Get access

Detection of nonopioid β-endorphin receptor in the rat myocardium

Authors


Elena V. Navolotskaya, Branch of Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, Science Avenue, 6, Pushchino, Moscow Region 142290, Russia. E-mail: navolotskaya@fibkh.serpukhov.su

Abstract

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 [3H]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 [3H]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, [Met5]enkephalin and [Leu5]enkephalin. Thus, β-endorphin, immunorphin and octarphin bind to the common high-affinity naloxone-insensitive receptor of the rat myocardial membranes. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.

Ancillary