Human glutathione S-transferases

Richard Whalen, Thomas D. Boyer

Research output: Contribution to journalReview article

140 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)345-358
Number of pages14
JournalSeminars in Liver Disease
Volume18
Issue number4
DOIs
StatePublished - Jan 1 1998

Keywords

  • Enzyme induction
  • Glutathione S-transferases
  • Polymorphisms

ASJC Scopus subject areas

  • Hepatology

Fingerprint Dive into the research topics of 'Human glutathione S-transferases'. Together they form a unique fingerprint.

  • Cite this