Dynorphin is a Specific Endogenous Ligand of the κ Opioid Receptor

In the guinea pig ileum myenteric plexus-longitudinal muscle preparation, dynorphin-(1-13) and the prototypical κ agonist ethylketocyclazocine had equally poor sensitivity to naloxone antagonism and showed selective cross protection in receptor inactivation experiments with the alkylating antagonist...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1982-01, Vol.215 (4531), p.413-415
Main Authors: Chavkin, Charles, James, Iain F., Goldstein, Avram
Format: Article
Language:English
Subjects:
Agonists
Amides
Analgesics, Opioid - metabolism
Animals
Binding sites
Binding, Competitive
Brain - metabolism
Cyclazocine - analogs & derivatives
Cyclazocine - metabolism
Dynorphins
Endorphins - metabolism
Enkephalin, Leucine
Enkephalins - metabolism
Ethylketocyclazocine
Guinea Pigs
Ileum
In Vitro Techniques
Inhibitory concentration 50
Ligands
Morphine
Morphine Derivatives - metabolism
Myenteric Plexus - metabolism
Naloxone - metabolism
Opioid analgesics
Opioid receptors
Peptide Fragments - metabolism
Receptors
Receptors, Opioid - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In the guinea pig ileum myenteric plexus-longitudinal muscle preparation, dynorphin-(1-13) and the prototypical κ agonist ethylketocyclazocine had equally poor sensitivity to naloxone antagonism and showed selective cross protection in receptor inactivation experiments with the alkylating antagonist β-chlornaltrexamine. In binding assays with membranes from guinea pig brain, ethylketocyclazocine and dynorphin-(1-13) amide were more potent in displacing tritium-labeled ethylketocyclazocine than in displacing typical μ and δ opioid receptor ligands. In the two preparations studied, the dynorphin receptor appears to be the same as the κ opioid receptor.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.6120570