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. 2008 May 1;149(8):3881–3889. doi: 10.1210/en.2008-0288

Figure 4.

Figure 4

Regulatory effects of 17β-estradiol on survival kinase expression as a function of ERα concentration. A, Western blot analysis for expression of phosphorylated and total ERK-2 in lysates from HTERα cells treated with increasing amounts of Dox in the presence or absence of 17β-estradiol. Dox treatment alone had no significant effect on ERK2 activation. However, estrogen treatment significantly suppressed pERK2 at the high Dox dose (50 μg/ml). B, Bars represent group means ± sem of the relative OD of pERK2 normalized to total ERK (n = 6 for each treatment condition). *, P < 0.05. C, Dox/17β-estradiol-induced changes in ERK2 phosphorylation were confirmed with the Bio-Plex phosphoprotein assay, indicating again that 17β-estradiol decreased constitutive ERK2 phosphorylation at high ERα expression (n = 6, P < 0.05). D, Dox/17β-estradiol-induced changes in Akt phosphorylation was determined with the Bio-Plex phosphoprotein assay specific for this signaling protein. Bars represent mean ± sem of a single representative experiment, with n = 6 for each treatment condition. The graph represents mean ± sem of phospho-Akt normalized to Akt for each group. 17β-Estradiol increased Akt phosphorylation at low ERα concentrations, but the same dose of estradiol significantly suppressed Akt activation at high ERα expression. *, P < 0.05 (comparisons between vehicle and 17β-estradiol treatment for each Dox dose).