Deciphering Posttranslational Processing Events in the Pituitary of a Neopterygian Fish: Cloning of a Gar Proopiomelanocortin cDNA
Identifieur interne : 000E88 ( Istex/Corpus ); précédent : 000E87; suivant : 000E89Deciphering Posttranslational Processing Events in the Pituitary of a Neopterygian Fish: Cloning of a Gar Proopiomelanocortin cDNA
Auteurs : Robert M. Dores ; Tana R. Smith ; David A. Rubin ; Phillip Danielson ; Luciano E. Marra ; John H. YousonSource :
- General and Comparative Endocrinology [ 0016-6480 ] ; 1997.
Abstract
A cDNA that codes for the polypeptide hormone precursor proopiomelanocortin (POMC) was cloned and sequenced from a gar (Lepisosteus osseus) pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 780-bp open reading frame. The deduced amino acid sequence for gar POMC is 259 amino acids in length. The general organization of gar POMC is very similar to that of other gnathostome POMC sequences. The β-endorphin sequence had 91% sequence identity with sockeye A β-endorphin and 71% sequence identity withXenopus laevisβ-endorphin. Three melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were detected. The gar α-MSH sequence was identical to the α-MSH sequence in rat POMC. The gar β-MSH sequence had 77% sequence identity with salmonid forms of β-MSH and 53% sequence identity with tetrapod forms of β-MSH. The γ-MSH region of gar POMC only had 26% primary sequence identity with tetrapod γ-MSH sequences. Gar γ-MSH had an incomplete MSH core sequence (HRF), an apparent internal deletion of five amino acids, and lacked flanking paired basic amino acids essential for proteolytic cleavage. The apparent degenerate nature of gar γ-MSH is discussed in light of the absence of this sequence in salmonid fish.
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DOI: 10.1006/gcen.1997.6947
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Youson</name><affiliation><mods:affiliation>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">General and Comparative Endocrinology</title><title level="j" type="abbrev">YGCEN</title><idno type="ISSN">0016-6480</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">107</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="401">401</biblScope><biblScope unit="page" to="413">413</biblScope></imprint><idno type="ISSN">0016-6480</idno></series><idno type="istex">02BD825C481E7FD86032FD519FE32ED3C5D61AE1</idno><idno type="DOI">10.1006/gcen.1997.6947</idno><idno type="PII">S0016-6480(97)96947-1</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0016-6480</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cDNA that codes for the polypeptide hormone precursor proopiomelanocortin (POMC) was cloned and sequenced from a gar (Lepisosteus osseus) pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 780-bp open reading frame. The deduced amino acid sequence for gar POMC is 259 amino acids in length. The general organization of gar POMC is very similar to that of other gnathostome POMC sequences. The β-endorphin sequence had 91% sequence identity with sockeye A β-endorphin and 71% sequence identity withXenopus laevisβ-endorphin. Three melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were detected. The gar α-MSH sequence was identical to the α-MSH sequence in rat POMC. The gar β-MSH sequence had 77% sequence identity with salmonid forms of β-MSH and 53% sequence identity with tetrapod forms of β-MSH. The γ-MSH region of gar POMC only had 26% primary sequence identity with tetrapod γ-MSH sequences. Gar γ-MSH had an incomplete MSH core sequence (HRF), an apparent internal deletion of five amino acids, and lacked flanking paired basic amino acids essential for proteolytic cleavage. The apparent degenerate nature of gar γ-MSH is discussed in light of the absence of this sequence in salmonid fish.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Robert M. Dores</name><affiliations><json:string>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</json:string></affiliations></json:item><json:item><name>Tana R. Smith</name><affiliations><json:string>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</json:string></affiliations></json:item><json:item><name>David A. Rubin</name><affiliations><json:string>Endocrine Unit, Massachusetts General Hospital, Harvard University Medical School, Boston, Massachusetts</json:string></affiliations></json:item><json:item><name>Phillip Danielson</name><affiliations><json:string>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</json:string></affiliations></json:item><json:item><name>Luciano E. Marra</name><affiliations><json:string>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</json:string></affiliations></json:item><json:item><name>John H. Youson</name><affiliations><json:string>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</json:string></affiliations></json:item></author><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>A cDNA that codes for the polypeptide hormone precursor proopiomelanocortin (POMC) was cloned and sequenced from a gar (Lepisosteus osseus) pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 780-bp open reading frame. The deduced amino acid sequence for gar POMC is 259 amino acids in length. The general organization of gar POMC is very similar to that of other gnathostome POMC sequences. The β-endorphin sequence had 91% sequence identity with sockeye A β-endorphin and 71% sequence identity withXenopus laevisβ-endorphin. Three melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were detected. The gar α-MSH sequence was identical to the α-MSH sequence in rat POMC. The gar β-MSH sequence had 77% sequence identity with salmonid forms of β-MSH and 53% sequence identity with tetrapod forms of β-MSH. The γ-MSH region of gar POMC only had 26% primary sequence identity with tetrapod γ-MSH sequences. Gar γ-MSH had an incomplete MSH core sequence (HRF), an apparent internal deletion of five amino acids, and lacked flanking paired basic amino acids essential for proteolytic cleavage. 