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Dynorphin A as a Potential Endogenous Ligand for Four Members of the Opioid Receptor Gene Family
Dynorphin A is an endogenous opioid peptide that activates the kappa opioid receptor (KOR) with high potency. Some studies also showed that the distribution and functional activity of dynorphin A are not completely correlated with those of KOR, suggesting that dynorphin A may interact with other rec...
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Published in: | The Journal of pharmacology and experimental therapeutics 1998-07, Vol.286 (1), p.136-141 |
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creator | Zhang, S Tong, Y Tian, M Dehaven, R N Cortesburgos, L Mansson, E Simonin, F Kieffer, B Yu, L |
description | Dynorphin A is an endogenous opioid peptide that activates the kappa opioid receptor (KOR) with high potency. Some studies also showed that the distribution and functional activity of dynorphin
A are not completely correlated with those of KOR, suggesting that dynorphin A may interact with other receptors. To investigate
the possibility that dynorphin A may serve as an agonist for other opioid receptors, we took the advantage of the cloning
of the three major types of opioid receptors, mu (MOR), delta (DOR) and KOR, and examined their affinity for and their activation by dynorphin A. We used mammalian cells transfected with
each of the cDNA clones for the human receptors hMOR, hDOR, hKOR and showed that dynorphin A displaced [ 3 H]-diprenorphine binding with K i values in the nanomolar range at all three receptors. We also showed that, when hMOR, hDOR or hKOR was coexpressed with a
G protein-activated potassium channel in Xenopus oocytes, dynorphin A induced a potassium current with EC 50 values in the nanomolar range for all three receptors. Furthermore, we showed that the human hORLl, an opioid receptor-like
receptor that has been identified as a novel member of the opioid receptor gene family, displayed dynorphin A binding and
functional activation. These results indicate that dynorphin A is capable of binding to and functional activation of all members
of the opioid receptor family, suggesting that, as a potential endogenous agonist, its activity in humans may involve interaction
with other members of the opioid receptor family in addition to kappa receptors. |
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A are not completely correlated with those of KOR, suggesting that dynorphin A may interact with other receptors. To investigate
the possibility that dynorphin A may serve as an agonist for other opioid receptors, we took the advantage of the cloning
of the three major types of opioid receptors, mu (MOR), delta (DOR) and KOR, and examined their affinity for and their activation by dynorphin A. We used mammalian cells transfected with
each of the cDNA clones for the human receptors hMOR, hDOR, hKOR and showed that dynorphin A displaced [ 3 H]-diprenorphine binding with K i values in the nanomolar range at all three receptors. We also showed that, when hMOR, hDOR or hKOR was coexpressed with a
G protein-activated potassium channel in Xenopus oocytes, dynorphin A induced a potassium current with EC 50 values in the nanomolar range for all three receptors. Furthermore, we showed that the human hORLl, an opioid receptor-like
receptor that has been identified as a novel member of the opioid receptor gene family, displayed dynorphin A binding and
functional activation. These results indicate that dynorphin A is capable of binding to and functional activation of all members
of the opioid receptor family, suggesting that, as a potential endogenous agonist, its activity in humans may involve interaction
