Study summary · research use only
The Selenoprotein Glutathione Peroxidase 4: From Molecular Mechanisms to Novel Therapeutic Opportunities
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This review discusses the selenoprotein glutathione peroxidase 4 (GPX4), an antioxidant enzyme in the human body that reduces complex hydroperoxides using reduced glutathione (GSH). The authors describe GPX4's role as a key regulator of ferroptosis and its identification as a pharmacological target studied in relation to cancers and neurodegenerative disorders. The review summarizes recent research on how GPX4 differs from other glutathione peroxidase family members, its biochemical properties, its relationship to lipid peroxidation and ferroptosis, and approaches being studied to modulate it as a potential therapeutic target.
Abstract
The selenoprotein glutathione peroxidase 4 (GPX4) is one of the main antioxidant mediators in the human body. Its central function involves the reduction of complex hydroperoxides into their respective alcohols often using reduced Glutathione (GSH) as a reducing agent. GPX4 has become a hotspot therapeutic target in biomedical research following its characterization as a chief regulator of ferroptosis, and its subsequent recognition as a specific pharmacological target for the treatment of an extensive variety of human diseases including cancers and neurodegenerative disorders. Several recent studies have provided insights into how GPX4 is distinguished from the rest of the glutathione peroxidase family, the unique biochemical properties of GPX4, how GPX4 is related to lipid peroxidation and ferroptosis, and how the enzyme may be modulated as a potential therapeutic target. This current report aims to review the literature underlying all these insights and present an up-to-date perspective on the current understanding of GPX4 as a potential therapeutic target.
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