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Hadley, Ed.</note><note type="content">Section title: Regular Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Deciphering Posttranslational Processing Events in the Pituitary of a Neopterygian Fish: Cloning of a Gar Proopiomelanocortin cDNA</title><author xml:id="author-1"><persName><forename type="first">Robert M.</forename><surname>Dores</surname></persName><note type="biography">To whom reprint requests should be addressed.</note><affiliation>To whom reprint requests should be addressed.</affiliation><affiliation>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</affiliation></author><author xml:id="author-2"><persName><forename type="first">Tana R.</forename><surname>Smith</surname></persName><affiliation>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</affiliation></author><author xml:id="author-3"><persName><forename type="first">David A.</forename><surname>Rubin</surname></persName><affiliation>Endocrine Unit, Massachusetts General Hospital, Harvard University Medical School, Boston, Massachusetts</affiliation></author><author xml:id="author-4"><persName><forename type="first">Phillip</forename><surname>Danielson</surname></persName><affiliation>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</affiliation></author><author xml:id="author-5"><persName><forename type="first">Luciano E.</forename><surname>Marra</surname></persName><affiliation>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</affiliation></author><author xml:id="author-6"><persName><forename type="first">John H.</forename><surname>Youson</surname></persName><affiliation>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</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)X0055-X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">107</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="401">401</biblScope><biblScope unit="page" to="413">413</biblScope></imprint></monogr><idno type="istex">02BD825C481E7FD86032FD519FE32ED3C5D61AE1</idno><idno type="DOI">10.1006/gcen.1997.6947</idno><idno type="PII">S0016-6480(97)96947-1</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>A cDNA that codes for the polypeptide hormone precursor proopiomelanocortin (POMC) was cloned and sequenced from a gar (Lepisosteus osseus) pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 780-bp open reading frame. The deduced amino acid sequence for gar POMC is 259 amino acids in length. The general organization of gar POMC is very similar to that of other gnathostome POMC sequences. The β-endorphin sequence had 91% sequence identity with sockeye A β-endorphin and 71% sequence identity withXenopus laevisβ-endorphin. Three melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were detected. The gar α-MSH sequence was identical to the α-MSH sequence in rat POMC. The gar β-MSH sequence had 77% sequence identity with salmonid forms of β-MSH and 53% sequence identity with tetrapod forms of β-MSH. The γ-MSH region of gar POMC only had 26% primary sequence identity with tetrapod γ-MSH sequences. Gar γ-MSH had an incomplete MSH core sequence (HRF), an apparent internal deletion of five amino acids, and lacked flanking paired basic amino acids essential for proteolytic cleavage. The apparent degenerate nature of gar γ-MSH is discussed in light of the absence of this sequence in salmonid fish.</p></abstract></profileDesc><revisionDesc><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/02BD825C481E7FD86032FD519FE32ED3C5D61AE1/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>96947</aid><ce:pii>S0016-6480(97)96947-1</ce:pii><ce:doi>10.1006/gcen.1997.6947</ce:doi><ce:copyright type="full-transfer" year="1997">Academic Press</ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>M. E. Hadley, Ed.</ce:note-para></ce:article-footnote><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Deciphering Posttranslational Processing Events in the Pituitary of a Neopterygian Fish: Cloning of a Gar Proopiomelanocortin cDNA</ce:title><ce:author-group><ce:author><ce:given-name>Robert M.</ce:given-name><ce:surname>Dores</ce:surname><ce:cross-ref refid="GC976947A0"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="GC976947FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Tana R.</ce:given-name><ce:surname>Smith</ce:surname><ce:cross-ref refid="GC976947A0"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>David A.</ce:given-name><ce:surname>Rubin</ce:surname><ce:cross-ref refid="GC976947A1"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Phillip</ce:given-name><ce:surname>Danielson</ce:surname><ce:cross-ref refid="GC976947A0"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Luciano E.</ce:given-name><ce:surname>Marra</ce:surname><ce:cross-ref refid="GC976947A2"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>John H.