Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives
Identifieur interne : 001257 ( Istex/Corpus ); précédent : 001256; suivant : 001258Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives
Auteurs : J. Michael Conlon ; Herve Tostivint ; Hubert VaudrySource :
- Regulatory Peptides [ 0167-0115 ] ; 1997.
Abstract
Recent advances in the fields of molecular cloning and peptide purification necessitate a reappraisal of our views concerning the evolution of the genes encoding somatostatin-related peptides. The currently widely held view that the genomes of tetrapods contain only the preprosomatostatin-I (PSS-I) gene, encoding somatostatin-14, with a second preprosomatostatin gene being expressed only in teleost fish is no longer tenable. Identification of genes encoding both somatostatin-14 and the somatostatin-related peptide, cortistatin in mammals, identification of the PSS-I and PSS-II preprosomatostatin genes in amphibia, and the isolation of gene products from at least two non-allelic preprosomatostatin genes in lampreys suggests the alternative hypothesis that duplication of the PSS-I gene occurred early in evolution, predating or concomitant with the appearance of the chordates. We speculate that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. It is probable that the preprosomatostatin-II (PSS-II) gene, encoding [Tyr7,Gly10]somatostatin-14 or a related peptide, arose from a second independent duplication of the PSS-I gene in the ancestor of present-day teleost fish at a time after the divergence of the teleost stock from the line of evolution leading to tetrapods. The recent isolation of urotensin II, a peptide which contains a region of structural similarity but is not evolutionarily related to somatostatin-14, from the central nervous systems of lampreys, elasmobranchs and amphibia necessitates that we modify the accepted view that urotensin II is exclusively a product of the caudal neurosecretory system of teleost fish.
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DOI: 10.1016/S0167-0115(97)02135-6
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Tel.: +1 402 2801733; fax: +1 402 2802690; e-mail: jmconlon@creighton.edu</mods:affiliation></affiliation></author><author><name sortKey="Tostivint, Herve" sort="Tostivint, Herve" uniqKey="Tostivint H" first="Herve" last="Tostivint">Herve Tostivint</name><affiliation><mods:affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</mods:affiliation></affiliation></author><author><name sortKey="Vaudry, Hubert" sort="Vaudry, Hubert" uniqKey="Vaudry H" first="Hubert" last="Vaudry">Hubert Vaudry</name><affiliation><mods:affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37</idno><date when="1997" year="1997">1997</date><idno type="doi">10.1016/S0167-0115(97)02135-6</idno><idno type="url">https://api.istex.fr/document/A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001257</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001257</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</title><author><name sortKey="Conlon, J Michael" sort="Conlon, J Michael" uniqKey="Conlon J" first="J. Michael" last="Conlon">J. Michael Conlon</name><affiliation><mods:affiliation>Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University, Omaha, NE 68178, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Corresponding author. Tel.: +1 402 2801733; fax: +1 402 2802690; e-mail: jmconlon@creighton.edu</mods:affiliation></affiliation></author><author><name sortKey="Tostivint, Herve" sort="Tostivint, Herve" uniqKey="Tostivint H" first="Herve" last="Tostivint">Herve Tostivint</name><affiliation><mods:affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</mods:affiliation></affiliation></author><author><name sortKey="Vaudry, Hubert" sort="Vaudry, Hubert" uniqKey="Vaudry H" first="Hubert" last="Vaudry">Hubert Vaudry</name><affiliation><mods:affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Regulatory Peptides</title><title level="j" type="abbrev">REGPEP</title><idno type="ISSN">0167-0115</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">69</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="95">95</biblScope><biblScope unit="page" to="103">103</biblScope></imprint><idno type="ISSN">0167-0115</idno></series><idno type="istex">A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37</idno><idno type="DOI">10.1016/S0167-0115(97)02135-6</idno><idno type="PII">S0167-0115(97)02135-6</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-0115</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recent advances in the fields of molecular cloning and peptide purification necessitate a reappraisal of our views concerning the evolution of the genes encoding somatostatin-related peptides. The currently widely held view that the genomes of tetrapods contain only the preprosomatostatin-I (PSS-I) gene, encoding somatostatin-14, with a second preprosomatostatin gene being expressed only in teleost fish is no longer tenable. Identification of genes encoding both