Glutathione Peroxidase 4

Glutathione peroxidase 4 (GPX4) is a selenium-containing antioxidant enzyme that protects cells from oxidative damage by reducing lipid hydroperoxides in cellular membranes. Using glutathione as an electron donor, GPX4 converts potentially harmful lipid hydroperoxides into less reactive lipid alcohols, thereby limiting membrane oxidation and preserving cell integrity. This activity makes GPX4 a central regulator of ferroptosis, an iron-dependent form of cell death driven by lipid peroxidation. In biology and biomedical research, studying GPX4 helps clarify mechanisms of oxidative stress, cancer cell survival, neurodegeneration, and tissue injury, while informing strategies that either preserve GPX4 function or inhibit it to promote ferroptotic cell death.

Glutathione Peroxidase 4 - Related Videos

Research

JoVE Journal - Immunology and Infection

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

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Cited by 2 •

2016

This protocol describes the quick enrichment of leukocytes from small blood samples for a subsequent specific determination of the halogenating peroxidase activity within the cells. The method can be applied to human and non-human material and may contribute to the evaluation of new inflammatory markers.

The Examination of Peroxidase-Positive Leukocytes in Semen

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Cited by 3 •

2024

This paper presents an economical and efficient protocol for examining peroxidase-positive leukocytes in semen. With the assistance of a computer-assisted semen analysis (CASA) system, the concentration of peroxidase-positive leukocytes in semen can be obtained within a total of 60 min, effectively improving the efficiency of andrology laboratory and andrologists.

Measuring Glutathione-induced Feeding Response in Hydra

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Cited by 9 •

2014

Here we describe a simple assay for the quantification of the feeding response in hydra induced by the reduced form of glutathione. This assay relies on measuring the distance between the apical end of the tentacle and mouth of hydra.

Education

JoVE Core - Pharmacokinetics and Pharmacodynamics

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

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2025

Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion. Several distinctive characteristics distinguish glutathione conjugation from other phase II...

Research

JoVE Journal - Biochemistry
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Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases

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Cited by 14 •

2020

Glutathione S-transferases (GSTs) are detoxification enzymes involved in the metabolism of numerous chemotherapeutic drugs. Overexpression of GSTs is correlated with cancer chemotherapy resistance. One way to counter this phenotype is to use inhibitors. This protocol describes a method using a spectrophotometric assay to screen for potential GST inhibitors.

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