distributions, extracellular localization, or substrate preferences^[2]. For experimental applications, pharmacological GPX1 mimetics and selenium-dependent approaches, including the organoselenium compound ebselen, have been used to modulate GPX-associated antioxidant activity and evaluate oxidative stress pathways in cellular models^[6].

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