somatostatin-14 and the somatostatin-related peptide, cortistatin in mammals, identification of the PSS-I and PSS-II preprosomatostatin genes in amphibia, and the isolation of gene products from at least two non-allelic preprosomatostatin genes in lampreys suggests the alternative hypothesis that duplication of the PSS-I gene occurred early in evolution, predating or concomitant with the appearance of the chordates. We speculate that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. It is probable that the preprosomatostatin-II (PSS-II) gene, encoding [Tyr7,Gly10]somatostatin-14 or a related peptide, arose from a second independent duplication of the PSS-I gene in the ancestor of present-day teleost fish at a time after the divergence of the teleost stock from the line of evolution leading to tetrapods. The recent isolation of urotensin II, a peptide which contains a region of structural similarity but is not evolutionarily related to somatostatin-14, from the central nervous systems of lampreys, elasmobranchs and amphibia necessitates that we modify the accepted view that urotensin II is exclusively a product of the caudal neurosecretory system of teleost fish.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>J.Michael Conlon</name><affiliations><json:string>Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University, Omaha, NE 68178, USA</json:string><json:string>Corresponding author. Tel.: +1 402 2801733; fax: +1 402 2802690; e-mail: jmconlon@creighton.edu</json:string></affiliations></json:item><json:item><name>Herve Tostivint</name><affiliations><json:string>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</json:string></affiliations></json:item><json:item><name>Hubert Vaudry</name><affiliations><json:string>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Somatostatin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cortistatin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Urotensin II</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Gene duplication</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Recent advances in the fields of molecular cloning and peptide purification necessitate a reappraisal of our views concerning the evolution of the genes encoding somatostatin-related peptides. The currently widely held view that the genomes of tetrapods contain only the preprosomatostatin-I (PSS-I) gene, encoding somatostatin-14, with a second preprosomatostatin gene being expressed only in teleost fish is no longer tenable. Identification of genes encoding both somatostatin-14 and the somatostatin-related peptide, cortistatin in mammals, identification of the PSS-I and PSS-II preprosomatostatin genes in amphibia, and the isolation of gene products from at least two non-allelic preprosomatostatin genes in lampreys suggests the alternative hypothesis that duplication of the PSS-I gene occurred early in evolution, predating or concomitant with the appearance of the chordates. We speculate that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. It is probable that the preprosomatostatin-II (PSS-II) gene, encoding [Tyr7,Gly10]somatostatin-14 or a related peptide, arose from a second independent duplication of the PSS-I gene in the ancestor of present-day teleost fish at a time after the divergence of the teleost stock from the line of evolution leading to tetrapods. The recent isolation of urotensin II, a peptide which contains a region of structural similarity but is not evolutionarily related to somatostatin-14, from the central nervous systems of lampreys, elasmobranchs and amphibia necessitates that we modify the accepted view that urotensin II is exclusively a product of the caudal neurosecretory system of teleost fish.</abstract><qualityIndicators><score>7.964</score><pdfVersion>1.1</pdfVersion><pdfPageSize>580 x 800 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>4</keywordCount><abstractCharCount>1727</abstractCharCount><pdfWordCount>6634</pdfWordCount><pdfCharCount>43519</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>247</abstractWordCount></qualityIndicators><title>Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</title><pii><json:string>S0167-0115(97)02135-6</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>69</volume><pii><json:string>S0167-0115(00)X0030-4</json:string></pii><pages><last>103</last><first>95</first></pages><issn><json:string>0167-0115</json:string></issn><issue>2</issue><genre><json:string>journal</json:string></genre><language><json:string>unknown</json:string></language><title>Regulatory Peptides</title><publicationDate>1997</publicationDate></host><categories><wos><json:string>science</json:string><json:string>physiology</json:string><json:string>endocrinology & metabolism</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>clinical medicine</json:string><json:string>endocrinology & metabolism</json:string></scienceMetrix></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1016/S0167-0115(97)02135-6</json:string></doi><id>A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37</id><score>0.033787847</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>©1997 Elsevier Science B.V.