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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Results indicate that the mode of interaction of OFQ with its receptor may be different from that of the opioid peptides with their respective receptors and might therefore account for the observed selectivity.
Helix-constrained nociceptin peptides are potent agonists and antagonists of ORL-1 and nociception.
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An NMR-derived three-dimensional solution structure is described for a potent ORL-1 agonist derived from nociceptin, along with structure-activity relationships leading to the most potent known α-helical OrL- 1 agonist and antagonist.
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N-terminal modifications leading to peptide ORL1 partial agonists and antagonists.
  • A. Judd, A. Kaushanskaya, +4 authors L. Toll
  • Chemistry, Medicine
    The journal of peptide research : official journal of the American Peptide Society
  • 2003
TLDR
The pharmacological activity of a series of N-terminally modified hexapeptides with high affinity for ORL1 are described, found to possess modest analgesic activity, but it was unable to block the morphine modulatory activity of N/OFQ.
Expression of orphanin FQ and the opioid receptor-like (ORL1) receptor in the developing human and rat brain
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Estimation of the normal pattern of expression of ORL1 mRNA in the human and rat brain at various developmental stages and the influence of early orphanin expression on maturation of stress and pain circuitry in the developing brain remains unknown.
Endomorphin peptides: pharmacological and functional implications of these opioid peptides in the brain of mammals. Part one
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The structure-relationship activity of both endomorphin molecules comparing their binding properties to different opioid receptors are reviewed, leading several authors to suggest the potential endogenous role of these peptides in major physiological processes.
Tissue distribution of the opioid receptor-like (ORL1) receptor
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The anatomic distribution of ORL1 receptor suggests a broad spectrum of action for the nociceptin/orphanin FQ system (sensory perception, memory process, emotional behavior, etc.).
Recognition and activation of the opioid receptor-like ORL 1 receptor by nociceptin, nociceptin analogs and opioids.
TLDR
The results suggest that the highly basic, internal core of nociceptin might be essential in conferring on the peptide both affinity for and activity at the ORL 1 receptor.
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