Duality of Gonadotropins in Gnathostomes
Identifieur interne : 000694 ( Istex/Corpus ); précédent : 000693; suivant : 000695Duality of Gonadotropins in Gnathostomes
Auteurs : Bruno Quérat ; Caroline Tonnerre-Doncarli ; Florence Géniès ; Christian SalmonSource :
- General and Comparative Endocrinology [ 0016-6480 ] ; 2001.
English descriptors
- KwdEn :
Abstract
The glycoprotein hormone α subunit and two β subunits were cloned from the ventral lobe of the pituitary gland of an elasmobranch fish, Scyliorhinus canicula. The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The Scyliorhinus β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The Scyliorhinus β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from Scyliorhinus displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that Scyliorhinus β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.
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DOI: 10.1006/gcen.2001.7715
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ISTEX:45CAB93523A1D7D586D5990940C3D78F935D05FCLe document en format XML
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The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The Scyliorhinus β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The Scyliorhinus β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from Scyliorhinus displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that Scyliorhinus β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Bruno Quérat</name><affiliations><json:string>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</json:string></affiliations></json:item><json:item><name>Caroline Tonnerre-Doncarli</name><affiliations><json:string>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</json:string></affiliations></json:item><json:item><name>Florence Géniès</name><affiliations><json:string>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</json:string></affiliations></json:item><json:item><name>Christian Salmon</name><affiliations><json:string>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>LH</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>FSH</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>gonadotropins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>elasmobranchs</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>The glycoprotein hormone α subunit and two β subunits were cloned from the ventral lobe of the pituitary gland of an elasmobranch fish, Scyliorhinus canicula. 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The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The Scyliorhinus β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The Scyliorhinus β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from Scyliorhinus displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that Scyliorhinus β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>LH</term></item><item><term>FSH</term></item><item><term>gonadotropins</term></item><item><term>elasmobranchs</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2001">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/45CAB93523A1D7D586D5990940C3D78F935D05FC/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>97715</aid><ce:pii>S0016-6480(01)97715-9</ce:pii><ce:doi>10.1006/gcen.2001.7715</ce:doi><ce:copyright type="full-transfer" year="2001">Elsevier Science (USA)</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Duality of Gonadotropins in Gnathostomes</ce:title><ce:author-group><ce:author><ce:given-name>Bruno</ce:given-name><ce:surname>Quérat</ce:surname></ce:author><ce:author><ce:given-name>Caroline</ce:given-name><ce:surname>Tonnerre-Doncarli</ce:surname></ce:author><ce:author><ce:given-name>Florence</ce:given-name><ce:surname>Géniès</ce:surname></ce:author><ce:author><ce:given-name>Christian</ce:given-name><ce:surname>Salmon</ce:surname></ce:author><ce:affiliation><ce:textfn>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</ce:textfn></ce:affiliation></ce:author-group><ce:date-accepted day="10" month="8" year="2001"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The glycoprotein hormone α subunit and two β subunits were cloned from the ventral lobe of the pituitary gland of an elasmobranch fish, <ce:italic>Scyliorhinus canicula</ce:italic>. The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The <ce:italic>Scyliorhinus</ce:italic> β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The <ce:italic>Scyliorhinus</ce:italic> β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from <ce:italic>Scyliorhinus</ce:italic> displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that <ce:italic>Scyliorhinus</ce:italic> β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>LH</ce:text></ce:keyword><ce:keyword><ce:text>FSH</ce:text></ce:keyword><ce:keyword><ce:text>gonadotropins</ce:text></ce:keyword><ce:keyword><ce:text>elasmobranchs</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Duality of Gonadotropins in Gnathostomes</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Duality of Gonadotropins in Gnathostomes</title></titleInfo><name type="personal"><namePart type="given">Bruno</namePart><namePart type="family">Quérat</namePart><affiliation>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Caroline</namePart><namePart type="family">Tonnerre-Doncarli</namePart><affiliation>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Florence</namePart><namePart type="family">Géniès</namePart><affiliation>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christian</namePart><namePart type="family">Salmon</namePart><affiliation>Laboratoire de Physiologie Générale et Comparée du Muséum National d'Histoire Naturelle, UMR 8572, 7, rue Cuvier, 75231, Paris Cedex 05, 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">2001</dateIssued><copyrightDate encoding="w3cdtf">2001</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 glycoprotein hormone α subunit and two β subunits were cloned from the ventral lobe of the pituitary gland of an elasmobranch fish, Scyliorhinus canicula. The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The Scyliorhinus β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The Scyliorhinus β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from Scyliorhinus displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that Scyliorhinus β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.</abstract><note type="content">Section title: Regular Article</note><subject lang="en"><genre>Keywords</genre><topic>LH</topic><topic>FSH</topic><topic>gonadotropins</topic><topic>elasmobranchs</topic></subject><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">200112</dateIssued></originInfo><identifier type="ISSN">0016-6480</identifier><identifier type="PII">S0016-6480(00)X0002-0</identifier><part><date>200112</date><detail type="volume"><number>124</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>257</start><end>388</end></extent><extent unit="pages"><start>308</start><end>314</end></extent></part></relatedItem><identifier type="istex">45CAB93523A1D7D586D5990940C3D78F935D05FC</identifier><identifier type="DOI">10.1006/gcen.2001.7715</identifier><identifier type="PII">S0016-6480(01)97715-9</identifier><accessCondition type="use and reproduction" contentType="copyright">©2001 Elsevier Science (USA)</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Elsevier Science (USA), ©2001</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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