ArticleProceedings of the National Academy of Sciences of the United States of America1997
Opioid receptors from a lower vertebrate (Catostomus commersoni): sequence, pharmacology, coupling to a G-protein-gated inward-rectifying potassium channel (GIRK1), and evolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 80 citations in OpenAlex.
- Spotlight on Nociceptin/Orphanin FQ Receptor in the Treatment of Pain.Molecules (Basel, Switzerland) · 2022Review
- Single Amino Acid Variation Underlies Species-Specific Sensitivity to Amphibian Skin-Derived Opioid-like Peptides.Chemistry & biology · 2015Article
- Mu opioids and their receptors: evolution of a concept.Pharmacological reviews · 2013Review
- Estradiol interacts with an opioidergic network to achieve rapid modulation of a vocal pattern generator.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2010Article
- Urotensin I-CRF-Urocortins: a mermaid's tail.General and comparative endocrinology · 2009Article
- The evolution of vertebrate opioid receptors.Frontiers in bioscience (Landmark edition) · 2009Review
- A pharmacological comparison of the cloned frog and human mu opioid receptors reveals differences in opioid affinity and function.European journal of pharmacology · 2008Article
- Evolution of vertebrate opioid receptors.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Cloning and bioinformatics of amphibian mu, delta, kappa, and nociceptin opioid receptors expressed in brain tissue: evidence for opioid receptor divergence in mammals.Neuroscience letters · 2007Article
- Opioid research in amphibians: an alternative pain model yielding insights on the evolution of opioid receptors.Brain research. Brain research reviews · 2004Review
- Opioid modulation of pain threshold in fish.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sectionsArticle
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
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Abstract
The molecular evolution of the opioid receptor family has been studied by isolating cDNAs that encode six distinct opioid receptor-like proteins from a lower vertebrate, the teleost fish Catostomus commersoni. One of these, which has been obtained in full-length form, encodes a 383-amino acid protein that exhibits greatest sequence similarity to mammalian mu-opioid receptors; the corresponding gene is expressed predominantly in brain and pituitary. Transfection of the teleost cDNA into HEK 293 cells resulted in the appearance of a receptor having high affinity for the mu-selective agonist [D-Ala2, MePhe4-Gly-ol5]enkephalin (DAMGO) (Kd = 0.63 +/- 0.15 nM) and for the nonselective antagonist naloxone (Kd = 3.1 +/- 1.3 nM). The receptor had negligible affinity for U50488 and [D-Pen2, D-Pen5]enkephalin (DPDPE), which are kappa- and delta-opioid receptor selective agonists, respectively. Stimulation of transfected cells with 1 microM DAMGO lowered forskolin-induced cAMP levels, an effect that could be reversed by naloxone. Experiments in Xenopus oocytes have demonstrated that the fish opioid receptor can, in an agonist-dependent fashion, activate a coexpressed mouse G-protein-gated inward-rectifying potassium channel (GIRK1). The identification of six distinct fish opioid receptor-like proteins suggests that additional mammalian opioid receptors remain to be identified at the molecular level. Furthermore, our data indicate that the mu-opioid receptor arose very early in evolution, perhaps before the appearance of vertebrates, and that the pharmacological and functional properties of this receptor have been conserved over a period of approximately 400 million years implying that it fulfills an important physiological role.
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