Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10566849 | Bioelectrochemistry | 2005 | 8 Pages |
Abstract
The goal of this study was to determine the effects of various compounds on the 17-β-estradiol-induced dimerization of the human estrogen receptor alpha (hERα), a nuclear transcription factor. For this purpose, we used a modified yeast two-hybrid (YTH) bioassay designed to study protein-protein interactions, based on the electrochemical monitoring of hERα dimerization and detected as β-d-galactosidase reporter gene activity in a synthetic substrate p-aminophenyl-β-d-galactopyranoside (pAPG). Compared with 17-β-estradiol activity, genistein, bisphenol-A (BPA), and naringenin induced dimerization to a lower extent by four, five and six magnitudes of orders of magnitude, respectively. In the presence of physiological concentrations of 17-β-estradiol, both tamoxifen and the analgesic drug acetaminophen inhibited hER dimerization in an antiestrogenic manner.
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Physical Sciences and Engineering
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Authors
Adrian Schwartz-Mittelman, Anat Baruch, Tova Neufeld, Virginia Buchner, Judith Rishpon,