Identification, partial characterization, and hypothalamic distribution of κ, μ, and δ opioid receptors in a passerine songbird (Junco hyemalis)

Deviche, Pierre; Cotter, P. F.; Gulledge, Cynthia C.

doi:10.1016/0006-8993(93)91038-t

Cited by 31 publications

(14 citation statements)

References 43 publications

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“…Non-specific binding was measured in the presence of excess concentrations of three unlabelled ligands with high, non-selective affinity for the three receptor subclasses. To assure that radiolabeled ligands occupied similar proportions of their respective receptors, each ligand was used at a concentration equal to twice its dissociation constant ( 3 H-DAMGO, 11 nM; 3 H-pCl-DPDPE, 0.48 nM; 3 H-EKC, 2.48 nM; Deviche et al, 1993). After incubation, slides were rinsed, dried, placed in X-ray cassettes that each contained a set of tritiated plastic standards, and exposed to radioactivity-sensitive film for 10-12 weeks.…”

Section: Methodsmentioning

confidence: 99%

“…Before radiolabeling, sections were preincubated with buffer at pH 7.40 to dissociate and eliminate receptor-bound endogenous ligands (Gulledge and Deviche, 1995). To label m receptors, pairs of slides with adjacent sections (one slide for total binding, TB, and the other slide for non-specific binding, NSB) were incubated in a solution containing Optimum incubation conditions and ligand binding specificities in dark-eyed Junco brains were previously determined (Deviche et al, 1993). Non-specific binding was measured in the presence of excess concentrations of three unlabelled ligands with high, non-selective affinity for the three receptor subclasses.…”

Section: Methodsmentioning

confidence: 99%

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Opioid receptor densities analyzed across seasons in the POM and VTA of the dark-eyed junco, Junco hyemalis

Woods

Deviche

Corbitt

2010

Journal of Chemical Neuroanatomy

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Opioid receptor densities analyzed across seasons in the POM and VTA of the dark-eyed junco, Junco hyemalis

Woods

Deviche

Corbitt

2010

Journal of Chemical Neuroanatomy

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“…The genes arose by duplications in the common ancestor of tetrapods and bony fishes (13). Opioid receptor sequences have been reported for a few nonmammalian tetrapods (14)(15)(16)(17)(18)) and a few teleost fishes (19)(20)(21)(22)(23)(24), and a partial sequence has been reported for a hagfish (19). Functional studies in amphibians and bony fishes have shown that the opioid system is involved in nociception also in these species (25,26).…”

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confidence: 99%

Evolution of vertebrate opioid receptors

Dreborg

Sundström

Larsson

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

110

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The opioid peptides and receptors have prominent roles in pain transmission and reward mechanisms in mammals. The evolution of the opioid receptors has so far been little studied, with only a few reports on species other than tetrapods. We have investigated species representing a broader range of vertebrates and found that the four opioid receptor types (delta, kappa, mu, and NOP) are present in most of the species. The gene relationships were deduced by using both phylogenetic analyses and chromosomal location relative to 20 neighboring gene families in databases of assembled genomes. The combined results show that the vertebrate opioid receptor gene family arose by quadruplication of a large chromosomal block containing at least 14 other gene families. The quadruplication seems to coincide with, and, therefore, probably resulted from, the two proposed genome duplications in early vertebrate evolution. We conclude that the quartet of opioid receptors was already present at the origin of jawed vertebrates Ϸ450 million years ago. A few additional opioid receptor gene duplications have occurred in bony fishes. Interestingly, the ancestral receptor gene duplications coincide with the origin of the four opioid peptide precursor genes. Thus, the complete vertebrate opioid system was already established in the first jawed vertebrates.chromosome ͉ G protein-coupled receptor ͉ gene duplication S everal opioid peptides, including endorphin and enkephalins, are important regulators of nociceptive neurotransmission and reward mechanisms in mammals. Specific binding sites in the brain for opioid compounds were first reported in 1973 (1-3), and it was soon evident that more than one type of binding site existed (4). Subsequently three distinct opioid receptors were identified and designated delta, kappa, and mu. These receptors were cloned and found to be encoded by separate genes belonging to the superfamily of rhodopsin-like G protein-coupled receptors (GPCRs) (5-8). The genes for the opioid receptors (OPR) have been named OPRD1 (delta), OPRK1 (kappa), and OPRM1 (mu) by the HUGO Gene Nomenclature Committee (HGNC).Homology searches resulted in the discovery of a fourth receptor in both rodents and humans initially named ORL1 for opioid receptor-like (9) or LC132 (10). This receptor shows 48-49% identity to the other three human receptors, which display 55-58% identity among one another. The receptor has been named NOP by the International Union of Basic and Clinical Pharmacology and its gene has been named OPRL1 by HGNC. An endogenous peptide ligand with some similarity to the other opioid peptides was discovered and named nociceptin (11) or orphanin FQ (12).The evolution of the endogenous opioid peptide ligands has been studied extensively and the major peptide ligands are generated from four prepropeptides that are encoded by separate genes in tetrapods. The genes arose by duplications in the common ancestor of tetrapods and bony fishes (13). Opioid receptor sequences have been reported for a few nonmammalian tetrapods (1...

