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Phorbol ester regulation of the human γ-glutamyltransferase gene promoter

Abstract : In the present study the molecular mechanisms underlying tetradecanoylphorbol-13-acetate (TPA) mediated regulation of the human gamma-glutamyltransferase (GGT) gene were examined. TPA challenge of HeLa cells resulted in an increase of GGT mRNA and enzyme activity. Deletion analysis of the promoter revealed that the -348 to +60 fragment was able to mediate TPA induced expression. Gel shift and supershift analyses showed that TPA treatment increased nuclear protein binding to a putative AP-1 site (-225 to -214) and that c-Jun was part of the complex. This AP-1 element, when cloned either in its native arrangement or as tandem repeat 5' of the minimal thymidine kinase promoter, mediated a significant increase of luciferase activity after TPA treatment of transfected HeLa cells, while its mutated counterpart abolished the induction. The same AP-1 element was able to mediate TPA induced expression in HepG2 cells. Collectively these results indicate that like other GSH metabolising enzymes, GGT too is a target for AP-1 mediated regulation.
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Contributor : Athanase Visvikis Connect in order to contact the contributor
Submitted on : Monday, August 26, 2019 - 10:50:32 AM
Last modification on : Saturday, September 7, 2019 - 1:11:31 AM

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Sandrine Daubeuf, Annelyse Duvoix, Maria Wellman-Rousseau, Marc Diederich, Athanase Visvikis. Phorbol ester regulation of the human γ-glutamyltransferase gene promoter. Biochemical and Biophysical Research Communications, Elsevier, 2004, 313 (2), pp.300-307. ⟨10.1016/j.bbrc.2003.11.121⟩. ⟨hal-02270671⟩



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