Glutathione S-transferase (GST) is an enzyme that plays a vital role in cellular detoxification processes. It is part of a larger family of Phase II metabolic enzymes and is found in various tissues, especially the liver.
The primary function of GST is to catalyze the binding of the tripeptide glutathione (GSH) to numerous endogenous and exogenous toxic compounds and reactive intermediates, including carcinogens, drugs, and environmental toxins. This conjugation reaction enhances the water solubility of these compounds, allowing them to be easily excreted from the body via urine or bile.
GST enzymes also participate in the biosynthesis of leukotrienes and prostaglandins, important mediators of inflammation and immune responses. They are involved in the regulation of oxidative stress by protecting against harmful reactive oxygen species (ROS) and facilitating the repair of damaged DNA. Additionally, GSTs have been implicated in various cellular signaling pathways, including the regulation of cell growth, apoptosis, and cell cycle progression.
Genetic variations in GST genes can influence enzyme activity, leading to individual differences in drug metabolism, susceptibility to environmental toxins, and disease risk. Therefore, measuring GST activity or genotype is useful in pharmacology and toxicology studies, as well as in understanding the role of GSTs in human health and disease.
Overall, glutathione S-transferases are essential enzymes that play a critical role in cellular detoxification, regulation of oxidative stress, and modulation of various biological processes.