</p></availability><date>1997</date></publicationStmt><notesStmt><note type="content">Fig. 1: A schematic representation of (a) frog preprosomatostatin-1 (PSS-1), (b) frog preprosomatostatin-2 (PSS-2), (c) rat preprocortistatin (PCS), (d) anglerfish preprosomatostatin-II (PSS-II) and (e) carp preprourotensin-II. The arrows indicate the cleavage sites that lead to generation of the mature peptides.</note><note type="content">Fig. 2: A comparison of the primary structures of peptides derived from prosomatostatin-I and containing the somatostatin-14 sequence (shown in bold type) from different vertebrate taxa. (—) Sequence identity: the frog, anglerfish and catfish sequences are deduced from the nucleotide sequence of a cDNA. Gaps denoted by (*) have been introduced into the amino acid sequences of the catfish and bowfin peptides to maximize structural similarity.</note><note type="content">Fig. 3: A comparison of the primary structures of peptides derived from prosomatostatin-II isolated from the Brockmann bodies of teleost fish. (—) Residue identity: (*) denotes a residue deletion that has been introduced to maximize sequence similarity. The [Tyr7,Gly10]somatostatin-14 sequence is shown in bold type.</note><note type="content">Fig. 4: A comparison of the primary structures of molecular variants of somatostatin-14 isolated from the tissues of phylogenetically ancient fish and from frog brain with the structure of rat corticostatin-14 deduced from the nucleotide sequence of a cDNA. (—) Residue identity; (*) residue deletion. The [Ser12]somatostatin-14 sequence is shown in bold type.</note><note type="content">Fig. 5: A comparison of the primary structures of (A) preprosomatostatin-1 (PSS-1) from rat and frog and (B) preprocortistatin (PCS) from rat and preprosomatostatin-2 (PSS-2) from frog as predicted from the nucleotide sequences of cloned cDNAs. The somatostatin-14 sequence is shown in bold type.</note><note type="content">Fig. 6: A comparison of the primary structures of urotensin II-related peptides isolated from tissues of either the caudal neurosecretory system or the central nervous system of species of different vertebrate taxa. (—) Residue identity; (*) residue deletion.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</title><author xml:id="author-1"><persName><forename type="first">J.Michael</forename><surname>Conlon</surname></persName><affiliation>Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University, Omaha, NE 68178, USA</affiliation><affiliation>Corresponding author. Tel.: +1 402 2801733; fax: +1 402 2802690; e-mail: jmconlon@creighton.edu</affiliation></author><author xml:id="author-2"><persName><forename type="first">Herve</forename><surname>Tostivint</surname></persName><affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Hubert</forename><surname>Vaudry</surname></persName><affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</affiliation></author></analytic><monogr><title level="j">Regulatory Peptides</title><title level="j" type="abbrev">REGPEP</title><idno type="pISSN">0167-0115</idno><idno type="PII">S0167-0115(00)X0030-4</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">69</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="95">95</biblScope><biblScope unit="page" to="103">103</biblScope></imprint></monogr><idno type="istex">A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37</idno><idno type="DOI">10.1016/S0167-0115(97)02135-6</idno><idno type="PII">S0167-0115(97)02135-6</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Recent advances in the fields of molecular cloning and peptide purification necessitate a reappraisal of our views concerning the evolution of the genes encoding somatostatin-related peptides. The currently widely held view that the genomes of tetrapods contain only the preprosomatostatin-I (PSS-I) gene, encoding somatostatin-14, with a second preprosomatostatin gene being expressed only in teleost fish is no longer tenable. Identification of genes encoding both somatostatin-14 and the somatostatin-related peptide, cortistatin in mammals, identification of the PSS-I and PSS-II preprosomatostatin genes in amphibia, and the isolation of gene products from at least two non-allelic preprosomatostatin genes in lampreys suggests the alternative hypothesis that duplication of the PSS-I gene occurred early in evolution, predating or concomitant with the appearance of the chordates. We speculate that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. It is probable that the preprosomatostatin-II (PSS-II) gene, encoding [Tyr7,Gly10]somatostatin-14 or a related peptide, arose from a second independent duplication of the PSS-I gene in the ancestor of present-day teleost fish at a time after the divergence of the teleost stock from the line of evolution leading to tetrapods. The recent isolation of urotensin II, a peptide which contains a region of structural similarity but is not evolutionarily related to somatostatin-14, from the central nervous systems of lampreys, elasmobranchs and amphibia necessitates that we modify the accepted view that urotensin II is exclusively a product of the caudal neurosecretory system of teleost fish.