New kappa opioid receptor from zebrafish Danio rerio
A cDNA that encodes a kappa opioid receptor like from zebrafish (ZFOR3) has been cloned and characterized. The encoded protein is 377 residues long and presents 70% identity with the mammalian kappa receptors, although less homology is found in the amino- and carboxyl-terminus as well as in the extr...
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| Veröffentlicht in: | Neuroscience letters 2006-09, Vol.405 (1), p.94-99 |
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| creator | Alvarez, Franscisco Alvar Rodriguez-Martin, Ivan Gonzalez-Nuñez, Veronica de Velasco, Ezequiel Marrón Fernández Gonzalez Sarmiento, Rogelio Rodríguez, Raquel E. |
| description | A cDNA that encodes a kappa opioid receptor like from zebrafish (ZFOR3) has been cloned and characterized. The encoded protein is 377 residues long and presents 70% identity with the mammalian kappa receptors, although less homology is found in the amino- and carboxyl-terminus as well as in the extracellular loops. In situ hybridization studies have revealed that ZFOR3 mRNA is highly expressed in particular brain areas that coincide with the expression of the kappa opioid receptor in other species. When ZFOR3 is stably expressed in HEK293 cells, [
3H]-diprenorphine binds with high affinity (
K
D
=
1.05
±
0.26
nM), being this value on the same range as those reported for mammalian kappa opioid receptors. On the other hand, the selective agonist for mammalian kappa receptors U69,593 does not bind to ZFOR3. [
3H]-diprenorphine binding is readily displaced by the peptidic ligand dynorphin A and by the non-endogenous compounds bremazocine, naloxone and morphine, although with different affinities. Our results demonstrate that ZFOR3 is a unique model to study the kappa opioid receptor functionality. |
| doi_str_mv | 10.1016/j.neulet.2006.06.028 |
| format | Article |
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3H]-diprenorphine binds with high affinity (
K
D
=
1.05
±
0.26
nM), being this value on the same range as those reported for mammalian kappa opioid receptors. On the other hand, the selective agonist for mammalian kappa receptors U69,593 does not bind to ZFOR3. [
3H]-diprenorphine binding is readily displaced by the peptidic ligand dynorphin A and by the non-endogenous compounds bremazocine, naloxone and morphine, although with different affinities. Our results demonstrate that ZFOR3 is a unique model to study the kappa opioid receptor functionality.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/j.neulet.2006.06.028</identifier><identifier>PMID: 16842913</identifier><identifier>CODEN: NELED5</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Binding, Competitive ; Biological and medical sciences ; Brain - anatomy & histology ; Brain - metabolism ; Cell Line ; Fundamental and applied biological sciences. Psychology ; Humans ; In Situ Hybridization ; Kappa opioid receptor ; Ligands ; Molecular Sequence Data ; Opioid binding ; Radioligand Assay ; Receptors, Opioid, kappa - biosynthesis ; Receptors, Opioid, kappa - genetics ; Receptors, Opioid, kappa - isolation & purification ; Sequence Homology, Amino Acid ; Vertebrates: nervous system and sense organs ; Zebrafish ; Zebrafish Proteins - biosynthesis ; Zebrafish Proteins - genetics ; Zebrafish Proteins - isolation & purification</subject><ispartof>Neuroscience letters, 2006-09, Vol.405 (1), p.94-99</ispartof><rights>2006 Elsevier Ireland Ltd</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-75f492fe2f71b6a445c9ce3df1352ca2434248caf8ae653b9413e1aa4ebaf1a13</citedby><cites>FETCH-LOGICAL-c390t-75f492fe2f71b6a445c9ce3df1352ca2434248caf8ae653b9413e1aa4ebaf1a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0304394006006148$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18031867$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16842913$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alvarez, Franscisco Alvar</creatorcontrib><creatorcontrib>Rodriguez-Martin, Ivan</creatorcontrib><creatorcontrib>Gonzalez-Nuñez, Veronica</creatorcontrib><creatorcontrib>de Velasco, Ezequiel Marrón Fernández</creatorcontrib><creatorcontrib>Gonzalez Sarmiento, Rogelio</creatorcontrib><creatorcontrib>Rodríguez, Raquel E.