Molecular Cloning and Pharmacological Characterization of a Somatostatin Receptor Subtype in the Gymnotiform Fish Apteronotus albifrons
Identifieur interne : 001174 ( Istex/Corpus ); précédent : 001173; suivant : 001175Molecular Cloning and Pharmacological Characterization of a Somatostatin Receptor Subtype in the Gymnotiform Fish Apteronotus albifrons
Auteurs : Günther K. H. Zupanc ; Sandra Siehler ; Eugenia M. C. Jones ; Klaus Seuwen ; Hiroto Furuta ; Daniel Hoyer ; Hideki YanoSource :
- General and Comparative Endocrinology [ 0016-6480 ] ; 1999.
Abstract
The actions of the various forms of somatostatin (SRIF), including those of the tetradecapeptide SRIF14, are mediated by specific receptors. In mammals, five subtypes of SRIF receptors, termed sst1–5, have been cloned. Using a combination of reverse transcriptase-polymerase chain reaction and genomic library screening in the gymnotiform fish Apteronotus albifrons, a gene encoding the first-known nonmammalian SRIF receptor has been isolated. The deduced amino acid sequence displays 59% identity with the human sst3 receptor protein; hence, the gene is termed “Apteronotus sst3.” The predicted protein consists of 494 amino acid residues exhibiting a putative seven-transmembrane domain topology typical of G protein-coupled receptors. A signal corresponding to the Apteronotus sst3 receptor was detected in brain after amplification of poly(A)+-RNA by reverse transcriptase-polymerase chain reaction, but not by Northern blot analysis or in situ hybridization, suggesting a low level of expression. Membranes prepared from CCL39 cells stably expressing the Apteronotus sst3 receptor gene bound [125I][Leu8,d-Trp22,125 I-Tyr25]SRIF28 with high affinity and in a saturable manner (Bmax=4470 fmol/mg protein; pKD=10.5). SRIF14 and various synthetic SRIF receptor agonists produced a dose-dependent inhibition of radioligand binding, with the following rank order of potency: SRIF14 ≈ SRIF28 > BIM 23052 > octreotide > BIM 23056. Under low stringency conditions, an Apteronotus sst3 probe hybridized to multiple DNA fragments in HindIII or EcoRI digests of A. albifrons DNA, indicating that the Apteronotus sst3 receptor is a member of a larger family of Apteronotus SRIF receptors.
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DOI: 10.1006/gcen.1999.7316
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In mammals, five subtypes of SRIF receptors, termed sst1–5, have been cloned. Using a combination of reverse transcriptase-polymerase chain reaction and genomic library screening in the gymnotiform fish Apteronotus albifrons, a gene encoding the first-known nonmammalian SRIF receptor has been isolated. The deduced amino acid sequence displays 59% identity with the human sst3 receptor protein; hence, the gene is termed “Apteronotus sst3.” The predicted protein consists of 494 amino acid residues exhibiting a putative seven-transmembrane domain topology typical of G protein-coupled receptors. A signal corresponding to the Apteronotus sst3 receptor was detected in brain after amplification of poly(A)+-RNA by reverse transcriptase-polymerase chain reaction, but not by Northern blot analysis or in situ hybridization, suggesting a low level of expression. Membranes prepared from CCL39 cells stably expressing the Apteronotus sst3 receptor gene bound [125I][Leu8,d-Trp22,125 I-Tyr25]SRIF28 with high affinity and in a saturable manner (Bmax=4470 fmol/mg protein; pKD=10.5). SRIF14 and various synthetic SRIF receptor agonists produced a dose-dependent inhibition of radioligand binding, with the following rank order of potency: SRIF14 ≈ SRIF28 > BIM 23052 > octreotide > BIM 23056. Under low stringency conditions, an Apteronotus sst3 probe hybridized to multiple DNA fragments in HindIII or EcoRI digests of A. albifrons DNA, indicating that the Apteronotus sst3 receptor is a member of a larger family of Apteronotus SRIF receptors.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Günther K.H. 