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Somatostatin</term></item><item><term>Cortistatin</term></item><item><term>Urotensin II</term></item><item><term>Gene duplication</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1997-02-05">Modified</change><change when="1997">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; 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:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity><istex:entity SYSTEM="gr5" NDATA="IMAGE" name="gr5"></istex:entity><istex:entity SYSTEM="gr6" NDATA="IMAGE" name="gr6"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>REGPEP</jid><aid>2135</aid><ce:pii>S0167-0115(97)02135-6</ce:pii><ce:doi>10.1016/S0167-0115(97)02135-6</ce:doi><ce:copyright year="1997" type="full-transfer">Elsevier Science B.V.</ce:copyright></item-info><head><ce:title>Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</ce:title><ce:author-group><ce:author><ce:given-name>J.Michael</ce:given-name><ce:surname>Conlon</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:author><ce:given-name>Herve</ce:given-name><ce:surname>Tostivint</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref></ce:author><ce:author><ce:given-name>Hubert</ce:given-name><ce:surname>Vaudry</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University, Omaha, NE 68178, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Tel.: +1 402 2801733; fax: +1 402 2802690; e-mail: jmconlon@creighton.edu</ce:text></ce:correspondence></ce:author-group><ce:date-received day="18" month="11" year="1996"></ce:date-received><ce:date-revised day="5" month="2" year="1997"></ce:date-revised><ce:date-accepted day="5" month="2" year="1997"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Recent advances in the fields of molecular cloning and peptide purification necessitate a reappraisal of our views concerning the evolution of the genes encoding somatostatin-related peptides. The currently widely held view that the genomes of tetrapods contain only the preprosomatostatin-I (PSS-I) gene, encoding somatostatin-14, with a second preprosomatostatin gene being expressed only in teleost fish is no longer tenable. Identification of genes encoding both somatostatin-14 and the somatostatin-related peptide, cortistatin in mammals, identification of the PSS-I and PSS-II preprosomatostatin genes in amphibia, and the isolation of gene products from at least two non-allelic preprosomatostatin genes in lampreys suggests the alternative hypothesis that duplication of the PSS-I gene occurred early in evolution, predating or concomitant with the appearance of the chordates. We speculate that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. It is probable that the preprosomatostatin-II (PSS-II) gene, encoding [Tyr<ce:sup>7</ce:sup>,Gly<ce:sup>10</ce:sup>]somatostatin-14 or a related peptide, arose from a second independent duplication of the PSS-I gene in the ancestor of present-day teleost fish at a time after the divergence of the teleost stock from the line of evolution leading to tetrapods. The recent isolation of urotensin II, a peptide which contains a region of structural similarity but is not evolutionarily related to somatostatin-14, from the central nervous systems of lampreys, elasmobranchs and amphibia necessitates that we modify the accepted view that urotensin II is exclusively a product of the caudal neurosecretory system of teleost fish.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Somatostatin</ce:text></ce:keyword><ce:keyword><ce:text>Cortistatin</ce:text></ce:keyword><ce:keyword><ce:text>Urotensin II</ce:text></ce:keyword><ce:keyword><ce:text>Gene duplication</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives</title></titleInfo><name type="personal"><namePart type="given">J.Michael</namePart><namePart type="family">Conlon</namePart><affiliation>Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University, Omaha, NE 68178, USA</affiliation><affiliation>Corresponding author. Tel.: +1 402 2801733; fax: +1 402 2802690; e-mail: jmconlon@creighton.