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Glutathione S-Transferase Polymorphisms and Their Biological Consequences

Hayes, John D., Strange, Richard C.·2000·Pharmacology

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.

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Metadata

Authors
Hayes, J. D., & Strange, R. C.
Venue
Pharmacology
Publisher
S. Karger AG
Published
2000
Volume
61
Issue
3
Pages
154-166
ISSN
  • 0031-7012 (ISSN-L)
  • 1423-0313
OpenAlex
W1976346227
Cited by
1,001
References
1
FWCI
9.35
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Glutathione S-Transferase Polymorphisms and Their Biological Consequences. https://app.cochat.ai/papers/10.1159/000028396
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Hayes, J. D., & Strange, R. C. (2000). Glutathione S-Transferase Polymorphisms and Their Biological Consequences. Pharmacology. https://doi.org/10.1159/000028396

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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