NDLI: Agonists and antagonists bind to different domains of the cloned kappa opioid receptor.

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Agonists and antagonists bind to different domains of the cloned kappa opioid receptor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yano, H. Raynor, K. Reisine, T. Takeda, J. Kong, H. Bell, G. I.
Description	Author Affiliation: Kong H ( Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia 19104.);
Abstract	Opium and its derivatives are potent analgesics that can also induce severe side effects, including respiratory depression and addiction. Opioids exert their diverse physiological effects through specific membrane-bound receptors. Three major types of opioid receptors have been described, termed delta, kappa, and mu. The recent molecular cloning of these receptor types opens up the possibility to identify the ligand-binding domains of these receptors. To identify the ligand-binding domains of the kappa and delta receptors, we have expressed in COS-7 cells the cloned mouse delta and kappa receptors and chimeric delta/kappa and kappa/delta receptors in which the NH2 termini have been exchanged. The opioid antagonist naloxone binds potently to wild-type kappa receptor but not to wild-type delta receptor. The kappa/delta chimera bound [3H]naloxone with high affinity. In contrast, the kappa-specific agonist [3H]U-69,593 did not bind to the kappa/delta chimera. These findings indicate that selective agonists and antagonists interact with different recognition sites in the kappa receptor and localize the antagonist-binding domain to the NH2 terminus. Consistent with the results of radioligand-binding studies, the kappa/delta chimera did not mediate kappa-agonist inhibition of cAMP formation. In contrast, the delta/kappa chimera did mediate kappa-agonist inhibition of cAMP formation, but this effect was not blocked by naloxone. Furthermore, a truncated kappa receptor lacking its NH2 terminus was able to mediate agonist inhibition of cAMP accumulation in a naloxone-insensitive manner. This result further indicates that the NH2 terminus of the kappa receptor contains the selective antagonist-binding domain. The ability to dissociate agonist- and antagonist-binding sites will facilitate the development of more specific kappa agonists, which could have analgesic properties devoid of side effects.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Benzeneacetamides Naloxone Metabolism Protein Structure, Secondary Pyrrolidines Receptors, Opioid, Delta Chemistry Receptors, Opioid, Kappa 3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer Analgesics Animals Binding Sites Cell Line Cercopithecus Aethiops Cloning, Molecular Colforsin Pharmacology Cyclic AMP Enkephalin, Leucine Analogs & Derivatives Kinetics Mice Molecular Sequence Data Mutagenesis, Site-Directed Naltrexone Oligodeoxyribonucleotides Radioligand Assay Recombinant Fusion Proteins Recombinant Proteins Transfection Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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