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“…The selective opioid radioligands, (Gillan and Kosterlitz, 1982), (Lahti et al, 1985;Kim et al, 1996), and (Akiyama et al, 1985) were used previously to characterize opioid binding sites in a variety of vertebrate species (Gillan and Kosterlitz, 1982;Clark et al, 1988;Goldstein and Naidu, 1989;Deviche et al, 1993;Emmerson et al, 1994;Niwa et al, 1994;Darlison et al, 1997). However, no studies thus far have systematically characterized selective opioid radioligand binding in the Northern grass frog, R. pipiens.…”

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confidence: 99%

Characterization of μ, κ, and δ Opioid Binding in Amphibian Whole Brain Tissue Homogenates

Newman

Sands

Wallace³

et al. 2002

J Pharmacol Exp Ther

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Opioid agonists produce analgesia in mammals through the activation of , , or ␦ opioid receptors. Previous behavioral and binding studies from our laboratory using an amphibian model suggested that , , or ␦ opioid agonists may activate a single type of opioid receptor in the grass frog, Rana pipiens. In the present study, kinetic, saturation, and competitive binding profiles for three opioid radioligands,were determined using frog whole brain homogenates. Kinetic analyses and experimentally derived values from saturation experiments gave affinity constants (K D ) in the low nanomolar range. The density of opioid binding sites (B max ) was 224.4, 118.6, and 268.9 fmol/mg for , , and ␦ opioid radioligands, respectively. The affinity values did not significantly differ among the three opioid radioligands, but the radioligand bound to significantly fewer sites than did the or ␦ radioligands. K i values for unlabeled , , and ␦ competitors, including highly selective opioid antagonists, were consistent with each radioligand selectivity profile. The present data suggest that , , and ␦ opioid radioligands bind to distinct opioid receptors in amphibians that are surprisingly similar to those found in mammalian brain.Pharmacological studies show that opioids produce analgesia in mammals through the activation of one or more of three distinct types of opioid receptors. Evidence for the multiplicity of opioid receptors in mammals was first noted with behavioral studies (Martin et al., 1976), was further confirmed by radioligand binding studies (Lord et al., 1977;Gillan et al., 1980), and was verified through molecular cloning techniques identifying three types of opioid receptors, the , , and ␦ opioid receptors (Raynor et al., 1994).Although a triad of opioid receptors is known to mediate opioid analgesia in humans and other mammals, it is not known which type of opioid receptors mediate opioid antinociception in nonmammalian vertebrates. The antinociceptive effects of a number of opioid agonists were shown in an amphibian model using a behavioral assay, the acetic acid test (Pezalla, 1983;Stevens and Pezalla, 1983;Stevens, 1988). The antinociception produced by these agents was shown to be opioid receptor-mediated as it was significantly blocked by the general opioid antagonists, naloxone and naltrexone (Stevens and Pezalla, 1984;Stevens et al., 1994). Selective , , and ␦ opioid agonists cause dose-dependent, naltrexone-reversible antinociceptive effects following systemic or central administration (Stevens et al., 1994;Stevens, 1996;Stevens and Rothe, 1997). Compared with results in mammals, the relative antinociceptive potency of selective , , and ␦ opioids is highly correlated following systemic and intraspinal administration in rodents and frogs (Stevens et al., 1994;Stevens, 1996). Thus, the amphibian model serves as an adjunct model for the testing of opioid analgesics, with unique advantages and disadvantages (Stevens, 1992(Stevens, , 1995 (Newman et al., 2000a,b). The rank order of [ 3 H]naloxone displacem...

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Identification, partial characterization, and hypothalamic distribution of κ, μ, and δ opioid receptors in a passerine songbird (Junco hyemalis)

Cited by 31 publications

References 43 publications

Opioid receptor densities analyzed across seasons in the POM and VTA of the dark-eyed junco, Junco hyemalis

Opioid receptor densities analyzed across seasons in the POM and VTA of the dark-eyed junco, Junco hyemalis

Evolution of vertebrate opioid receptors

Characterization of μ, κ, and δ Opioid Binding in Amphibian Whole Brain Tissue Homogenates

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