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In mammals, five subtypes of SRIF receptors, termed sst1–5, have been cloned. Using a combination of reverse transcriptase-polymerase chain reaction and genomic library screening in the gymnotiform fish Apteronotus albifrons, a gene encoding the first-known nonmammalian SRIF receptor has been isolated. The deduced amino acid sequence displays 59% identity with the human sst3 receptor protein; hence, the gene is termed “Apteronotus sst3.” The predicted protein consists of 494 amino acid residues exhibiting a putative seven-transmembrane domain topology typical of G protein-coupled receptors. A signal corresponding to the Apteronotus sst3 receptor was detected in brain after amplification of poly(A)+-RNA by reverse transcriptase-polymerase chain reaction, but not by Northern blot analysis or in situ hybridization, suggesting a low level of expression. Membranes prepared from CCL39 cells stably expressing the Apteronotus sst3 receptor gene bound [125I][Leu8,d-Trp22,125 I-Tyr25]SRIF28 with high affinity and in a saturable manner (Bmax=4470 fmol/mg protein; pKD=10.5). SRIF14 and various synthetic SRIF receptor agonists produced a dose-dependent inhibition of radioligand binding, with the following rank order of potency: SRIF14 ≈ SRIF28 > BIM 23052 > octreotide > BIM 23056. Under low stringency conditions, an Apteronotus sst3 probe hybridized to multiple DNA fragments in HindIII or EcoRI digests of A. albifrons DNA, indicating that the Apteronotus sst3 receptor is a member of a larger family of Apteronotus SRIF receptors.</abstract><qualityIndicators><score>7.844</score><pdfVersion>1.2</pdfVersion><pdfPageSize>554 x 734 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>1682</abstractCharCount><pdfWordCount>7516</pdfWordCount><pdfCharCount>48421</pdfCharCount><pdfPageCount>13</pdfPageCount><abstractWordCount>237</abstractWordCount></qualityIndicators><title>Molecular Cloning and Pharmacological Characterization of a Somatostatin Receptor Subtype in the Gymnotiform Fish Apteronotus 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xml:id="author-7"><persName><forename type="first">Hideki</forename><surname>Yano</surname></persName><note type="biography">Present address: Department of Molecular Medicine, Center for Biomedical Science, Chiba University Graduate School of Medicine, Chiba 260-0856, Japan.</note><affiliation>Present address: Department of Molecular Medicine, Center for Biomedical Science, Chiba University Graduate School of Medicine, Chiba 260-0856, Japan.</affiliation><affiliation>Howard Hughes Medical Institute, Departments of Biochemistry and Molecular Biology, and Medicine, The University of Chicago, Chicago, Illinois, 60637</affiliation></author></analytic><monogr><title level="j">General and Comparative Endocrinology</title><title level="j" type="abbrev">YGCEN</title><idno type="pISSN">0016-6480</idno><idno type="PII">S0016-6480(00)X0030-5</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999"></date><biblScope unit="volume">115</biblScope><biblScope 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In mammals, five subtypes of SRIF receptors, termed sst1–5, have been cloned. Using a combination of reverse transcriptase-polymerase chain reaction and genomic library screening in the gymnotiform fish Apteronotus albifrons, a gene encoding the first-known nonmammalian SRIF receptor has been isolated. The deduced amino acid sequence displays 59% identity with the human sst3 receptor protein; hence, the gene is termed “Apteronotus sst3.” The predicted protein consists of 494 amino acid residues exhibiting a putative seven-transmembrane domain topology typical of G protein-coupled receptors. A signal corresponding to the Apteronotus sst3 receptor was detected in brain after amplification of poly(A)+-RNA by reverse transcriptase-polymerase chain reaction, but not by Northern blot analysis or in situ hybridization, suggesting a low level of expression. Membranes prepared from CCL39 cells stably expressing the Apteronotus sst3 receptor gene bound [125I][Leu8,d-Trp22,125 I-Tyr25]SRIF28 with high affinity and in a saturable manner (Bmax=4470 fmol/mg protein; pKD=10.5). SRIF14 and various synthetic SRIF receptor agonists produced a dose-dependent inhibition of radioligand binding, with the following rank order of potency: SRIF14 ≈ SRIF28 > BIM 23052 > octreotide > BIM 23056. Under low stringency conditions, an Apteronotus sst3 probe hybridized to multiple DNA fragments in HindIII or EcoRI digests of A. albifrons DNA, indicating that the Apteronotus sst3 receptor is a member of a larger family of Apteronotus SRIF receptors.