Glutathione transferases: substrates, inihibitors and pro-drugs in cancer and neurodegenerative diseases

Glutathione transferase classical GSH conjugation activity plays a critical role in cellular detoxification against xenobiotics and noxious compounds as well as against oxidative stress. However, this feature is also exploited by cancer cells to acquire drug resistance and improve their survival. As...

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Veröffentlicht in:Oncogenesis (New York, NY) Jg. 7; H. 1; S. 8 - 15
Hauptverfasser: Allocati, Nerino, Masulli, Michele, Di Ilio, Carmine, Federici, Luca
Format: Journal Article
Sprache:Englisch
Veröffentlicht: London Nature Publishing Group UK 24.01.2018
Nature Publishing Group
Schlagworte:
631/67/1059/153
631/67/1059/2326
Apoptosis
Cancer
Cell Biology
Detoxification
Drug resistance
Glutathione
Glutathione transferase
Human Genetics
Internal Medicine
Medicine
Medicine & Public Health
Mutation
Neurodegeneration
Neurodegenerative diseases
Oncology
Oxidative stress
Prodrugs
Review
Review Article
Xenobiotics
ISSN:2157-9024, 2157-9024
Online-Zugang:Volltext
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Zusammenfassung:Glutathione transferase classical GSH conjugation activity plays a critical role in cellular detoxification against xenobiotics and noxious compounds as well as against oxidative stress. However, this feature is also exploited by cancer cells to acquire drug resistance and improve their survival. As a result, various members of the family were found overexpressed in a number of different cancers. Moreover several GST polymorphisms, ranging from null phenotypes to point mutations, were detected in members of the family and found to correlate with the onset of neuro-degenerative diseases. In the last decades, a great deal of research aimed at clarifying the role played by GSTs in drug resistance, at developing inhibitors to counteract this activity but also at exploiting GSTs for prodrugs specific activation in cancer cells. Here we summarize some of the most important achievements reached in this lively area of research.
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ISSN:2157-9024
2157-9024
DOI:10.1038/s41389-017-0025-3