Radioligand binding of antagonists of platelet‐activating factor to intact human platelets

Abstract
Two new antagonists of platelet‐activating factor (PAF), the pyrrolothiazole derivative 52770 RP and the triazolodiazepine WEB 2086, have been studied as radioligands in intact human platelets. [3H]52770 RP and [3H]WEB 2086 bound specifically to high‐affinity sites with dissociation constants (K d) of 14.8 and 6.1 nM, respectively. The maximal number of sites for [3H]52770 RP binding was approx. 15‐fold higher than for [3H]PAF and [3H]WEB 2086. In addition, C16‐PAF, lyso‐PAF, WEB 2086 and 52770 RP had K i values which were nearly identical for both [3H]PAF and [3H]WEB 2086, whereas only 52770 RP competed for [3H]52770 RP‐binding sites. These results demonstrate that in human platelets the sites of [3H]WEB 2086 binding are identical to [3H]PAF‐binding sites, whereas those of [3H]52770 RP are not. [3H]WEB 2086 appears, therefore, to be a suitable antagonist radioligand for labelling PAF receptors.