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Glutathione S-transferases--a review
1Chemistry Department, Swinburne University of Technology, John St., Hawthorn, 3122, Australia.
Current Medicinal Chemistry
|April 2, 1999
Summary
Glutathione S-transferases (GSTs) are key in detoxification but can cause multi-drug resistance in cancer chemotherapy. Targeting specific GST isoforms offers a promising strategy for cancer treatment.
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Glutathione S-transferases (GSTs) are crucial enzymes for cellular detoxification of harmful compounds.
- GSTs are classified into subclasses (alpha, mu, pi, theta) based on sequence and immunological properties.
- Their catalytic mechanism involves conjugation with glutathione (GSH), producing less toxic, excretable products.
Purpose of the Study:
- To review the literature on GST classes, their functions, and mechanisms.
- To explore the role of GSTs in multi-drug resistance during cancer chemotherapy.
- To discuss GSTs as potential therapeutic targets for disease treatment.
Main Methods:
- Literature review of studies on GST structure, function, and classification.
- Analysis of X-ray crystallography and site-directed mutagenesis data for GSTs.
- Examination of research on GST expression patterns in normal and tumor cells.
Main Results:
- GSTs exhibit high specificity for GSH but variable substrate specificity.
- Increased GST levels, particularly p-GST, are observed in tumor cells, contributing to multi-drug resistance.
- Isoform-specific expression patterns vary across tissues and cell types.
Conclusions:
- Understanding GST isoform expression and substrate specificity is vital for deciphering their role in drug resistance.
- Targeting GSTs with specific inhibitors presents a promising therapeutic strategy against cancer.
- Further research into GSTs can lead to novel approaches in disease treatment and chemotherapy enhancement.