with other members of the opioid receptor family in addition to kappa receptors.</description><identifier>ISSN: 0022-3565</identifier><identifier>EISSN: 1521-0103</identifier><identifier>PMID: 9655852</identifier><language>eng</language><publisher>United States: American Society for Pharmacology and Experimental Therapeutics</publisher><subject>Animals ; Dynorphins - metabolism ; Dynorphins - pharmacology ; Female ; Humans ; Receptors, Opioid - drug effects ; Receptors, Opioid - genetics ; Receptors, Opioid - metabolism ; Receptors, Opioid, delta - metabolism ; Receptors, Opioid, kappa - metabolism ; Receptors, Opioid, mu - metabolism ; Recombinant Proteins - metabolism ; Xenopus</subject><ispartof>The Journal of pharmacology and experimental therapeutics, 1998-07, Vol.286 (1), p.136-141</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9655852$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, S</creatorcontrib><creatorcontrib>Tong, Y</creatorcontrib><creatorcontrib>Tian, M</creatorcontrib><creatorcontrib>Dehaven, R N</creatorcontrib><creatorcontrib>Cortesburgos, L</creatorcontrib><creatorcontrib>Mansson, E</creatorcontrib><creatorcontrib>Simonin, F</creatorcontrib><creatorcontrib>Kieffer, B</creatorcontrib><creatorcontrib>Yu, L</creatorcontrib><title>Dynorphin A as a Potential Endogenous Ligand for Four Members of the Opioid Receptor Gene Family</title><title>The Journal of pharmacology and experimental therapeutics</title><addtitle>J Pharmacol Exp Ther</addtitle><description>Dynorphin A is an endogenous opioid peptide that activates the kappa opioid receptor (KOR) with high potency. Some studies also showed that the distribution and functional activity of dynorphin
A are not completely correlated with those of KOR, suggesting that dynorphin A may interact with other receptors. To investigate
the possibility that dynorphin A may serve as an agonist for other opioid receptors, we took the advantage of the cloning
of the three major types of opioid receptors, mu (MOR), delta (DOR) and KOR, and examined their affinity for and their activation by dynorphin A. We used mammalian cells transfected with
each of the cDNA clones for the human receptors hMOR, hDOR, hKOR and showed that dynorphin A displaced [ 3 H]-diprenorphine binding with K i values in the nanomolar range at all three receptors. We also showed that, when hMOR, hDOR or hKOR was coexpressed with a
G protein-activated potassium channel in Xenopus oocytes, dynorphin A induced a potassium current with EC 50 values in the nanomolar range for all three receptors. Furthermore, we showed that the human hORLl, an opioid receptor-like
receptor that has been identified as a novel member of the opioid receptor gene family, displayed dynorphin A binding and
functional activation. These results indicate that dynorphin A is capable of binding to and functional activation of all members
of the opioid receptor family, suggesting that, as a potential endogenous agonist, its activity in humans may involve interaction
with other members of the opioid receptor family in addition to kappa receptors.</description><subject>Animals</subject><subject>Dynorphins - metabolism</subject><subject>Dynorphins - pharmacology</subject><subject>Female</subject><subject>Humans</subject><subject>Receptors, Opioid - drug effects</subject><subject>Receptors, Opioid - genetics</subject><subject>Receptors, Opioid - metabolism</subject><subject>Receptors, Opioid, delta - metabolism</subject><subject>Receptors, Opioid, kappa - metabolism</subject><subject>Receptors, Opioid, mu - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Xenopus</subject><issn>0022-3565</issn><issn>1521-0103</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNpFkE9LwzAchoMoc04_gpCTt0L-LGlzHHObwmQieo5p-lsbaZOatEi_vQMHnt7LwwPPe4HmVDCaEUr4JZoTwljGhRTX6CalL0Locin5DM2UFKIQbI4-HycfYt84j1fYJGzwaxjAD860eOOrUIMPY8J7Vxtf4WOIeBvGiF-gKyEmHI54aAAfehdchd_AQj-cmB14wFvTuXa6RVdH0ya4O-8CfWw37-unbH_YPa9X-6xmkg0ZGFUwVqoyLwRVpTBWWWYFs1bmvID8CKXiVilmpQFZEEkrkVNgOahS2pLzBXr48_YxfI-QBt25ZKFtjYdTgS4IITln8gTen8Gx7KDSfXSdiZM-X_Ivalzd_LgIum9M7IwNbagnzQqpqaZc8l__0Wrx</recordid><startdate>19980701</startdate><enddate>19980701</enddate><creator>Zhang, S</creator><creator>Tong, Y</creator><creator>Tian, M</creator><creator>Dehaven, R N</creator><creator>Cortesburgos, L</creator><creator>Mansson, E</creator><creator>Simonin, F</creator><creator>Kieffer, B</creator><creator>Yu, L</creator><general>American Society for Pharmacology and Experimental Therapeutics</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19980701</creationdate><title>Dynorphin A as a Potential Endogenous Ligand