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Herve</namePart><namePart type="family">Tostivint</namePart><affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hubert</namePart><namePart type="family">Vaudry</namePart><affiliation>European Institute for Peptide Research, Laboratory of Cellular and Molecular Neuroendocrinology INSERM U413, CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France</affiliation><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">1997</dateIssued><dateModified encoding="w3cdtf">1997-02-05</dateModified><copyrightDate encoding="w3cdtf">1997</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">Recent advances in the fields of molecular cloning and peptide purification necessitate a reappraisal of our views concerning the evolution of the genes encoding somatostatin-related peptides. The currently widely held view that the genomes of tetrapods contain only the preprosomatostatin-I (PSS-I) gene, encoding somatostatin-14, with a second preprosomatostatin gene being expressed only in teleost fish is no longer tenable. Identification of genes encoding both somatostatin-14 and the somatostatin-related peptide, cortistatin in mammals, identification of the PSS-I and PSS-II preprosomatostatin genes in amphibia, and the isolation of gene products from at least two non-allelic preprosomatostatin genes in lampreys suggests the alternative hypothesis that duplication of the PSS-I gene occurred early in evolution, predating or concomitant with the appearance of the chordates. We speculate that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. It is probable that the preprosomatostatin-II (PSS-II) gene, encoding [Tyr7,Gly10]somatostatin-14 or a related peptide, arose from a second independent duplication of the PSS-I gene in the ancestor of present-day teleost fish at a time after the divergence of the teleost stock from the line of evolution leading to tetrapods. The recent isolation of urotensin II, a peptide which contains a region of structural similarity but is not evolutionarily related to somatostatin-14, from the central nervous systems of lampreys, elasmobranchs and amphibia necessitates that we modify the accepted view that urotensin II is exclusively a product of the caudal neurosecretory system of teleost fish.</abstract><note type="content">Fig. 1: A schematic representation of (a) frog preprosomatostatin-1 (PSS-1), (b) frog preprosomatostatin-2 (PSS-2), (c) rat preprocortistatin (PCS), (d) anglerfish preprosomatostatin-II (PSS-II) and (e) carp preprourotensin-II. The arrows indicate the cleavage sites that lead to generation of the mature peptides.</note><note type="content">Fig. 2: A comparison of the primary structures of peptides derived from prosomatostatin-I and containing the somatostatin-14 sequence (shown in bold type) from different vertebrate taxa. (—) Sequence identity: the frog, anglerfish and catfish sequences are deduced from the nucleotide sequence of a cDNA. Gaps denoted by (*) have been introduced into the amino acid sequences of the catfish and bowfin peptides to maximize structural similarity.</note><note type="content">Fig. 3: A comparison of the primary structures of peptides derived from prosomatostatin-II isolated from the Brockmann bodies of teleost fish. (—) Residue identity: (*) denotes a residue deletion that has been introduced to maximize sequence similarity. The [Tyr7,Gly10]somatostatin-14 sequence is shown in bold type.</note><note type="content">Fig. 4: A comparison of the primary structures of molecular variants of somatostatin-14 isolated from the tissues of phylogenetically ancient fish and from frog brain with the structure of rat corticostatin-14 deduced from the nucleotide sequence of a cDNA. (—) Residue identity; (*) residue deletion. The [Ser12]somatostatin-14 sequence is shown in bold type.</note><note type="content">Fig. 5: A comparison of the primary structures of (A) preprosomatostatin-1 (PSS-1) from rat and frog and (B) preprocortistatin (PCS) from rat and preprosomatostatin-2 (PSS-2) from frog as predicted from the nucleotide sequences of cloned cDNAs. The somatostatin-14 sequence is shown in bold type.</note><note type="content">Fig. 6: A comparison of the primary structures of urotensin II-related peptides isolated from tissues of either the caudal neurosecretory system or the central nervous system of species of different vertebrate taxa. (—) Residue identity; (*) residue deletion.</note><subject><genre>Keywords</genre><topic>Somatostatin</topic><topic>Cortistatin</topic><topic>Urotensin II</topic><topic>Gene duplication</topic></subject><relatedItem type="host"><titleInfo><title>Regulatory Peptides</title></titleInfo><titleInfo type="abbreviated"><title>REGPEP</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19970326</dateIssued></originInfo><identifier type="ISSN">0167-0115</identifier><identifier type="PII">S0167-0115(00)X0030-4</identifier><part><date>19970326</date><detail type="volume"><number>69</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue pages"><start>53</start><end>112</end></extent><extent unit="pages"><start>95</start><end>103</end></extent></part></relatedItem><identifier type="istex">A54489F7DBFD61558D18C3292EFAAA7A9BB3FC37</identifier><identifier type="DOI">10.1016/S0167-0115(97)02135-6</identifier><identifier type="PII">S0167-0115(97)02135-6</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Elsevier Science B.V.</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Elsevier Science B.V., ©1997</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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