Glutathione S-Transferase Polymorphisms and Cancer Susceptibility
Summary
Glutathione S-transferases (GSTs) are a superfamily of phase II detoxification enzymes that protect cells by conjugating electrophilic compounds, including carcinogens, to glutathione. Genetic polymorphisms in GST genes—for example, null variants of GSTM1 and GSTT1 or single-nucleotide changes in GSTP1—can alter enzyme activity or expression. Such variation influences the capacity to detoxify reactive intermediates and modulate redox-sensitive signalling pathways. As a result, individuals harbouring certain GST genotypes may exhibit heightened oxidative stress, DNA damage and inflammation, with downstream effects on tumour initiation, progression and response to therapy. Population studies have revealed associations between specific GST profiles and risk of lung, colorectal, breast and other cancers, underscoring the importance of these enzymes in chemical carcinogenesis. Understanding GST polymorphisms has practical applications in risk stratification, chemoprevention strategies and the design of personalised therapeutic regimens.
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Glutathione S-Transferase Polymorphisms and Cancer Susceptibility publication trend
The graph below shows the total number of articles in glutathione s-transferase polymorphisms and cancer susceptibility across all publications each year (not limited to Nature Index journals).
Technical terms
Glutathione S-Transferase (GST): A family of enzymes that catalyse the conjugation of the tripeptide glutathione to electrophilic substrates, facilitating their detoxification and elimination.
Polymorphism: A genetic variation at a specific locus that exists in multiple forms within a population, potentially affecting gene function or expression.
Phase II metabolism: The biochemical processes in which endogenous molecules (such as glutathione) are conjugated to xenobiotics or metabolic by-products, increasing their solubility and excretion.
Isoenzyme: One of several enzyme variants that catalyse the same reaction but differ in amino-acid sequence, regulatory properties or tissue distribution.
References
- Low-molecular-weight thiol transferases in redox regulation and antioxidant defence. Redox Biology (2024).
- The role of glutathione S-transferases in human disease pathogenesis and their current inhibitors. Genes & Diseases (2024).
- Overexpression of Glutathione S-Transferases in Human Diseases: Drug Targets and Therapeutic Implications. Antioxidants (2023).
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