sup. alpha. N-acetyl derivatives of. beta. -endorphin-(1-31) and -(1-27) regulate the supraspinal antinociceptive activity of different opioids in mice

Garzon, J; Sanchez-Blazquez, P

doi:10.1016/0024-3205(91)90439-I

Title: sup. alpha. N-acetyl derivatives of. beta. -endorphin-(1-31) and -(1-27) regulate the supraspinal antinociceptive activity of different opioids in mice

Full Record
Other Related Research

Abstract

{sup {alpha}}N-acetyl human {beta}-endorphin(1-31) injected icv to mice antagonized the analgesic activity of {beta}-endorphin-(1-31) and morphine whereas the analgesia evoked by DADLE and DAGO was enhanced by this treatment. The modulatory activity of {sup {alpha}}N-acetyl {beta}-endorphin-(1-31) was exhibited at remarkable low doses (fmols) reaching a maximum that persisted even though the dose was increased 100,000 times. The regulatory effect of a single dose of the acetylated neuropeptide lasted for 24h. The activity of {sup {alpha}}N-acetyl human {beta}-endorphin(1-31) was partially retained by the shorter peptide {sup {alpha}}N-acetyl human {beta}-endorphin-(1-27) and to a lesser extent by {beta}-endorphin-(1-27), {beta}-endorphin-(1-31) lacked this regulatory activity on opioid analgesia. Acetylated {beta}-endorphin-(1-31) displayed a biphasic curve when competing with 5 pM ({sup 125}I)-Tyr{sup 27} human {beta}-endorphin-(1-31) specific binding, the first step was abolished with an apparent IC{sub 50} of 0.35 nM, and the rest with an IC{sub 50} of 200 nM. It is suggested that {sup {alpha}}N-acetyl {beta}-endorphin-(1-31) changed the efficiency of the opioid analgesics by acting upon a specific substrate that is functionally coupled to the opioid receptor, presumably the guanine nucleotide binding regulatory proteins G{sub i}/G{sub 0}.

Authors:

Garzon, J; Sanchez-Blazquez, P ^[1]

Cajal Institute, Madrid (Spain)

Publication Date:: Tue Jan 01 00:00:00 EST 1991

OSTI Identifier:: 5947300

Resource Type:: Journal Article

Journal Name:: Life Sciences; (USA)

Additional Journal Information:: Journal Volume: 48:14; Journal ID: ISSN 0024-3205

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; ENDORPHINS; RECEPTORS; MORPHINE; BIOLOGICAL EFFECTS; PEPTIDES; BIOCHEMICAL REACTION KINETICS; GUANINE; IODINE 125; MICE; TRACER TECHNIQUES; ALKALOIDS; AMINES; ANALGESICS; ANIMALS; AROMATICS; AUTONOMIC NERVOUS SYSTEM AGENTS; AZAARENES; BETA DECAY RADIOISOTOPES; CENTRAL NERVOUS SYSTEM DEPRESSANTS; DAYS LIVING RADIOISOTOPES; DRUGS; ELECTRON CAPTURE RADIOISOTOPES; HETEROCYCLIC COMPOUNDS; HYDROXY COMPOUNDS; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; MAMMALS; MEMBRANE PROTEINS; NARCOTICS; NEUROREGULATORS; NUCLEI; ODD-EVEN NUCLEI; OPIUM; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; PROTEINS; PURINES; RADIOISOTOPES; REACTION KINETICS; RODENTS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats


                    Garzon, J, and Sanchez-Blazquez, P. sup. alpha. N-acetyl derivatives of. beta. -endorphin-(1-31) and -(1-27) regulate the supraspinal antinociceptive activity of different opioids in mice.  United States: N. p., 1991. 
        Web.  doi:10.1016/0024-3205(91)90439-I.

