Detection of nonopioid β-endorphin receptor in the rat myocardium.

Two selective agonists of nonopioid β-endorphin receptor, synthetic peptides TPLVTLFK (octarphin) and SLTCLVKGFY (immunorphin), were labeled with tritium to specific activity of 29 and 25 Ci/mmol, respectively. Both labeled peptides were found to bind to high-affinity naloxone-insensitive binding sites on the membranes isolated from the rat myocardium (Kd = 2.0 ± 0.2 and 2.5 ± 0.3 nM, respectively). The [(3)H]octarphin specific binding to the myocardial membranes was inhibited by unlabeled β-endorphin (Ki = 1.9 ± 0.2 nM) and immunorphin (Ki = 2.2 ± 0.3 nM). The [(3)H]immunorphin specific binding with the membranes was inhibited by unlabeled β-endorphin (Ki = 2.3 ± 0.3 nM) and octarphin (Ki = 2.4 ± 0.3 nM). The binding specificity study revealed that these binding sites were insensitive not only to naloxone but also to α-endorphin, γ-endorphin, [Met(5)]enkephalin and [Leu(5)]enkephalin. Thus, β-endorphin, immunorphin and octarphin bind to the common high-affinity naloxone-insensitive receptor of the rat myocardial membranes.