Rapid communicationIdentity of the putative δ1-opioid receptor as a δ–κ heteromer in the mouse spinal cord
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Acknowledgments
This work was supported by the National Institute on Drug Abuse research grant R37 DA01533. The animal protocols used in these experiments were approved by the University of Minnesota Institutional Animal Care and Use Committee (IACUC).
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Contribution of heteromerization to G protein-coupled receptor function
2017, Current Opinion in PharmacologyDOR<inf>2</inf>-selective but not DOR<inf>1</inf>-selective antagonist abolishes anxiolytic-like effects of the δ opioid receptor agonist KNT-127
2014, NeuropharmacologyCitation Excerpt :Recently, the coexistence of DOR and MOR on dorsal root ganglion neurons in laminae I-II of mouse spinal cord has been shown to contribute to the presynaptic inhibition of nociceptive afferent transmission (Wang et al., 2010). Other reports suggested that the DOR subtypes may be a DOR-KOR heterodimer (Bhushan et al., 2004; Jordan and Devi, 1999; Portoghese and Lunzer, 2003). Therefore, it is possible that KNT-127-induced DOR subtype-mediated pharmacological profiles may be due to interactions between KNT-127 and either splice variants of DOR or opioid receptor heterodimers.
The novel δ opioid receptor agonist KNT-127 produces antidepressant-like and antinociceptive effects in mice without producing convulsions
2011, Behavioural Brain ResearchCitation Excerpt :Our findings thus contrast with previous arguments that there is no evidence for the existence of genes encoding different DOP subtypes [53–56]. However, several investigators have proposed that DOP splice variants [57,58] and heterodimers [59–61] may contribute to the distinctive DOP subtypes observed in in vivo studies. Indeed, Gaveriaux-Ruff et al. [57] reported that a DOP variant also has been reported in mouse brain.
A comprehensive study on the putative δ-opioid receptor (sub)types using the highly selective δ-antagonist, Tyr-Tic-(2S,3R)-β-MePhe-Phe- OH
2011, Neurochemistry InternationalCitation Excerpt :Growing number of data have shown that G-protein coupled receptors are able to form homo- and heterooligomers, which may result in altered pharmacology of the receptors and provide an explanation for the existence of receptor subtypes (George et al., 2000; Jordan and Devi, 1999; Levac et al., 2002). It has been suggested that the δ1-opioid receptor is a result of heterodimerization between the δ- and κ-opioid receptors (Portoghese and Luzan, 2003). Others postulated that while the δ1-opioid receptor is a δ–μ heterodimer, the δ2-opioid receptor is a δ–δ homodimer (van Rijn and Whistler, 2009) Deltorphin II was suggested to be a full agonist for δ–μ-receptor heterodimer (Fan et al., 2005) DAMGO, DPDPE, morphine, endomorphin-1, endomorphin-2, etc were able to activate the heterodimer (George et al., 2000).
Effect of linker substitution on the binding of butorphan univalent and bivalent ligands to opioid receptors
2010, Bioorganic and Medicinal Chemistry LettersOpioid-receptor-heteromer-specific trafficking and pharmacology
2010, Current Opinion in Pharmacology