Interaction of the synthetic peptide octarphin with rat adrenal cortex membranes
The synthetic peptide octarphin (TPLVTLFK, fragment 12–19 of β-endorphin), a selective agonist of the nonopioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [ 3 H]octarphin to rat adrenal cortex membranes was studied under normal conditions...
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| Published in | Biochemistry (Moscow) Vol. 77; no. 12; pp. 1377 - 1381 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Dordrecht
SP MAIK Nauka/Interperiodica
01.12.2012
Springer Springer Nature B.V |
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| Online Access | Get full text |
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| Abstract | The synthetic peptide octarphin (TPLVTLFK, fragment 12–19 of β-endorphin), a selective agonist of the nonopioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [
3
H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [
3
H]octarphin specifically binds to the membranes with high affinity:
K
d1
= 36.3 ± 2.5 nM, B
max1
= 41.0 ± 3.8 pmol/mg protein. The specific binding of [
3
H]octarphin to the membranes was inhibited by unlabeled β-endorphin (
K
i
= 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin (
K
i
= 36.8 ± 3.3 nM). Unlabeled naloxone, [Leu
5
]- and [Met
5
]enkephalins, α- and γ-endorphins, and corticotropin were inactive (
K
i
> 1 μM). Both cold and heat shocks decreased the binding affinity:
K
d2
= 55.6 ± 4.2 nM and
K
d3
= 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β-endorphin receptor of adrenal cortex membranes. |
|---|---|
| AbstractList | The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the non-opioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [³H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [³H]octarphin specifically binds to the membranes with high affinity: [K.sub.d1] = 36.3 ± 2.5 nM, [B.sub.max1] = 41.0 ± 3.8 pmol/mg protein. The specific binding of [³H]octarphin to the membranes was inhibited by unlabeled β-endorphin ([K.sub.i] = 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin ([K.sub.i] = 36.8 ± 3.3 nM). Unlabeled naloxone, [[Leu.sup.5]]- and [[Met.sup.5]]enkephalins, α- and γ-endorphins, and corticotropin were inactive ([K.sub.i] > 1 µM). Both cold and heat shocks decreased the binding affinity: [K.sub.d2] = 55.6 ± 4.2 nM and [K.sub.d3] = 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β- endorphin receptor of adrenal cortex membranes. DOI: 10.1134/S000629791212005X Key words: β-endorphin, naloxone, peptides, receptors, adrenal cortex The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the nonopioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [^sup 3^H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [^sup 3^H]octarphin specifically binds to the membranes with high affinity: K ^sub d1^ = 36.3 ± 2.5 nM, B^sub max1^ = 41.0 ± 3.8 pmol/mg protein. The specific binding of [^sup 3^H]octarphin to the membranes was inhibited by unlabeled β-endorphin (K ^sub i^ = 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin (K ^sub i^ = 36.8 ± 3.3 nM). Unlabeled naloxone, [Leu^sup 5^]- and [Met^sup 5^]enkephalins, α- and γ-endorphins, and corticotropin were inactive (K ^sub i^ > 1 μM). Both cold and heat shocks decreased the binding affinity: K ^sub d2^ = 55.6 ± 4.2 nM and K ^sub d3^ = 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β-endorphin receptor of adrenal cortex membranes.[PUBLICATION ABSTRACT] The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the non-opioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [³H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [³H]octarphin specifically binds to the membranes with high affinity: [K.sub.d1] = 36.3 ± 2.5 nM, [B.sub.max1] = 41.0 ± 3.8 pmol/mg protein. The specific binding of [³H]octarphin to the membranes was inhibited by unlabeled β-endorphin ([K.sub.i] = 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin ([K.sub.i] = 36.8 ± 3.3 nM). Unlabeled naloxone, [[Leu.sup.5]]- and [[Met.sup.5]]enkephalins, α- and γ-endorphins, and corticotropin were inactive ([K.sub.i] > 1 µM). Both cold and heat shocks decreased the binding affinity: [K.sub.d2] = 55.6 ± 4.2 nM and [K.sub.d3] = 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β- endorphin receptor of adrenal cortex