</p></abstract></profileDesc><revisionDesc><change when="1999">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/A6A3C008B4D1EA869D48A60ADF5BA7F6D3A8683E/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YGCEN</jid><aid>97316</aid><ce:pii>S0016-6480(99)97316-1</ce:pii><ce:doi>10.1006/gcen.1999.7316</ce:doi><ce:copyright type="full-transfer" year="1999">Academic Press</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Molecular Cloning and Pharmacological Characterization of a Somatostatin Receptor Subtype in the Gymnotiform Fish <ce:italic>Apteronotus albifrons</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Günther K.H.</ce:given-name><ce:surname>Zupanc</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="A2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="A3"><ce:sup>c</ce:sup></ce:cross-ref><ce:cross-ref refid="A4"><ce:sup>d</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="FN2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Sandra</ce:given-name><ce:surname>Siehler</ce:surname><ce:cross-ref refid="A4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Eugenia M.C.</ce:given-name><ce:surname>Jones</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="FN3"><ce:sup>3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Klaus</ce:given-name><ce:surname>Seuwen</ce:surname><ce:cross-ref refid="A4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Hiroto</ce:given-name><ce:surname>Furuta</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="FN4"><ce:sup>4</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Daniel</ce:given-name><ce:surname>Hoyer</ce:surname><ce:cross-ref refid="A4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Hideki</ce:given-name><ce:surname>Yano</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="FN5"><ce:sup>5</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="A1"><ce:label>a</ce:label><ce:textfn>Howard Hughes Medical Institute, Departments of Biochemistry and Molecular Biology, and Medicine, The University of Chicago, Chicago, Illinois, 60637</ce:textfn></ce:affiliation><ce:affiliation id="A2"><ce:label>b</ce:label><ce:textfn>Department of Physical Biology, Max Planck Institute for Developmental Biology, D-72011, Tübingen, Germany</ce:textfn></ce:affiliation><ce:affiliation id="A3"><ce:label>c</ce:label><ce:textfn>School of Biological Sciences, The University of Manchester, Manchester, M13 9PT, United Kingdom</ce:textfn></ce:affiliation><ce:affiliation id="A4"><ce:label>d</ce:label><ce:textfn>Nervous System Research, Novartis Pharma AG, CH-4002, Basel, Switzerland</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>Present address: School of Biological Sciences, University of Manchester, 3.614 Stopford Building, Oxford Road, Manchester M13 9PT, United Kingdom.</ce:note-para></ce:footnote><ce:footnote id="FN2"><ce:label>2</ce:label><ce:note-para>To whom correspondence should be addressed. Fax +44 (0) 161 775 7126. E-mail: gunther.zupanc@man.ac.uk.</ce:note-para></ce:footnote><ce:footnote id="FN3"><ce:label>3</ce:label><ce:note-para>Present address: Department of Neurophysiology, University of Wisconsin, Madison, WI 53706.</ce:note-para></ce:footnote><ce:footnote id="FN4"><ce:label>4</ce:label><ce:note-para>Present address: The First Department of Medicine, Wakayama University of Medical Science, Wakayama 640-8136, Japan.</ce:note-para></ce:footnote><ce:footnote id="FN5"><ce:label>5</ce:label><ce:note-para>Present address: Department of Molecular Medicine, Center for Biomedical Science, Chiba University Graduate School of Medicine, Chiba 260-0856, Japan.