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Vol. 61, Issue 6, 1273-1283, June 2002
, an
Estrogen-Responsive Element, and the Activator Protein 1 Response
Element
Karo Bio AB, Huddinge, Sweden (T.B., S.N.); and Department of
Medical Nutrition, Novum, Huddinge, Sweden (L.-A.H., J.-A.G.)
The pS2 promoter is complex with binding sites for a number of
protein factors that may participate in modulating its activity. The
pS2 gene was transcriptionally activated by estrogens in
HepG2 cells transformed (HepER3) to express the estrogen receptor 
(ER). The phorbol ester phorbol 12-myristate 13-acetate (PMA) stimulated pS2 expression in both HepER3 and the parental,
non-ER-expressing HepG2 cells, although its activity was substantially
less in HepG2 cells. The use of selective protein kinase inhibitors
suggested that the MAPK pathway contributes substantially to estrogen
stimulation of the pS2 promoter. The activator protein 1 (AP1) site at
332 to 338 in the pS2 promoter had a dominant role in the response to both estrogens and PMA, although the estrogen response element at
393 to 405 was essential to mediate the response to estrogen. The
potentiation of pS2 promoter activity by the AP1 motif in response to
estrogen was dependent on the ligand binding domain of ER.
Furthermore, the presence of an intact AP1 element in the pS2 promoter
sustained suppression of pS2 promoter activity by an LXXLL peptide. In
summary, the data suggest that the effect of estrogen is mediated
through a cross-talk between the estrogen-responsive element and the
AP1 response element and that ER plays a crucial role in mediating
the effect of both estrogen and PMA.
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