【摘 要】
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Glutathione S-transferases (GSTs,EC 2.5.1.18) are a family of super enzymes with multiple functions,and play a major role in detoxification of endogenous and xenobiotic compounds.In our previous study
【机 构】
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State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
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Glutathione S-transferases (GSTs,EC 2.5.1.18) are a family of super enzymes with multiple functions,and play a major role in detoxification of endogenous and xenobiotic compounds.In our previous study,we have predicted twenty-three putative cytosolic GSTs in the silkworm genome by bioinformatics method.In this study we cloned and studied the epsilon-class GST gene,GSTe4,from the silkworm,Bombyx mori.We found that the recombinant GSTe4 (Bac-BmGSTe4) was functionally overexpressed in sf9 cell lines,and had effective GST activity.The expression of BmGSTe4 was especially down-regulated after the silkworms were fumigated with or licked phoxim.Moreover,BmGSTe4 overexpression in HEK293 cell lines led to inhibition of apoptosis.Thus,our results showed that BmGSTe4 has GST activity,is sensitive to phoxim,and plays a role in inhibition of apoptosis.
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