Semin Liver Dis 1998; 18(4): 345-358
DOI: 10.1055/s-2007-1007169
ORIGINAL ARTICLE

© 1998 by Thieme Medical Publishers, Inc.

Human Glutathione S-Transferases

Richard Whalen, Thomas D. Boyer
  • Department of Medicine, Division of Digestive Diseases, Emory University School of Medicine, Atlanta, Georgia
Further Information

Publication History

Publication Date:
16 April 2008 (online)

ABSTRACT

Human glutathione S-transferases (GSTs) are a functionally diverse family of soluble enzymes of detoxification that use reduced glutathione (GSH) in conjugation and reduction reactions. Toxic electrophiles, including a variety of carcinogens, are substrates for the GSTs and after conjugation or reduction they are more easily excreted into bile or urine. Many of the GSTs have been cloned, and the three-dimensional structures of GSTs from several species, including humans, have been determined. These data have provided significant insight into how the GSTs function as enzymes. Many GST substrates are inducers of GST gene expression; nonsubstrate inducers include H2O2 and other reactive oxygen species. The regulatory elements of several human GST genes have been partially characterized, and the regulation of the GSTs in humans appears to be very different from that in rodents. Several polymorphisms of GST expression occur commonly in humans and have been associated with an increased susceptibility to certain cancers, particularly when combined with other genetic and environmental factors such as smoking. The role of GSTs in protecting cells from injury by toxic electrophiles continues to be developed.