Insect glutathione transferases and insecticide resistance
Article first published online: 21 JAN 2005
Insect Molecular Biology
Volume 14, Issue 1, pages 3–8, January 2005
How to Cite
Enayati, A. A., Ranson, H. and Hemingway, J. (2005), Insect glutathione transferases and insecticide resistance. Insect Molecular Biology, 14: 3–8. doi: 10.1111/j.1365-2583.2004.00529.x
- Issue published online: 21 JAN 2005
- Article first published online: 21 JAN 2005
- doi: 10.1111/j.1365-2583.2004.00529.x; Received 30 April 2004; accepted after revision 20 August 2004.
- insecticide resistance;
- glutathione transferases
Glutathione transferases (GSTs) are a diverse family of enzymes found ubiquitously in aerobic organisms. They play a central role in the detoxification of both endogenous and xenobiotic compounds and are also involved in intracellular transport, biosynthesis of hormones and protection against oxidative stress. Interest in insect GSTs has primarily focused on their role in insecticide resistance. GSTs can metabolize insecticides by facilitating their reductive dehydrochlorination or by conjugation reactions with reduced glutathione, to produce water-soluble metabolites that are more readily excreted. In addition, they contribute to the removal of toxic oxygen free radical species produced through the action of pesticides. Annotation of the Anopheles gambiae and Drosophila melanogaster genomes has revealed the full extent of this enzyme family in insects. This mini review describes the insect GST enzyme family, focusing specifically on their role in conferring insecticide resistance.