</creatorcontrib><title>New kappa opioid receptor from zebrafish Danio rerio</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>A cDNA that encodes a kappa opioid receptor like from zebrafish (ZFOR3) has been cloned and characterized. The encoded protein is 377 residues long and presents 70% identity with the mammalian kappa receptors, although less homology is found in the amino- and carboxyl-terminus as well as in the extracellular loops. In situ hybridization studies have revealed that ZFOR3 mRNA is highly expressed in particular brain areas that coincide with the expression of the kappa opioid receptor in other species. When ZFOR3 is stably expressed in HEK293 cells, [
3H]-diprenorphine binds with high affinity (
K
D
=
1.05
±
0.26
nM), being this value on the same range as those reported for mammalian kappa opioid receptors. On the other hand, the selective agonist for mammalian kappa receptors U69,593 does not bind to ZFOR3. [
3H]-diprenorphine binding is readily displaced by the peptidic ligand dynorphin A and by the non-endogenous compounds bremazocine, naloxone and morphine, although with different affinities. Our results demonstrate that ZFOR3 is a unique model to study the kappa opioid receptor functionality.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Brain - anatomy & histology</subject><subject>Brain - metabolism</subject><subject>Cell Line</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>In Situ Hybridization</subject><subject>Kappa opioid receptor</subject><subject>Ligands</subject><subject>Molecular Sequence Data</subject><subject>Opioid binding</subject><subject>Radioligand Assay</subject><subject>Receptors, Opioid, kappa - biosynthesis</subject><subject>Receptors, Opioid, kappa - genetics</subject><subject>Receptors, Opioid, kappa - isolation & purification</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vertebrates: nervous system and sense organs</subject><subject>Zebrafish</subject><subject>Zebrafish Proteins - biosynthesis</subject><subject>Zebrafish Proteins - genetics</subject><subject>Zebrafish Proteins - isolation & purification</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AQhhdRbK3-A5Fc9Ja6X0k2F0HqJxS96HmZbGZxa5qNu6miv96EFrwJA3OY550ZHkJOGZ0zyvLL1bzFTYP9nFOaz8fiao9MmSp4WpQF3ydTKqhMRSnphBzFuKKUZiyTh2TCciV5ycSUyCf8St6h6yDxnfOuTgIa7HofEhv8OvnBKoB18S25gdb5YRqcPyYHFpqIJ7s-I693ty-Lh3T5fP-4uF6mRpS0T4vMypJb5LZgVQ5SZqY0KGrLRMYNcCkkl8qAVYB5JqpSMoEMQGIFlgETM3Kx3dsF_7HB2Ou1iwabBlr0m6hzVbBSZcUAyi1ogo8xoNVdcGsI35pRPdrSK721pUdbeiyuhtjZbv-mWmP9F9rpGYDzHQDRQGMDtMbFP05RwVQ-3r_acjjY-HQYdDQOW4O1G3T2uvbu_09-AYjMia0</recordid><startdate>20060911</startdate><enddate>20060911</enddate><creator>Alvarez, Franscisco Alvar</creator><creator>Rodriguez-Martin, Ivan</creator><creator>Gonzalez-Nuñez, Veronica</creator><creator>de Velasco, Ezequiel Marrón Fernández</creator><creator>Gonzalez Sarmiento, Rogelio</creator><creator>Rodríguez, Raquel E.