Isolation and structure of the endogenous agonist of opioid receptor-like ORL1 receptor
@article{Meunier1995IsolationAS, title={Isolation and structure of the endogenous agonist of opioid receptor-like ORL1 receptor}, author={Jean Claude Meunier and Catherine Mollereau and Lawrence Toll and Charles Suaudeau and Christiane Moisand and Paul Alvinerie and J. L. Butour and Jean Claude Guillemot and Pascual Ferrara and Bernard Monsarrat and Honoré Mazarguil and Gilbert Vassart and Marc Parmentier and Jean Costentin}, journal={Nature}, year={1995}, volume={377}, pages={532-535} }
THE ORL1 receptor, an orphan receptor whose human1and murine2á¤-8 complementary DNAs have recently been characterized, structurally resembles opioid receptors and is negatively coupled with adenylate cyclase1. ORL1 transcripts are particularly abundant in the central nervous system. Here we report the isolation, on the basis of its ability to inhibit the cyclase in a stable recombinant CHO(ORL1 +) cell line, of a neuropeptide that resembles dynorphin A9 and whose amino acid sequence is Phe-Gly…
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References
SHOWING 1-10 OF 18 REFERENCES
Specific receptor for the opioid peptide dynorphin: structure--activity relationships.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1981
Structural features responsible for the high potency and opiate receptor specificity of the opioid peptide dynorphin in the guinea pig ileum myenteric plexus were examined and lysine-11 and arginine-7 were found to be important for selectivity of interaction with the Dynorphin receptor, which is distinguishable from the mu receptor in this tissue.
Human kappa opiate receptor second extracellular loop elevates dynorphin's affinity for human mu/kappa chimeras.
- Biology, ChemistryThe Journal of biological chemistry
- 1994
cDNA Cloning of an orphan opiate receptor gene family member and its splice variant
- Biology, ChemistryFEBS letters
- 1994
Isolation of a novel cDNA encoding a putative membrane receptor with high homology to the cloned μ, δ, and κ opioid receptors
- Biology, Chemistry
- 1994
Molecular cloning and tissue distribution of a putative member of the rat opioid receptor gene family that is not a μ, δ or κ opioid receptor type
- Biology, Chemistry
- 1994
Molecular Cloning of a Novel G Protein‐Coupled Receptor Related to the Opiate Receptor Family
- Biology, ChemistryJournal of neurochemistry
- 1995
It is suggested that the endogenous ligand for this receptor may represent a novel neuropeptide that may be closely related to the opiate peptide family.
Molecular cloning, tissue distribution and chromosomal localization of a novel member of the opioid receptor gene family
- BiologyFEBS letters
- 1994
Porcine pituitary dynorphin: complete amino acid sequence of the biologically active heptadecapeptide.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1981
The full primary structure of the very potent opioid peptide dynorphin, from porcine pituitary, has been determined and it has the same potency in the guinea pig ileum myenteric plexus--longitudinal muscle bioassay.
cDNA cloning and regional distribution of a novel member of the opioid receptor family
- Biology, ChemistryFEBS letters
- 1994