Synthetic peptide TPLVTLFK (octarphin) reduces the corticosterone production by rat adrenal cortex through nonopioid β‐endorphin receptor

@article{Nekrasova2012SyntheticPT,
  title={Synthetic peptide TPLVTLFK (octarphin) reduces the corticosterone production by rat adrenal cortex through nonopioid $\beta$‐endorphin receptor},
  author={Yu. N. Nekrasova and Yu. A. Zolotarev and Elena V. Navolotskaya},
  journal={Journal of Peptide Science},
  year={2012},
  volume={18}
}
The synthetic peptide octarphin (TPLVTLFK) corresponding to the sequence 12–19 of β‐endorphin, a selective agonist of nonopioid β‐endorphin receptor, was labeled with tritium to a specific activity of 29 Ci/mmol. [3H]Octarphin was found to bind to high‐affinity naloxone‐insensitive binding sites on membranes isolated from rat adrenal cortex (Kd = 35.7 ± 2.3 nM, Bmax = 41.0 ± 3.6 pmol/mg protein). The binding specificity study revealed that these binding sites were insensitive not only to… 
5 Citations
Interaction of synthetic peptide octarphin (TPLVTLFK) with human blood lymphocytes
TLDR
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.
Interaction of synthetic peptide octarphin with human blood lymphocytes
TLDR
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).
The second life of antibodies
TLDR
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.
Use of deuterium labeling by high-temperature solid-state hydrogen-exchange reaction for mass spectrometric analysis of bradykinin biotransformation.
TLDR
Quantitative assays demonstrated applicability of the heavy peptide for both sequencing and quantification of generated fragments of bradykinin and its in vitro degradation metabolites.

References

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Binding of synthetic peptide TPLVTLFK to nonopioid beta‐endorphin receptor on rat brain membranes
TLDR
Octarphin binds with a high affinity and specificity to nonopioid receptor of β‐endorphin on rat brain cortex membranes.
Binding of synthetic fragments of β‐endorphin to nonopioid β‐endorphin receptor
TLDR
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.
Immunostimulating effect of the synthetic peptide octarphin corresponding to β-endorphin fragment 12–19
TLDR
Octarphin was shown to stimulate activity of murine immuno-competent cells in vitro and in vivo and enhanced the adhesion and spreading of peritoneal macrophages as well as their ability to digest bacteria of Salmonella typhimurium virulent strain 415 in vitro.
β-Endorphin-like Peptide SLTCLVKGFY Is a Selective Agonist of Nonopioid β-Endorphin Receptor
TLDR
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.
Detection of nonopioid β‐endorphin receptor in the rat myocardium
TLDR
Two selective agonists of nonopioid β‐endorphin receptor, synthetic peptides TPLVTLFK (octarphin) and SLTCLVKGFY (immunorphin), were found to bind to high‐affinity naloxone‐insensitive binding sites on the membranes isolated from the rat myocardium.
The synthetic peptide octraphin TPLVTLFK is a selective agonist of nonopioid β-endorphin receptor
TLDR
Octarphin is a selective agonist of nonopioid (insensitive to the opioid antagonist naloxone) β-endorphin receptor of rat brain cortex membranes and mouse peritoneal macrophages and stimulates activity of mouse immunocompetent cells in vitro.
Interaction of synthetic peptide octarphin with rat myocardium membranes
TLDR
The results indicate participation of non-opioid β-endorphin receptor in the regulation of myocardial activity.
Beta-endorphin binding to naloxone-insensitive sites on a human mononuclear cell line (U937): effects of cations and guanosine triphosphate.
TLDR
Although naloxone insensitive, beta-endorphin binds to sites on human U937 cells similar to those observed on normal murine splenocytes that exhibit properties, such as size, salt sensitivity, and coupling to a GTP-binding protein, that are similar toThose observed for agonist binding to brain opiate receptors.
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