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INTERACTION OF PAH-RELATED COMPOUNDS WITH THE ALPHA AND BETA ISOFORMS OF ESTROGEN RECEPTOR. (R826192)
Citation:
Fertuck, K. C., S. Kumar, H. C. Sikka, J. B. Matthews, AND T. R. Zacharewski. INTERACTION OF PAH-RELATED COMPOUNDS WITH THE ALPHA AND BETA ISOFORMS OF ESTROGEN RECEPTOR. (R826192). TOXICOLOGY LETTERS. American Chemical Society, Washington, DC, 121(3):167-177, (2001).
Description:
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 17 
-estradiol (E2) for binding to either a glutathione-S-transferase and human ER [small alpha, Greek] D, E, and F domain fusion protein (GST-hER def) or to the full-length human ER 
. Competitive binding was comparable for both isoforms, with IC50 values ranging from 20 to 300 nM (E2 IC50 approximately 3 nM). However, several compounds were able to induce reporter gene expression preferentially through mER , using MCF-7 cells transiently transfected with either a Gal4-human ER def or Gal4-mouse ER def construct, as well as a Gal4-regulated reporter. These data extend the number and type of PAH-related compounds capable of interacting with ER and ER , 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.
Author Keywords: Estrogen receptor; Estrogenic endocrine disruptor; PAHs; Heterocyclic PAHs; Monohydroxy PAHs