Advances in glutathione S-transferases research
- VernacularTitle:谷胱甘肽硫-转移酶研究进展
- Author:
Lihong NIE
;
Shengyong WANG
;
Yiling HU
- Publication Type:Journal Article
- Keywords:
Glutathione transferases;
Noeplasms;
Molecular structure
- From:
Chinese Journal of Pathophysiology
2000;0(11):-
- CountryChina
- Language:Chinese
-
Abstract:
Glutathione S-transferases(GSTs) are a family of soluble detoxification enzymes which use reduced glutathione(GSH) in conjugation and reduction reactions.Toxic electrophiles,including a variety of carcinogens,are substrates for the GSTs and are more easily excreted into bile or urine after conjugation or reduction .The three-dimensional structures of GSTs from several species,including humans,have been determined.GST activity has been found to present in all human tissues,and expression of the various GST isoenzymes differs in degree in the various tissues. Glutathione S-transferases may play a role in the protection of cells against toxic electrophiles and in the resistance to cancer chemotherapeutic agants.The polymorphisms of GSTs genes are one of the important factors that exercise influence on individual susceptibility to cancer.
