Abstract
Ligand binding properties were investigated in recombinant human alpha 2C2-adrenoceptors expressed in three different host systems: Shionogi S115 mouse mammary tumour cells, Spodoptera frugiperda Sf9 insect cells and Saccharomyces cerevisiae yeast cells. The expected 43 kDa alpha 2C2 protein was visualized with immunoblotting using a polyclonal alpha 2C2-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 alpha 2C2-adrenoceptors retain their binding characteristics irrespective of the host environment.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adrenergic alpha-Antagonists / pharmacology
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Amino Acid Sequence
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Animals
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Cells, Cultured
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Chlorpromazine / pharmacology
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Dioxanes / pharmacology
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Humans
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Idazoxan / analogs & derivatives
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Immunoblotting
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Mammary Neoplasms, Experimental / metabolism*
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Mice
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Molecular Sequence Data
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Moths / metabolism*
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Oxymetazoline / pharmacology
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Prazosin / pharmacology
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Receptors, Adrenergic, alpha / drug effects
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Receptors, Adrenergic, alpha / genetics
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Receptors, Adrenergic, alpha / metabolism*
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / metabolism*
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Transfection
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Tumor Cells, Cultured
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Yohimbine / metabolism*
Substances
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Adrenergic alpha-Antagonists
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Dioxanes
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Receptors, Adrenergic, alpha
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Recombinant Proteins
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Yohimbine
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Oxymetazoline
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2-methoxyidazoxan
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Chlorpromazine
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Prazosin
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Idazoxan