GLUTATHIONE TRANSFERASES
John D. Hayes, Jack U. Flanagan, Ian R. Jowsey
The Annual Review of Pharmacology and Toxicology
Abstract
▪ Abstract This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β-unsaturated aldehydes, quinones, epoxides, and hydroperoxides formed as secondary metabolites during oxidative stress. These enzymes are also intimately involved in the biosynthesis of leukotrienes, prostaglandins, testosterone, and progesterone, as well as the degradation of tyrosine. Among their substrates, GSTs conjugate the signaling molecules 15-deoxy-Δ 12,14 -prostaglandin J 2 (15d-PGJ 2 ) and 4-hydroxynonenal with glutathione, and consequen