for Four Members of the Opioid Receptor Gene Family</title><author>Zhang, S ; Tong, Y ; Tian, M ; Dehaven, R N ; Cortesburgos, L ; Mansson, E ; Simonin, F ; Kieffer, B ; Yu, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g262t-ea9822b9b78519b5ac9c2c52cc6738e7feb93c992c6ae68061d571e27e9b6cb33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Dynorphins - metabolism</topic><topic>Dynorphins - pharmacology</topic><topic>Female</topic><topic>Humans</topic><topic>Receptors, Opioid - drug effects</topic><topic>Receptors, Opioid - genetics</topic><topic>Receptors, Opioid - metabolism</topic><topic>Receptors, Opioid, delta - metabolism</topic><topic>Receptors, Opioid, kappa - metabolism</topic><topic>Receptors, Opioid, mu - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, S</creatorcontrib><creatorcontrib>Tong, Y</creatorcontrib><creatorcontrib>Tian, M</creatorcontrib><creatorcontrib>Dehaven, R N</creatorcontrib><creatorcontrib>Cortesburgos, L</creatorcontrib><creatorcontrib>Mansson, E</creatorcontrib><creatorcontrib>Simonin, F</creatorcontrib><creatorcontrib>Kieffer, B</creatorcontrib><creatorcontrib>Yu, L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of pharmacology and experimental therapeutics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, S</au><au>Tong, Y</au><au>Tian, M</au><au>Dehaven, R N</au><au>Cortesburgos, L</au><au>Mansson, E</au><au>Simonin, F</au><au>Kieffer, B</au><au>Yu, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynorphin A as a Potential Endogenous Ligand for Four Members of the Opioid Receptor Gene Family</atitle><jtitle>The Journal of pharmacology and experimental therapeutics</jtitle><addtitle>J Pharmacol Exp Ther</addtitle><date>1998-07-01</date><risdate>1998</risdate><volume>286</volume><issue>1</issue><spage>136</spage><epage>141</epage><pages>136-141</pages><issn>0022-3565</issn><eissn>1521-0103</eissn><abstract>Dynorphin A is an endogenous opioid peptide that activates the kappa opioid receptor (KOR) with high potency. Some studies also showed that the distribution and functional activity of dynorphin
A are not completely correlated with those of KOR, suggesting that dynorphin A may interact with other receptors. To investigate
the possibility that dynorphin A may serve as an agonist for other opioid receptors, we took the advantage of the cloning
of the three major types of opioid receptors, mu (MOR), delta (DOR) and KOR, and examined their affinity for and their activation by dynorphin A. We used mammalian cells transfected with
each of the cDNA clones for the human receptors hMOR, hDOR, hKOR and showed that dynorphin A displaced [ 3 H]-diprenorphine binding with K i values in the nanomolar range at all three receptors. We also showed that, when hMOR, hDOR or hKOR was coexpressed with a
G protein-activated potassium channel in Xenopus oocytes, dynorphin A induced a potassium current with EC 50 values in the nanomolar range for all three receptors. Furthermore, we showed that the human hORLl, an opioid receptor-like
receptor that has been identified as a novel member of the opioid receptor gene family, displayed dynorphin A binding and
functional activation. These results indicate that dynorphin A is capable of binding to and functional activation of all members
of the opioid receptor family, suggesting that, as a potential endogenous agonist, its activity in humans may involve interaction
with other members of the opioid receptor family in addition to kappa receptors.</abstract><cop>United States</cop><pub>American Society for Pharmacology and Experimental Therapeutics</pub><pmid>9655852</pmid><tpages>6</tpages></addata></record> |
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subjects | Animals Dynorphins - metabolism Dynorphins - pharmacology Female Humans Receptors, Opioid - drug effects Receptors, Opioid - genetics Receptors, Opioid - metabolism Receptors, Opioid, delta - metabolism Receptors, Opioid, kappa - metabolism Receptors, Opioid, mu - metabolism Recombinant Proteins - metabolism Xenopus |
title | Dynorphin A as a Potential Endogenous Ligand for Four Members of the Opioid Receptor Gene Family |
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