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. Author manuscript; available in PMC: 2009 Jan 14.
Published in final edited form as: Eur J Pharmacol. 2007 Oct 2;578(2-3):349–358. doi: 10.1016/j.ejphar.2007.09.029

Figure 3.

Figure 3

Mean competition curves showing α1-adrenoceptor antagonist inhibition of [125I]HEAT binding in membranes from SMG-C10 cells. For each concentration of antagonist, [125I]HEAT binding is expressed as percent of specific binding in the absence of drugs. The competition curves were fit to one- and two-site binding models and mean Ki values (Table 1) were determined from the curve fits. Competition curves for the non-subtype selective antagonist prazosin and the α1D-subtype selective antagonist BMY 7378 fit best to a one-site binding model. In contrast, competition curves for 5-methylurapidil (5-MU) fit significantly better to a two-site model (p < 0.05 using an F test; Table 1) indicating that both α1A- and α1B-adrenoceptors are present in SMG-C10 cells. Each curve is the mean ± S.E.M. of 4-5 individual experiments, each using different SMG-C10 cell cultures.