Similar ligand binding in recombinant human α2C2-adrenoceptors produced in mammalian, insect and yeast cells

Anne Marjamäki, Katariina Pohjanoksa, Sari Ala-Uotila, Dorothea Sizmann, Christian Oker-Blom, Hitoshi Kurose, Mika Scheinin

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)117-121
Number of pages5
JournalEuropean Journal of Pharmacology: Molecular Pharmacology
Issue number1
Publication statusPublished - Mar 15 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Pharmacology

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