A Single Nucleotide Polymorphic Mutation in the Human μ-Opioid Receptor Severely Impairs Receptor Signaling
Large scale sequencing of the human μ-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated whether the mutations N40D in the extracellular N-terminal region, N152D in the third transmembrane domain, and R265H and S268P in the third...
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Published in | The Journal of biological chemistry Vol. 276; no. 5; pp. 3130 - 3137 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
02.02.2001
American Society for Biochemistry and Molecular Biology |
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Abstract | Large scale sequencing of the human μ-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated whether the mutations N40D in the extracellular N-terminal region, N152D in the third transmembrane domain, and R265H and S268P in the third intracellular loop alter functional properties of the receptor expressed in mammalian cells. The N152D receptor was produced at low densities. Binding affinities of structurally diverse opioids (morphine, diprenorphine, DAMGO and CTOP) and the main endogenous opioid peptides (β-endorphin, [Met]enkephalin, and dynorphin A) were not markedly changed in mutant receptors (<3-fold). Receptor signaling was strongly impaired in the S268P mutant, with a reduction of efficacy and potency of several agonists (DAMGO, β-endorphin, and morphine) in two distinct functional assays. Signaling at N40D and R265H mutants was highly similar to wild type, and none of the mutations induced detectable constitutive activity. DAMGO-induced down-regulation of receptor-binding sites, following 20 h of treatment, was identical in wild-type and mutant receptors. Our data show that natural sequence variations in hMOR gene have little influence on ligand binding or receptor down-regulation but could otherwise modify receptor density and signaling. Importantly, the S268P mutation represents a loss-of-function mutation for the human μ-opioid receptor, which may have an incidence on opioid-regulated behaviors or drug addiction in vivo. |
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AbstractList | Large scale sequencing of the human mu -opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated whether the mutations N40D in the extracellular N-terminal region, N152D in the third transmembrane domain, and R265H and S268P in the third intracellular loop alter functional properties of the receptor expressed in mammalian cells. The N152D receptor was produced at low densities. Binding affinities of structurally diverse opioids (morphine, diprenorphine, DAMGO and CTOP) and the main endogenous opioid peptides ( beta -endorphin, [Met]enkephalin, and dynorphin A) were not markedly changed in mutant receptors (<3-fold). Receptor signaling was strongly impaired in the S268P mutant, with a reduction of efficacy and potency of several agonists (DAMGO, beta - endorphin, and morphine) in two distinct functional assays. Signaling at N40D and R265H mutants was highly similar to wild type, and none of the mutations induced detectable constitutive activity. DAMGO- induced down-regulation of receptor-binding sites, following 20 h of treatment, was identical in wild-type and mutant receptors. Our data show that natural sequence variations in hMOR gene have little influence on ligand binding or receptor down-regulation but could otherwise modify receptor density and signaling. Importantly, the S268P mutation represents a loss-of-function mutation for the human mu -opioid receptor, which may have an incidence on opioid- regulated behaviors or drug addiction in vivo. Large scale sequencing of the human μ-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated whether the mutations N40D in the extracellular N-terminal region, N152D in the third transmembrane domain, and R265H and S268P in the third intracellular loop alter functional properties of the receptor expressed in mammalian cells. The N152D receptor was produced at low densities. Binding affinities of structurally diverse opioids (morphine, diprenorphine, DAMGO and CTOP) and the main endogenous opioid peptides (β-endorphin, [Met]enkephalin, and dynorphin A) were not markedly changed in mutant receptors (<3-fold). Receptor signaling was strongly impaired in the S268P mutant, with a reduction of efficacy and potency of several agonists (DAMGO, β-endorphin, and morphine) in two distinct functional assays. Signaling at N40D and R265H mutants was highly similar to wild type, and none of the mutations induced detectable constitutive activity. DAMGO-induced down-regulation of receptor-binding sites, following 20 h of treatment, was