membranes. The synthetic peptide octarphin (TPLVTLFK, fragment 12–19 of β-endorphin), a selective agonist of the nonopioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [ 3 H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [ 3 H]octarphin specifically binds to the membranes with high affinity: K d1 = 36.3 ± 2.5 nM, B max1 = 41.0 ± 3.8 pmol/mg protein. The specific binding of [ 3 H]octarphin to the membranes was inhibited by unlabeled β-endorphin ( K i = 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin ( K i = 36.8 ± 3.3 nM). Unlabeled naloxone, [Leu 5 ]- and [Met 5 ]enkephalins, α- and γ-endorphins, and corticotropin were inactive ( K i > 1 μM). Both cold and heat shocks decreased the binding affinity: K d2 = 55.6 ± 4.2 nM and K d3 = 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β-endorphin receptor of adrenal cortex membranes. The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the non-opioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [3H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [(3)H]octarphin specifically binds to the membranes with high affinity: K(d1) = 36.3 ± 2.5 nM, B(max1) = 41.0 ± 3.8 pmol/mg protein. The specific binding of [(3)H]octarphin to the membranes was inhibited by unlabeled β-endorphin (K(i) = 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin (K(i) = 36.8 ± 3.3 nM). Unlabeled naloxone, [Leu(5)]- and [Met(5)]enkephalins, α- and γ-endorphins, and corticotropin were inactive (K(i) > 1 µM). Both cold and heat shocks decreased the binding affinity: K(d2) = 55.6 ± 4.2 nM and K(d3) = 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β-endorphin receptor of adrenal cortex membranes. The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the non-opioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [3H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [(3)H]octarphin specifically binds to the membranes with high affinity: K(d1) = 36.3 ± 2.5 nM, B(max1) = 41.0 ± 3.8 pmol/mg protein. The specific binding of [(3)H]octarphin to the membranes was inhibited by unlabeled β-endorphin (K(i) = 33.9 ± 3.6 nM) and the agonist of the non-opioid receptor decapeptide immunorphin (K(i) = 36.8 ± 3.3 nM). Unlabeled naloxone, [Leu(5)]- and [Met(5)]enkephalins, α- and γ-endorphins, and corticotropin were inactive (K(i) > 1 µM). Both cold and heat shocks decreased the binding affinity: K(d2) = 55.6 ± 4.2 nM and K(d3) = 122.7 ± 5.6 nM, respectively. In both cases, the maximal binding capacity of the receptor did not change. Thus, even a short-term thermal shock significantly affects the sensitivity of the non-opioid β-endorphin receptor of adrenal cortex membranes. |
| Audience | Academic |
| Author | Navolotskaya, E. V. Zolotarev, Y. A. Nekrasova, Y. N. |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23244733$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_peptides_2013_10_001 crossref_primary_10_1134_S0006297914010015 |
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| Copyright | Pleiades Publishing, Ltd. 2012 COPYRIGHT 2012 Springer |
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| Keywords | naloxone peptides β-endorphin receptors adrenal cortex |
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| Snippet | The synthetic peptide octarphin (TPLVTLFK, fragment 12–19 of β-endorphin), a selective agonist of the nonopioid β-endorphin receptor, was labeled with tritium... The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the non-opioid β-endorphin receptor, was labeled with tritium... The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the nonopioid β-endorphin receptor, was labeled with tritium... |
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| SubjectTerms | Adrenal Cortex - cytology Adrenal glands Amino Acid Sequence Animals Beta-endorphin Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Cell Membrane - metabolism Cold Temperature Heat-Shock Response Intermedin Life Sciences Membranes Microbiology Oligopeptides - chemical synthesis Oligopeptides - chemistry Oligopeptides - metabolism Peptides Protein Binding Rats Rats, Wistar Rodents Tritium |
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| Title | Interaction of the synthetic peptide octarphin with rat adrenal cortex membranes |
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