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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

[3H]RX821002 (2-methoxyidazoxan) binds to alpha 2-adrenoceptor subtypes and a non-adrenoceptor imidazoline binding site in rat kidney.

The binding of [3H]RX821002 (2-methoxyidazoxan) was evaluated in rat kidney membranes. [3H]RX821002 (0.13-16 nM) recognized a single, saturable binding site with high affinity. Different binding site densities were calculated depending on non-specific binding as defined by (-)-adrenaline or RX821002 (10 microM). Competition assays using (-)-adrenaline and the subtype-selective drugs ARC 239 (2-[2-[4-(o-methoxyphenyl)-piperazin-1-yl]-ethyl]-4,4-dimethyl-1,3 (2H,4H)-isoquinolindione), BRL 44408 (2-[2H-(1-methyl-1,3-dihydroisoindole)methyl]-4,5-dihydroimidaz ole), oxymetazoline or prazosin for [3H]RX821002 binding sites revealed the presence of alpha 2B-adrenoceptors (33-51%), alpha 2D-adrenoceptors (15-28%) and an adrenaline-insensitive population (34-40%), sensitive to imidazolines. After the addition of (-)-adrenaline (3 microM) to mask alpha 2-adrenoceptors, [3H]RX821002 specifically identified a saturable binding site with high affinity (Kd = 4.9 +/- 1.5 nM). The pharmacological profile of this non-adrenoceptor, [3H]RX821002 binding site (potencies: efaroxan > clonidine > guanabenz > BRL 44408 > ARC 239 > BU 224 (2-(4,5-dihydroimidaz-2-yl)quinoline) > moxonidine > (-)-nor-adrenaline > cimetidine) is different to that of imidazoline I1 or imidazoline I2 binding sites. Alternative incubation in the presence of ARC 239 (50 nM) to mask alpha 2B-adrenoceptors or BRL 44408 (100 nM) to mask alpha 2D-adrenoceptors confirmed the existence of both alpha 2-adrenoceptor subtypes and a non-adrenoceptor imidazoline binding site.[1]


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