</ce:note-para></ce:footnote></ce:author-group><ce:date-accepted day="23" month="4" year="1999"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The actions of the various forms of somatostatin (SRIF), including those of the tetradecapeptide SRIF<ce:inf>14</ce:inf>, are mediated by specific receptors. In mammals, five subtypes of SRIF receptors, termed sst<ce:inf>1–5</ce:inf>, have been cloned. Using a combination of reverse transcriptase-polymerase chain reaction and genomic library screening in the gymnotiform fish <ce:italic>Apteronotus albifrons,</ce:italic> a gene encoding the first-known nonmammalian SRIF receptor has been isolated. The deduced amino acid sequence displays 59% identity with the human sst<ce:inf>3</ce:inf> receptor protein; hence, the gene is termed “<ce:italic>Apteronotus</ce:italic> sst<ce:inf>3</ce:inf>.” The predicted protein consists of 494 amino acid residues exhibiting a putative seven-transmembrane domain topology typical of G protein-coupled receptors. A signal corresponding to the <ce:italic>Apteronotus</ce:italic> sst<ce:inf>3</ce:inf> receptor was detected in brain after amplification of poly(A)<ce:sup>+</ce:sup>-RNA by reverse transcriptase-polymerase chain reaction, but not by Northern blot analysis or <ce:italic>in situ</ce:italic> hybridization, suggesting a low level of expression. Membranes prepared from CCL39 cells stably expressing the <ce:italic>Apteronotus</ce:italic> sst<ce:inf>3</ce:inf> receptor gene bound [<ce:sup>125</ce:sup>I][Leu<ce:sup>8</ce:sup>,<math altimg="si1.gif"><sc>d</sc></math>-Trp<ce:sup>22</ce:sup>,<ce:sup>125</ce:sup> I-Tyr<ce:sup>25</ce:sup>]SRIF<ce:inf>28</ce:inf> with high affinity and in a saturable manner (<ce:italic>B</ce:italic><ce:inf>max</ce:inf><ce:hsp sp="0.2"></ce:hsp>=<ce:hsp sp="0.2"></ce:hsp>4470 fmol/mg protein; p<ce:italic>K</ce:italic><ce:inf>D</ce:inf><ce:hsp sp="0.2"></ce:hsp>=<ce:hsp sp="0.2"></ce:hsp>10.5). SRIF<ce:inf>14</ce:inf> and various synthetic SRIF receptor agonists produced a dose-dependent inhibition of radioligand binding, with the following rank order of potency: SRIF<ce:inf>14</ce:inf> ≈ SRIF<ce:inf>28</ce:inf> > BIM 23052 > octreotide > BIM 23056. Under low stringency conditions, an <ce:italic>Apteronotus</ce:italic> sst<ce:inf>3</ce:inf> probe hybridized to multiple DNA fragments in <ce:italic>Hin</ce:italic>dIII or <ce:italic>Eco</ce:italic>RI digests of <ce:italic>A. albifrons</ce:italic> DNA, indicating that the <ce:italic>Apteronotus</ce:italic> sst<ce:inf>3</ce:inf> receptor is a member of a larger family of <ce:italic>Apteronotus</ce:italic> SRIF receptors.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Molecular Cloning and Pharmacological Characterization of a Somatostatin Receptor Subtype in the Gymnotiform Fish Apteronotus albifrons</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Molecular Cloning and Pharmacological Characterization of a Somatostatin Receptor Subtype in the Gymnotiform Fish</title></titleInfo><name type="personal"><namePart type="given">Günther K.H.</namePart><namePart type="family">Zupanc</namePart><affiliation>Howard Hughes Medical Institute, Departments of Biochemistry and Molecular Biology, and Medicine, The University of Chicago, Chicago, Illinois, 60637</affiliation><description>Present address: School of Biological Sciences, University of Manchester, 3.614 Stopford Building, Oxford Road, Manchester M13 9PT, United Kingdom.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sandra</namePart><namePart type="family">Siehler</namePart><affiliation>Nervous System Research, Novartis Pharma AG, CH-4002, Basel, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eugenia M.C.</namePart><namePart type="family">Jones</namePart><affiliation>Howard Hughes Medical Institute, Departments of Biochemistry and Molecular Biology, and Medicine, The University of Chicago, Chicago, Illinois, 60637</affiliation><description>Present address: Department of Neurophysiology, University of Wisconsin, Madison, WI 53706.