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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/1845
Title: Interaction of Omega, Sigma, and Theta glutathione transferases with p38b mitogen-activated protein kinase from the fruit fly, Drosophila melanogaster.
Authors: Wongtrakul, J.
Janphen, K.
Saisawang, C.
Ketterman, AJ.
Mahidol University. Institute of Molecular Biosciences
Keywords: Interaction of Omega;Sigma;Theta glutathione;p38b;mitogen-activated;Drosophila melanogaster;Open Access article
Issue Date: 2014
Citation: Journal of Insect Science. Vol.14, No.60 (2014), 1-13
Abstract: Glutathione S-transferases (GSTs) are a diverse family of phase II detoxification enzymes found in almost all organisms. Besides playing a major role in the detoxification of xenobiotic and toxic compounds, GSTs are also involved in the regulation of mitogen activated protein (MAP) kinase signal transduction by interaction with proteins in the pathway. An in vitro study was performed for Theta, Omega, Sigma GSTs and their interaction with MAP kinase p38b protein from the fruit fly Drosophila melanogaster Meigen (Diptera: Drosophilidae). The study included the effects of all five Omega class GSTs (DmGSTO1, DmGSTO2a, DmGSTO2b, DmGSTO3, DmGSTO4), all five Theta class GSTs (DmGSTT1, DmGSTT2, DmGSTT3a, DmGSTT3b, DmGSTT4), and one Sigma class glutathione transferase on the activity of Drosophila p38b, including the reciprocal effect of this kinase protein on glutathione transferase activity. It was found that DmGSTT2, DmGSTT3b, DmGSTO1, and DmGSTO3 activated p38b significantly. Substrate specificities of GSTs were also altered after co-incubation with p38b. Although p38b activated DmGSTO1, DmGSTO2a, and DmGSTT2, it inhibited DmGSTT3b and DmGSTO3 activity toward xenobiotic and physiological substrates tested. These results suggest a novel link between Omega and Theta GSTs with the p38b MAP kinase pathway.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/1845
metadata.dc.identifier.url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4207522/pdf/031.014.60.pdf
ISSN: 1536-2442
Appears in Collections:MB-Article

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