identical in wild-type and mutant receptors. Our data show that natural sequence variations in hMOR gene have little influence on ligand binding or receptor down-regulation but could otherwise modify receptor density and signaling. Importantly, the S268P mutation represents a loss-of-function mutation for the human μ-opioid receptor, which may have an incidence on opioid-regulated behaviors or drug addiction in vivo. Large scale sequencing of the human-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated whether the mutations N40D in the extracellular N-terminal region, N152D in the third transmembrane domain, and R265H and S268P in the third intracellular loop alter functional properties of the receptor expressed in mammalian cells. The N152D receptor was produced at low densities. Binding affinities of structurally diverse opioids (morphine, diprenorphine, DAMGO and CTOP) and the main endogenous opioid peptides (-endorphin, [Met]enkephalin, and dynorphin A) were not markedly changed in mutant receptors (<3fold). Receptor signaling was strongly impaired in the S268P mutant, with a reduction of efficacy and potency of several agonists (DAMGO, -endorphin, and morphine) in two distinct functional assays. Signaling at N40D and R265H mutants was highly similar to wild type, and none of the mutations induced detectable constitutive activity. DAMGO-induced down-regulation of receptor-binding sites, following 20 h of treatment, was identical in wild-type and mutant receptors. Our data show that natural sequence variations in hMOR gene have little influence on ligand binding or receptor down-regulation but could otherwise modify receptor density and signaling. Importantly, the S268P mutation represents a loss-of-function mutation for the human-opioid receptor, which may have an incidence on opioid-regulated behaviors or drug addiction in vivo. |
Author | Gavériaux-Ruff, Claire Hoehe, Margret R. Filliol, Dominique Kieffer, Brigitte L. Décaillot, Fabien M. Befort, Katia |
Author_xml | – sequence: 1 givenname: Katia surname: Befort fullname: Befort, Katia organization: From the Laboratoire des Récepteurs et Protéines Membranaires, UPR CNRS 9050, ESBS, Parc d'Innovation, 67400 Illkirch, France – sequence: 2 givenname: Dominique surname: Filliol fullname: Filliol, Dominique organization: From the Laboratoire des Récepteurs et Protéines Membranaires, UPR CNRS 9050, ESBS, Parc d'Innovation, 67400 Illkirch, France – sequence: 3 givenname: Fabien M. surname: Décaillot fullname: Décaillot, Fabien M. organization: From the Laboratoire des Récepteurs et Protéines Membranaires, UPR CNRS 9050, ESBS, Parc d'Innovation, 67400 Illkirch, France – sequence: 4 givenname: Claire surname: Gavériaux-Ruff fullname: Gavériaux-Ruff, Claire organization: From the Laboratoire des Récepteurs et Protéines Membranaires, UPR CNRS 9050, ESBS, Parc d'Innovation, 67400 Illkirch, France – sequence: 5 givenname: Margret R. surname: Hoehe fullname: Hoehe, Margret R. organization: From the Laboratoire des Récepteurs et Protéines Membranaires, UPR CNRS 9050, ESBS, Parc d'Innovation, 67400 Illkirch, France – sequence: 6 givenname: Brigitte L. surname: Kieffer fullname: Kieffer, Brigitte L. organization: From the Laboratoire des Récepteurs et Protéines Membranaires, UPR CNRS 9050, ESBS, Parc d'Innovation, 67400 Illkirch, France |
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Snippet | Large scale sequencing of the human μ-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated... Large scale sequencing of the human mu-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated... Large scale sequencing of the human mu -opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have... Large scale sequencing of the human-opioid receptor (hMOR) gene has revealed polymorphic mutations that occur within the coding region. We have investigated... |
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SubjectTerms | Analgesics, Opioid - pharmacology Animals Asparagine - genetics Aspartic Acid - genetics b-endorphin Cells, Cultured Chemical Sciences COS Cells Cyclic AMP - metabolism diprenorphine dynorphin A Enkephalin, Ala-MePhe-Gly- - pharmacology Guanosine 5'-O-(3-Thiotriphosphate) - metabolism hMOR gene Humans Mutagenesis, Site-Directed Narcotics - pharmacology opioids Organic chemistry Polymorphism, Single Nucleotide Proline - genetics Receptors, Opioid, mu - agonists Receptors, Opioid, mu - genetics Receptors, Opioid, mu - metabolism Serine - genetics Signal Transduction - physiology Sulfur Radioisotopes |
Title | A Single Nucleotide Polymorphic Mutation in the Human μ-Opioid Receptor Severely Impairs Receptor Signaling |
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