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Klaus</namePart><namePart type="family">Seuwen</namePart><affiliation>Nervous System Research, Novartis Pharma AG, CH-4002, Basel, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hiroto</namePart><namePart type="family">Furuta</namePart><affiliation>Howard Hughes Medical Institute, Departments of Biochemistry and Molecular Biology, and Medicine, The University of Chicago, Chicago, Illinois, 60637</affiliation><description>Present address: The First Department of Medicine, Wakayama University of Medical Science, Wakayama 640-8136, Japan.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Daniel</namePart><namePart type="family">Hoyer</namePart><affiliation>Nervous System Research, Novartis Pharma AG, CH-4002, Basel, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hideki</namePart><namePart type="family">Yano</namePart><affiliation>Howard Hughes Medical Institute, Departments of Biochemistry and Molecular Biology, and Medicine, The University of Chicago, Chicago, Illinois, 60637</affiliation><description>Present address: Department of Molecular Medicine, Center for Biomedical Science, Chiba University Graduate School of Medicine, Chiba 260-0856, Japan.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1999</dateIssued><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">The actions of the various forms of somatostatin (SRIF), including those of the tetradecapeptide SRIF14, are mediated by specific receptors. In mammals, five subtypes of SRIF receptors, termed sst1–5, have been cloned. Using a combination of reverse transcriptase-polymerase chain reaction and genomic library screening in the gymnotiform fish Apteronotus albifrons, a gene encoding the first-known nonmammalian SRIF receptor has been isolated. The deduced amino acid sequence displays 59% identity with the human sst3 receptor protein; hence, the gene is termed “Apteronotus sst3.” The predicted protein consists of 494 amino acid residues exhibiting a putative seven-transmembrane domain topology typical of G protein-coupled receptors. A signal corresponding to the Apteronotus sst3 receptor was detected in brain after amplification of poly(A)+-RNA by reverse transcriptase-polymerase chain reaction, but not by Northern blot analysis or in situ hybridization, suggesting a low level of expression. Membranes prepared from CCL39 cells stably expressing the Apteronotus sst3 receptor gene bound [125I][Leu8,d-Trp22,125 I-Tyr25]SRIF28 with high affinity and in a saturable manner (Bmax=4470 fmol/mg protein; pKD=10.5). SRIF14 and various synthetic SRIF receptor agonists produced a dose-dependent inhibition of radioligand binding, with the following rank order of potency: SRIF14 ≈ SRIF28 > BIM 23052 > octreotide > BIM 23056. Under low stringency conditions, an Apteronotus sst3 probe hybridized to multiple DNA fragments in HindIII or EcoRI digests of A. albifrons DNA, indicating that the Apteronotus sst3 receptor is a member of a larger family of Apteronotus SRIF receptors.</abstract><note type="content">Section title: Regular Article</note><relatedItem type="host"><titleInfo><title>General and Comparative Endocrinology</title></titleInfo><titleInfo type="abbreviated"><title>YGCEN</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199909</dateIssued></originInfo><identifier type="ISSN">0016-6480</identifier><identifier type="PII">S0016-6480(00)X0030-5</identifier><part><date>199909</date><detail type="volume"><number>115</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>309</start><end>476</end></extent><extent unit="pages"><start>333</start><end>345</end></extent></part></relatedItem><identifier type="istex">A6A3C008B4D1EA869D48A60ADF5BA7F6D3A8683E</identifier><identifier type="DOI">10.1006/gcen.1999.7316</identifier><identifier type="PII">S0016-6480(99)97316-1</identifier><accessCondition type="use and reproduction" contentType="copyright">©1999 Academic Press</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Academic Press, ©1999</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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