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. 2010 Sep;78(3):511–523. doi: 10.1124/mol.110.064493

Fig. 2.

Fig. 2.

Characterization of the binding and functional properties of ABA-X-BY630 at the human adenosine A1 receptor. a, ABA-X-BY630 mediated a robust, concentration-dependent increase in intracellular calcium mobilization (○) and ERK1/2 phosphorylation (●) in CHO-A1 cells. Data are expressed as a percentage of the response mediated by 1 μM NECA and represent the mean ± S.E.M. from four experiments. b, a confocal image showing discrete membrane binding of 30 nM ABA-X-BY630 at CHO-A1 cells. Association and dissociation kinetics of 10 (closed gray circle), 30 (○), and 100 (●) nM ABA-X-BY630 at CHO-A1 (c) and CHO-NT (d) cells. Normalized association (e) and dissociation (f) kinetics of 10 (closed gray circle), 30 (○), and 100 (●) nM ABA-X-BY630 at CHO-A1 cells. For the purposes of direct comparison, confocal configurations remained constant for both total and nonspecific binding. Confocal fluorescence and phase images were obtained at 2-s intervals for the duration of the experiment. Data represent the mean ± S.E.M. from three to six separate experiments in which each replicate reflects the fluorescence intensity from the plasma membrane of 10 cells.