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The first radiolabeled histamine H3 receptor antagonist, [125I]iodophenpropit: Saturable and reversible binding to rat cortex membranes

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Abstract

We describe the binding to rat cortex membranes of [125I]iodophenpropit, the first radiolabeled histamine H3 antagonist. The binding of [125I]iodophenpropit is selective, saturable, readily reversible, and of high affinity (KD 0.32 nM; Bmax 209 fmol/mg of protein). Specific binding at a concentration of 0.3 nM accounted for 45–55% of the total binding. [125I]Iodophenpropit seems to fulfill the criteria for a suitable ligand for histamine H3 receptor binding studies.

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    Citation Excerpt :

    Moreover, clobenpropit and thioperamide have been reported to have significant affinities for the human histamine H4 receptor (O'Reilly et al., 2002; Esbenshade et al., 2003) that would be expected to limit their utility. Two additional radioligands, [125I]iodophenpropit (Jansen et al., 1992) and [3H]S-methylthioperamide (Yanai et al., 1994) have also been described as antagonist radioligands for the H3 histamine receptor. However, these H3 receptor radioligands exhibited lower signal to noise ratios and are also not commercially available.

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