Copy to clipboard


                    Garzon, J, & Sanchez-Blazquez, P. sup. alpha. N-acetyl derivatives of. beta. -endorphin-(1-31) and -(1-27) regulate the supraspinal antinociceptive activity of different opioids in mice.  United States.  https://doi.org/10.1016/0024-3205(91)90439-I

Copy to clipboard


                    Garzon, J, and Sanchez-Blazquez, P. 1991.  
        "sup. alpha. N-acetyl derivatives of. beta. -endorphin-(1-31) and -(1-27) regulate the supraspinal antinociceptive activity of different opioids in mice".  United States.  https://doi.org/10.1016/0024-3205(91)90439-I.

Copy to clipboard


                    
@article{osti_5947300,

  title        = {sup. alpha. N-acetyl derivatives of. beta. -endorphin-(1-31) and -(1-27) regulate the supraspinal antinociceptive activity of different opioids in mice},

  author       = {Garzon, J and Sanchez-Blazquez, P},

  abstractNote = {{sup {alpha}}N-acetyl human {beta}-endorphin(1-31) injected icv to mice antagonized the analgesic activity of {beta}-endorphin-(1-31) and morphine whereas the analgesia evoked by DADLE and DAGO was enhanced by this treatment. The modulatory activity of {sup {alpha}}N-acetyl {beta}-endorphin-(1-31) was exhibited at remarkable low doses (fmols) reaching a maximum that persisted even though the dose was increased 100,000 times. The regulatory effect of a single dose of the acetylated neuropeptide lasted for 24h. The activity of {sup {alpha}}N-acetyl human {beta}-endorphin(1-31) was partially retained by the shorter peptide {sup {alpha}}N-acetyl human {beta}-endorphin-(1-27) and to a lesser extent by {beta}-endorphin-(1-27), {beta}-endorphin-(1-31) lacked this regulatory activity on opioid analgesia. Acetylated {beta}-endorphin-(1-31) displayed a biphasic curve when competing with 5 pM ({sup 125}I)-Tyr{sup 27} human {beta}-endorphin-(1-31) specific binding, the first step was abolished with an apparent IC{sub 50} of 0.35 nM, and the rest with an IC{sub 50} of 200 nM. It is suggested that {sup {alpha}}N-acetyl {beta}-endorphin-(1-31) changed the efficiency of the opioid analgesics by acting upon a specific substrate that is functionally coupled to the opioid receptor, presumably the guanine nucleotide binding regulatory proteins G{sub i}/G{sub 0}.},

  doi          = {10.1016/0024-3205(91)90439-I},

  url          = {https://www.osti.gov/biblio/5947300},
  journal      = {Life Sciences; (USA)},

  issn         = {0024-3205},

  number       = ,

  volume       = 48:14,

  place        = {United States},

  year         = {Tue Jan 01 00:00:00 EST 1991},

  month        = {Tue Jan 01 00:00:00 EST 1991}

}

Copy to clipboard

Journal Article:

https://doi.org/10.1016/0024-3205(91)90439-I

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Effects of stress and. beta. -funal trexamine pretreatment on morphine analgesia and opioid binding in rats

Journal Article Adams, J; Andrews, J; Hiller, J; ... - Life Sci.; (United States)

This study was essentially an in vivo protection experiment designed to test further the hypothesis that stress induces release of endogenous opiods which then act at opioid receptors. Rats that were either subjected to restraint stress for 1 yr or unstressed were injected ICV with either saline or 2.5 ..mu..g of ..beta..-funaltrexamine (..beta..-FNA), an irreversible opioid antagonist that alkylates the mu-opioid receptor. Twenty-four hours later, subjects were tested unstressed for morphine analgesia or were sacrificed and opioid binding in brain was determined. (/sup 3/H)D-Ala/sup 2/NMePhe/sup 4/-Gly/sup 5/(ol)enkephalin (DAGO) served as a specific ligand for mu-opioid receptors, and (/sup 3/H)-bremazocine asmore »« less
https://doi.org/10.1016/0024-3205(87)90430-9
The opioid receptors of the rat periaqueductal gray

