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pubmed-article:2542691pubmed:abstractTextThe binding of catechol estrogens, epoxyenones and methoxyestrogens was evaluated using estrogen receptors in cytosol prepared from human breast cancers. The relative affinity of 2-hydroxyestradiol, a metabolite formed in vitro from estradiol-17 beta by breast cancer cells, was indistinguishable from that of estradiol-17 beta. 4-Hydroxyestradiol, which is also a metabolite of estradiol-17 beta, associated with the estrogen receptor with a relative affinity approximately 1.5-fold greater than that of estradiol-17 beta. Epoxyenones and methoxyestrogens were weak competitors compared to the binding of estradiol-17 beta, exhibiting relative affinities 3% or less than the affinity of estradiol-17 beta. Sucrose density gradient centrifugation revealed that both 2- and 4-hydroxyestradiol inhibited the binding of estradiol-17 beta to both the 4S and 8S isoforms of the estrogen receptor in a competitive manner, with a Ki = 0.94 nM for 2-hydroxyestradiol and a Ki = 0.48 nM for 4-hydroxyestradiol. It can be concluded that these data demonstrate a specific receptor-mediated estrogenic action for both of these catechol estrogens.lld:pubmed
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pubmed-article:2542691pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:2542691pubmed:articleTitleBinding of 2-hydroxyestradiol and 4-hydroxyestradiol to estrogen receptors from human breast cancers.lld:pubmed
pubmed-article:2542691pubmed:affiliationDepartment of Biochemistry, University of Louisville, KY 40292.lld:pubmed
pubmed-article:2542691pubmed:publicationTypeJournal Articlelld:pubmed
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