</creator><general>Elsevier Ireland Ltd</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20060911</creationdate><title>New kappa opioid receptor from zebrafish Danio rerio</title><author>Alvarez, Franscisco Alvar ; Rodriguez-Martin, Ivan ; Gonzalez-Nuñez, Veronica ; de Velasco, Ezequiel Marrón Fernández ; Gonzalez Sarmiento, Rogelio ; Rodríguez, Raquel E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-75f492fe2f71b6a445c9ce3df1352ca2434248caf8ae653b9413e1aa4ebaf1a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Brain - anatomy & histology</topic><topic>Brain - metabolism</topic><topic>Cell Line</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>In Situ Hybridization</topic><topic>Kappa opioid receptor</topic><topic>Ligands</topic><topic>Molecular Sequence Data</topic><topic>Opioid binding</topic><topic>Radioligand Assay</topic><topic>Receptors, Opioid, kappa - biosynthesis</topic><topic>Receptors, Opioid, kappa - genetics</topic><topic>Receptors, Opioid, kappa - isolation & purification</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vertebrates: nervous system and sense organs</topic><topic>Zebrafish</topic><topic>Zebrafish Proteins - biosynthesis</topic><topic>Zebrafish Proteins - genetics</topic><topic>Zebrafish Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alvarez, Franscisco Alvar</creatorcontrib><creatorcontrib>Rodriguez-Martin, Ivan</creatorcontrib><creatorcontrib>Gonzalez-Nuñez, Veronica</creatorcontrib><creatorcontrib>de Velasco, Ezequiel Marrón Fernández</creatorcontrib><creatorcontrib>Gonzalez Sarmiento, Rogelio</creatorcontrib><creatorcontrib>Rodríguez, Raquel E.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alvarez, Franscisco Alvar</au><au>Rodriguez-Martin, Ivan</au><au>Gonzalez-Nuñez, Veronica</au><au>de Velasco, Ezequiel Marrón Fernández</au><au>Gonzalez Sarmiento, Rogelio</au><au>Rodríguez, Raquel E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New kappa opioid receptor from zebrafish Danio rerio</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>2006-09-11</date><risdate>2006</risdate><volume>405</volume><issue>1</issue><spage>94</spage><epage>99</epage><pages>94-99</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><coden>NELED5</coden><abstract>A cDNA that encodes a kappa opioid receptor like from zebrafish (ZFOR3) has been cloned and characterized. The encoded protein is 377 residues long and presents 70% identity with the mammalian kappa receptors, although less homology is found in the amino- and carboxyl-terminus as well as in the extracellular loops. In situ hybridization studies have revealed that ZFOR3 mRNA is highly expressed in particular brain areas that coincide with the expression of the kappa opioid receptor in other species. When ZFOR3 is stably expressed in HEK293 cells, [
3H]-diprenorphine binds with high affinity (
K
D
=
1.05
±
0.26
nM), being this value on the same range as those reported for mammalian kappa opioid receptors. On the other hand, the selective agonist for mammalian kappa receptors U69,593 does not bind to ZFOR3. [
3H]-diprenorphine binding is readily displaced by the peptidic ligand dynorphin A and by the non-endogenous compounds bremazocine, naloxone and morphine, although with different affinities. Our results demonstrate that ZFOR3 is a unique model to study the kappa opioid receptor functionality.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>16842913</pmid><doi>10.1016/j.neulet.2006.06.028</doi><tpages>6</tpages></addata></record> |
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| ispartof | Neuroscience letters, 2006-09, Vol.405 (1), p.94-99 |
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| subjects | Amino Acid Sequence Animals Binding, Competitive Biological and medical sciences Brain - anatomy & histology Brain - metabolism Cell Line Fundamental and applied biological sciences. Psychology Humans In Situ Hybridization Kappa opioid receptor Ligands Molecular Sequence Data Opioid binding Radioligand Assay Receptors, Opioid, kappa - biosynthesis Receptors, Opioid, kappa - genetics Receptors, Opioid, kappa - isolation & purification Sequence Homology, Amino Acid Vertebrates: nervous system and sense organs Zebrafish Zebrafish Proteins - biosynthesis Zebrafish Proteins - genetics Zebrafish Proteins - isolation & purification |
| title | New kappa opioid receptor from zebrafish Danio rerio |
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