Miscellaneous Fedynyshyn, J

The opioid binding characteristics of the rat (PAG) and the signal transduction mechanisms of the opioid receptors were examined with in vitro radioligand binding, GTPase, adenylyl cyclase, and inositol phosphate assays. The nonselective ligand {sup 3}H-ethylketocyclazocine (EKC), the {mu} and {delta} selective ligand {sup 3}H-(D-Ala{sup 2}, D-Leu{sup 5}) enkephalin (DADLE), the {mu} selective ligand {sup 3}H-(D-Ala{sup 2}, N-methyl Phe{sup 4}, Glyol{sup 5}) enkephalin (DAGO), and the {delta} selective ligand {sup 3}H-(D-Pen{sup 2}, D-Pen{sup 5}) enkephalin (DPDPE) were separately used as tracer ligands to label opioid binding sites in rat PAG enriched P{sub 2} membrane in competition with unlabeled DADLE, DAGO,more »« less
US -endorphin-(1-27) is a naturally occurring antagonist to etorphine-induced analgesia

Journal Article Nicolas, P; Li, C - Proc. Natl. Acad. Sci. U.S.A.; (United States)

The potent opioid peptide US -endorphin is found in the brain and pituitary with two related fragments, US -endorphin-(1-27) and US -endorphin-(1-26). The fragments, retain substantial opioid-receptor binding activity but are virtually inactive analgesically. US -Endorphin-(1-27) inhibits US -endorphin-induced and etorphine-induced analgesia when coinjected intracerebroventricularly into mice. Antagonism by competition at the same site(s) is suggested from parallel shifts of the dose-response curves of etorphine or US -endorphin in the presence of US -endorphin-(1-27). Its potency is 4-5 times greater than that of the opiate antagonist naloxone. US -Endorphin-(1-26) does not antagonize the antinociceptive action of etorphine or US -endorphinmore » in doses up to 500 pmol per animal.« less
https://doi.org/10.1073/pnas.82.10.3178
Biotinylated human. beta. -endorphins as probes for the opioid receptor

Journal Article Hochhaus, G; Gibson, B; Sadee, W - J. Biol. Chem.; (United States)

The reaction of human ..beta..-endorphin and biotinyl N-hydroxysuccinimide with or without spacer arm, afforded a series of products that were separated by high performance liquid chromatography (HPLC). Liquid secondary ion mass spectrometry of the biotinylated products and their tryptic digests produced abundant protonated molecular ions (MH/sup +/), which specified the number and location of biotinylation. Between 1 and 4 biotinyl residues were incorporated per human ..beta..-endorphin molecule, at Lys-9, -19, -24, -28, and -29, but not at the amino-terminal Try-1. Three HPLC fractions were isolated for receptor binding studies monobiotinylation of Lys-9, Lys-19, and a mixture of Lys-24, Lys-28, andmore »« less
Rapid agonist-induced loss of sup 125 I-. beta. -endorphin opioid receptor sites in NG108-15, but not SK-N-SH neuroblastoma cells

Journal Article Cone, R; Lameh, J; Sadee, W - Life Sciences; (United States)

The authors have measured {mu} and {delta} opioid receptor sites on intact SK-N-SH and NG108-15 neuroblastoma cells, respectively, in culture. Use of {sup 125}I-{beta}-endorphin ({beta}E) as a tracer, together with {beta}E(6-31) to block high-affinity non-opioid binding in both cell lines, permitted the measurement of cell surface {mu} and {delta} opioid receptor sites. Labeling was at {delta} sites in NG108-15 cells and predominantly at {mu} sites in SK-N-SH cells. Pretreatment with the {mu} and {delta} agonist, DADLE, caused a rapid loss of cell surface {delta} receptor sites in NG108-15 cells, but failed to reduce significantly {mu} receptor density in SK-N-SH cells.

Similar Records