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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The pure antiestrogen ICI 182,780 binds to a high-affinity site distinct from the estrogen receptor.

Both estrogen receptor-positive ( ER+), tamoxifen-sensitive (5-21) and tamoxifen-resistant (5-23) subclones of the parental MCF-7 breast cancer cell line were used in competitive ligand binding studies involving either [3H]ICI 182,780 or 4-OH-[3H]tamoxifen (4OHT) displacement by unlabelled estradiol (E2) or the antiestrogens (AE) 4OHT and ICI 182,780. Neither radioligand was displaced significantly by E2 over a range of concentrations; binding was predominantly inhibited by the corresponding radio-inert ligand. Scatchard analysis of the data revealed that the binding capacities of both cell lines for ICI 182,780 were approximately 7-fold greater than the previously determined number of ER sites per cell, with the affinity being an order of magnitude less than that of E2 for ER. No difference was found between the TAM-sensitive and -resistant cells in their binding of either AE. When cells were preincubated with either E2, TAM or 4OHT at a high, fixed concentration to block the ER or AE binding sites (AEBS), respectively, displaceable binding of [3H]ICI 182,780 was still observed, indicating binding at a site other than the classical ER or previously described AEBS. Our results suggest that there is a specific, saturable and relatively high-affinity binding site for ICI 182,780 in MCF 5-21 and MCF 5-23 breast cancer cells. However, the physiological relevance of this binding site requires further clarification because in cell growth assays, E2 (at 1/10 the dose of ICI 182,780) overcame the inhibitory effect of the antiestrogen in both of the cell lines.[1]


  1. The pure antiestrogen ICI 182,780 binds to a high-affinity site distinct from the estrogen receptor. Parisot, J.P., Hu, X.F., Sutherland, R.L., Wakeling, A., Zalcberg, J.R., DeLuise, M. Int. J. Cancer (1995) [Pubmed]
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