Glutathione S-Transferase Polymorphisms and Their Biological Consequences

J. D. Hayes (Lead / Corresponding author), R. C. Strange

    Research output: Contribution to journalArticlepeer-review

    747 Citations (Scopus)

    Abstract

    Two supergene families encode proteins with glutathione S-transferase (GST) activity: the family of soluble enzymes comprises at least 16 genes; the separate family of microsomal enzymes comprises at least 6 genes. These two GST families are believed to exert a critical role in cellular protection against oxidative stress and toxic foreign chemicals. They detoxify a variety of electrophilic compounds, including oxidized lipid, DNA and catechol products generated by reactive oxygen species-induced damage to intracellular molecules. An increasing number of GST genes are being recognized as polymorphic. Certain alleles, particularly those that confer impaired catalytic activity (e.g. GSTM1*0, GSTT1*0), may be associated with increased sensitivity to toxic compounds. GST polymorphisms may be disease modifying; for example, in subgroups of patients with basal cell carcinoma or bronchial hyper-responsiveness, certain GST appear to exert a statistically significant and biologically relevant impact on disease susceptibility.

    © 2000 S. Karger AG, Basel
    Original languageEnglish
    Pages (from-to)154-166
    JournalPharmacology
    Volume61
    Issue number3
    DOIs
    Publication statusPublished - 2000

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