Ligand binding properties were investigated in recombinant human α2C2-adrenoceptors expressed in three different host systems: Shionogi S115 mouse mammary tumour cells, Spodoptera frugiperda Sf9 insect cells and Saccharomyces cerevisae yeast cells. The expected 43 kDa α2C2 protein was visualized with immunoblotting using a polyclonal α2C2-receptor antibody. [3H]Rauwolscine binding in cell homogenates or membranes (Bmax 3-11 pmol/mg protein; Kd approximately 5.5 nM) was inhibited by prazosin, oxymetazoline, RX821002, chlorpromazine and (-)-noradrenaline with and without the GTP-analogue Gpp(NH)p with similar Ki values in the different host systems. This indicates that α2C2-adrenoceptors retain their binding characteristics irrespective of the host environment.
|Number of pages||5|
|Journal||European Journal of Pharmacology: Molecular Pharmacology|
|Publication status||Published - Mar 15 1994|
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