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• W1995420714 abstract "The ability of several 4- and 5-ring polycyclic aromatic hydrocarbons (PAHs), heterocyclic PAHs, and their monohydroxy derivatives to interact with the estrogen receptor (ER) alpha and beta isoforms was examined. Only compounds possessing a hydroxyl group were able to compete with 3H-labeled 17beta-estradiol (E2) for binding to either a glutathione-S-transferase and human ERalpha D, E, and F domain fusion protein (GST-hERalphadef) or to the full-length human ERbeta. Competitive binding was comparable for both isoforms, with IC(50) values ranging from 20 to 300 nM (E2 IC(50) approximately 3 nM). However, several compounds were able to induce reporter gene expression preferentially through mERbeta, using MCF-7 cells transiently transfected with either a Gal4-human ERalphadef or Gal4-mouse ERbetadef construct, as well as a Gal4-regulated reporter. These data extend the number and type of PAH-related compounds capable of interacting with ERalpha and ERbeta, and provides additional evidence that even though some compounds may possess a similar affinity for both ER isoforms, the capacity for transcriptional activation can still be isoform-specific." @default.
• W1995420714 created "2016-06-24" @default.
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• W1995420714 date "2001-05-01" @default.
• W1995420714 modified "2023-10-15" @default.
• W1995420714 title "Interaction of PAH-related compounds with the α and β isoforms of the estrogen receptor" @default.
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• W1995420714 doi "https://doi.org/10.1016/s0378-4274(01)00344-7" @default.
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