Interaction of synthetic peptide octarphin with rat myocardium membranes

• Published in: Biochemistry (Moscow) Vol. 76; no. 12; pp. 1337 - 1341
• Main Authors: Nekrasova, Y. N., Zolotarev, Y. A., Navolotskaya, E. V.
• Format: Journal Article
• Language: English
• Published: Dordrecht SP MAIK Nauka/Interperiodica 01.12.2011; Springer; Springer Nature B.V
• Subjects: Animals; Beta-endorphin; Biochemistry; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Cell Membrane - chemistry; Cell Membrane - metabolism; Heart; Humans; Intermedin; Kinetics; Life Sciences; Male; Membranes; Microbiology; Myocardial Infarction - metabolism; Myocardium - chemistry; Myocardium - metabolism; Oligopeptides - chemistry; Oligopeptides - metabolism; Peptides; Protein Binding; Rats; Rats, Sprague-Dawley; Receptors, Opioid - agonists; Receptors, Opioid - chemistry; Receptors, Opioid - metabolism; Rodents; naloxone; peptide; β-endorphin; myocardium; receptor
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297911120066

A selective agonist of non-opioid β-endorphin receptor synthetic peptide octarphin (TPLVTLFK, specific activity 28 Ci/mmol) was prepared. The [ 3 H]octarphin binding to rat myocardium membranes before and after experimental myocardial infarction (EMI) was studied. It was found that [ 3 H]octarphin with high affinity and specificity binds to non-opioid β-endorphin receptor of rat myocardium membranes before EMI: K d1 value of the [ 3 H]octarphin specific binding to membranes was 1.8 ± 0.2 nM. In 3 h after EMI a sharp lowering in affinity of the binding is observed ( K d2 = 13.3 ± 0.4 nM), and in 48 h its almost complete restoration ( K d4 = 2.2 ± 0.3 nM). The results indicate participation of non-opioid β-endorphin receptor in the regulation of myocardial activity.