Glutathione S-transferases--a review.

摘要: The Glutathione S-transferases (GSTs) form a group of multi-gene isoenzymes involved in the cellular detoxification both xenobiotic and endobiotic compounds. GSTs have been divided into number subclasses, alpha (α), mu (μ), pi (π), theta (θ). classification was made on basis sequence similarity immunological cross-reactivity. show high level specificity toward GSH but electrophilic second substrate can vary significantly between within classes spite their similarity. X-ray crystallography site-directed mutagenesis studies together elucidated structure mechanism GSTs. Catalysis occurs by conjugation with glutathione (GSH) less toxic more hydrophilic products then be partially metabolised excreted. This invaluable service is however disadvantageous during chemotherapy where associated multi-drug resistance tumour cells. Levels expression different isoforms are tissue specific. variations normal cells interest most cases levels increased, especially π-GST. Understanding complex role that play drug begins determining pattern isoform specificities each isoform. use isozyme-specific, analogues as inhibitors to modulate GST activity promising strategy battle against cancer. review attempts provide detailed overview literature concerning GSTs, function therapeutic targets for disease current at time submission