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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1989-7-12
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pubmed:abstractText |
The 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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-hydroxyestradiol,
http://linkedlifedata.com/resource/pubmed/chemical/4-hydroxyestradiol-17 beta,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens, Catechol,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-4731
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
485-92
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2542691-Binding, Competitive,
pubmed-meshheading:2542691-Breast Neoplasms,
pubmed-meshheading:2542691-Centrifugation, Density Gradient,
pubmed-meshheading:2542691-Cytosol,
pubmed-meshheading:2542691-Estradiol,
pubmed-meshheading:2542691-Estrogens, Catechol,
pubmed-meshheading:2542691-Female,
pubmed-meshheading:2542691-Humans,
pubmed-meshheading:2542691-Kinetics,
pubmed-meshheading:2542691-Receptors, Estrogen,
pubmed-meshheading:2542691-Tumor Cells, Cultured
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pubmed:year |
1989
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pubmed:articleTitle |
Binding of 2-hydroxyestradiol and 4-hydroxyestradiol to estrogen receptors from human breast cancers.
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pubmed:affiliation |
Department of Biochemistry, University of Louisville, KY 40292.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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