</ce:given-name><ce:surname>Youson</ce:surname><ce:cross-ref refid="GC976947A2"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="GC976947A0"><ce:label>a</ce:label><ce:textfn>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</ce:textfn></ce:affiliation><ce:affiliation id="GC976947A1"><ce:label>b</ce:label><ce:textfn>Endocrine Unit, Massachusetts General Hospital, Harvard University Medical School, Boston, Massachusetts</ce:textfn></ce:affiliation><ce:affiliation id="GC976947A2"><ce:label>c</ce:label><ce:textfn>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</ce:textfn></ce:affiliation><ce:footnote id="GC976947FN1"><ce:label>1</ce:label><ce:note-para>To whom reprint requests should be addressed.</ce:note-para></ce:footnote></ce:author-group><ce:date-accepted day="28" month="5" year="1997"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>A cDNA that codes for the polypeptide hormone precursor proopiomelanocortin (POMC) was cloned and sequenced from a gar (<ce:italic>Lepisosteus osseus</ce:italic>) pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 780-bp open reading frame. The deduced amino acid sequence for gar POMC is 259 amino acids in length. The general organization of gar POMC is very similar to that of other gnathostome POMC sequences. The β-endorphin sequence had 91% sequence identity with sockeye A β-endorphin and 71% sequence identity with<ce:italic>Xenopus laevis</ce:italic>β-endorphin. Three melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were detected. The gar α-MSH sequence was identical to the α-MSH sequence in rat POMC. The gar β-MSH sequence had 77% sequence identity with salmonid forms of β-MSH and 53% sequence identity with tetrapod forms of β-MSH. The γ-MSH region of gar POMC only had 26% primary sequence identity with tetrapod γ-MSH sequences. Gar γ-MSH had an incomplete MSH core sequence (HRF), an apparent internal deletion of five amino acids, and lacked flanking paired basic amino acids essential for proteolytic cleavage. The apparent degenerate nature of gar γ-MSH is discussed in light of the absence of this sequence in salmonid fish.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Deciphering Posttranslational Processing Events in the Pituitary of a Neopterygian Fish: Cloning of a Gar Proopiomelanocortin cDNA</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Deciphering Posttranslational Processing Events in the Pituitary of a Neopterygian Fish: Cloning of a Gar Proopiomelanocortin cDNA</title></titleInfo><name type="personal"><namePart type="given">Robert M.</namePart><namePart type="family">Dores</namePart><affiliation>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</affiliation><description>To whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Tana R.</namePart><namePart type="family">Smith</namePart><affiliation>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David A.</namePart><namePart type="family">Rubin</namePart><affiliation>Endocrine Unit, Massachusetts General Hospital, Harvard University Medical School, Boston, Massachusetts</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Phillip</namePart><namePart type="family">Danielson</namePart><affiliation>Department of Biological Sciences, University of Denver, Denver, Colorado, 80208</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Luciano E.</namePart><namePart type="family">Marra</namePart><affiliation>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John H.</namePart><namePart type="family">Youson</namePart><affiliation>Division of Life Sciences, University of Toronto, Scarborough Campus, Scarborough, Ontario, M1C 1A4, Canada</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><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">A cDNA that codes for the polypeptide hormone precursor proopiomelanocortin (POMC) was cloned and sequenced from a gar (Lepisosteus osseus) pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 780-bp open reading frame. The deduced amino acid sequence for gar POMC is 259 amino acids in length. The general organization of gar POMC is very similar to that of other gnathostome POMC sequences. The β-endorphin sequence had 91% sequence identity with sockeye A β-endorphin and 71% sequence identity withXenopus laevisβ-endorphin. Three melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were detected. The gar α-MSH sequence was identical to the α-MSH sequence in rat POMC. The gar β-MSH sequence had 77% sequence identity with salmonid forms of β-MSH and 53% sequence identity with tetrapod forms of β-MSH. The γ-MSH region of gar POMC only had 26% primary sequence identity with tetrapod γ-MSH sequences. Gar γ-MSH had an incomplete MSH core sequence (HRF), an apparent internal deletion of five amino acids, and lacked flanking paired basic amino acids essential for proteolytic cleavage. The apparent degenerate nature of gar γ-MSH is discussed in light of the absence of this sequence in salmonid fish.</abstract><note>M. E. Hadley, Ed.</note><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">199709</dateIssued></originInfo><identifier type="ISSN">0016-6480</identifier><identifier type="PII">S0016-6480(00)X0055-X</identifier><part><date>199709</date><detail type="volume"><number>107</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>291</start><end>462</end></extent><extent unit="pages"><start>401</start><end>413</end></extent></part></relatedItem><identifier type="istex">02BD825C481E7FD86032FD519FE32ED3C5D61AE1</identifier><identifier type="DOI">10.1006/gcen.1997.6947</identifier><identifier type="PII">S0016-6480(97)96947-1</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Academic Press</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Academic Press, ©1997</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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