Author(s): Vos RM, Van Bladeren PJ
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Abstract The glutathione S-transferases (GST) are a family of isoenzymes serving a major role in the biotransformation of many reactive compounds. The isoenzymes from rat, man and mouse are divided into three classes, alpha, mu and pi, on the basis of similar structural and enzymatic properties. In view of the fact that the individual isoenzymes demonstrate differential though overlapping substrate selectivities, the extent to which biotransformation occurs is dependent on the actual profile of isoenzymes present. Consequently, both genetic factors as well as external factors causing changes in the levels or activities of individual isoenzymes are of relevance with respect to an individual's susceptibility towards electrophilic compounds. This review article deals with a number of determinants of GST isoenzyme patterns and/or activities, including tissue distribution, developmental patterns, hormonal influences, induction and inhibition. In addition, current knowledge on specific properties of class alpha, class mu and class pi isoenzymes is presented.
This article was published in Chem Biol Interact
and referenced in Metabolomics:Open Access