glutathionStransferase

Glutathione S-transferases (GSTs) are a family of enzymes found in most aerobic organisms. They play a crucial role in detoxification by catalyzing the conjugation of glutathione (GSH) to a wide range of electrophilic substrates. This process, known as glutathione conjugation or S-alkylation, typically makes the substrate more water-soluble and thus easier to excrete from the body. GSTs are involved in the metabolism of numerous endogenous and exogenous compounds, including xenobiotics, drugs, carcinogens, and reactive oxygen species.

The GST superfamily is broadly divided into several distinct classes based on their sequence homology and substrate specificities. These classes include alpha, mu, pi, sigma, theta, and kappa GSTs, among others, each with varying tissue distribution and functions. For instance, pi-class GSTs are often upregulated in response to oxidative stress and are implicated in cancer resistance, while mu-class GSTs are involved in the detoxification of certain environmental pollutants.

Beyond their detoxification roles, GSTs are also involved in cellular signaling, lipid metabolism, and protection against oxidative damage. Their diverse functions highlight their importance in maintaining cellular homeostasis and protecting against a variety of cellular insults. Due to their involvement in drug metabolism and resistance to toxins, GSTs are also a significant area of research in pharmacology and toxicology. Variations in GST gene expression and activity can influence an individual's susceptibility to certain diseases and their response to therapeutic agents.