Interaction of synthetic peptide octarphin with rat myocardium membranes

  title={Interaction of synthetic peptide octarphin with rat myocardium membranes},
  author={Yu. N. Nekrasova and Yu. A. Zolotarev and Elena V. Navolotskaya},
  journal={Biochemistry (Moscow)},
A selective agonist of non-opioid β-endorphin receptor synthetic peptide octarphin (TPLVTLFK, specific activity 28 Ci/mmol) was prepared. The [3H]octarphin binding to rat myocardium membranes before and after experimental myocardial infarction (EMI) was studied. It was found that [3H]octarphin with high affinity and specificity binds to non-opioid β-endorphin receptor of rat myocardium membranes before EMI: Kd1 value of the [3H]octarphin specific binding to membranes was 1.8 ± 0.2 nM. In 3 h… 
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Interaction of the synthetic peptide octarphin with rat adrenal cortex membranes
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Interaction of synthetic peptide octarphin with human blood lymphocytes
T and B lymphocytes of human blood possess a nonopioid β-endorphin receptor whose binding is provided by the fragment 12–19 (the octarphin sequence).
Octarphin, a nonopioid peptide of opioid origin
The data on the properties and the mechanism of action of the peptide octarphin, a selective agonist of the nonopioid (insensitive to the opioid antagonist naloxone) β-endorphin receptor detected on cells of the immune (peritoneal macrophages), endocrine (adrenal cortex, pituitary), and cardiovascular systems (cardiomyocytes) have been analyzed and systematized.
Interaction of synthetic peptide octarphin (TPLVTLFK) with human blood lymphocytes
Both T and B lymphocytes from normal human blood express non‐opioid receptor for β‐endorphin, and tests of the specificity of the receptors revealed that they are not sensitive to naloxone, α‐endomorphin, γ‐end Morphin, [Met5]enkephalin, and [Leu5] enkephaline.
Synthetic peptide TPLVTLFK (octarphin) reduces the corticosterone production by rat adrenal cortex through nonopioid β‐endorphin receptor
Octarphin decreases the adrenal cortex functional activity through the high affinity binding to nonopioid receptor of β‐endorphin.
The second life of antibodies
Fragments of the H-chain of IgG produced as a result of enzymatic cleavage of Igg within the antigen-antibody complex were discovered, synthesized, and studied and their role in regulating the immune response is analyzed.
Effect of Processes Occurring in the Presence of Metal Catalysts on the Main Characteristics of the Hydrogen Isotope Labeled Organic Compounds Obtained
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Binding of synthetic peptide TPLVTLFK to nonopioid beta‐endorphin receptor on rat brain membranes
Octarphin binds with a high affinity and specificity to nonopioid receptor of β‐endorphin on rat brain cortex membranes.
Elucidation and Characteristics of Non-opioid β-Endorphin Receptors in Rat Adrenal Cortex
Investigation of the detection and characterization of nonopioid β-endorphin receptors on rat adrenal cortex membranes and intramuscular injection of immunorphin at doses of 10-100 μg/kg was found to reduce the secretion of 11-oxycorticosteroids from the adrenals to the bloodstream.
Characteristics of Non-opioid β-Endorphin Receptor
Tritium-labeled selective agonist of non-opioid β-endorphin receptor, the decapeptide immunorphine, with specific activity of 24 Ci/mmol has been prepared and revealed and characterized on mouse peritoneal macrophages and rat myocardium, spleen, adrenal, and brain membranes.
Immunostimulating effect of the synthetic peptide octarphin corresponding to β-endorphin fragment 12–19
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Binding of synthetic fragments of β‐endorphin to nonopioid β‐endorphin receptor
The ability to inhibit the [3H]immunorphin specific binding to macrophages was studied and unlabeled fragment 12–19 (TPLVTLFK, the author's name of the peptide octarphin) was found to be the shortest peptide possessing practically the same inhibitory activity as β‐endorphin.
β-Endorphin-like Peptide SLTCLVKGFY Is a Selective Agonist of Nonopioid β-Endorphin Receptor
It has been found that β-END and IMN bind to common NAL-insensitive binding sites on T lymphocytes and enhance Con A-induced proliferation of these cells.
Effect of Synthetic β-Endorphin-Like Peptide Immunorphin on Human T Lymphocytes
β-endorphin and immunorphin interact with common naloxone insensitive receptors on T lymphocytes and stimulate concanavalin A-induced proliferation of T lymphocyte proliferation from the blood of healthy donors.
Specific nonopiate receptors for beta-endorphin.
Iodinated beta H-[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes, which suggests the existence of a specific, non-opiate binding site (receptor) for beta- endorphin.