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Ligand modulation of [35S]GTPgammaS binding at human alpha2A, alpha2B and alpha2C adrenoceptors.

Audinot V, Fabry N, Nicolas JP, Beauverger P, Newman-Tancredi A, Millan MJ, Try A, Bornancin F, Canet E, Boutin JA.
Cell Signal. 2002 Oct;14(10):829-37.

Affinities and efficacies of chemically diverse ligands--some of them used as clinical agents--were examined, employing [3H]RX821,002 and [35S]GTPgammaS binding assays, respectively, at human (h) cloned, halpha2A, halpha2B and halpha2C adrenoceptors (AR) expressed in Chinese hamster ovary (CHO) cells. As compared to noradrenaline (NA, efficacy defined as 100%), the majority of the 13 agonists tested generally behaved as partial agonists. Amongst 18 antagonists, pKB and pKi values, which were highly correlated for each alpha2-AR subtype, failed to reveal any strikingly selective agents. Inverse agonist properties were not detected for any antagonist, consistent with a lack of constitutive activity suggested by the monophasic inhibition of [35S]GTPgammaS binding by GTPgammaS. These data should facilitate interpretation of experimental and clinical actions of adrenergic agonists. Moreover, they emphasize the continuing need for alpha2-AR subtype-selective antagonists in order to define further the roles and therapeutic relevance of halpha2A-, halpha2B-, and halpha2C-AR.