Neuropeptide families and their receptors: evolutionary perspectives
Identifieur interne : 000889 ( Main/Corpus ); précédent : 000888; suivant : 000890Neuropeptide families and their receptors: evolutionary perspectives
Auteurs : Charles H. V. HoyleSource :
- Brain Research [ 0006-8993 ] ; 1999.
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Abstract
Examination of families of neuropeptides and their receptors can provide information about phyletic relationships and evolutionary processes. Within an individual a given signal molecule may serve many diverse functions, mediated via subtypes of the receptor which may be coupled to their transduction mechanisms in different ways. The rate of evolution of a peptide may reflect or be reflected in the rate of evolution of its receptor. For example, in the neuropeptide Y (NPY) family, pancreatic polypeptide (PP) shows significant structural diversity, while NPY is highly conserved. Molecular forms of a given subtype of NPY receptor that is selectively activated by NPY (Y1 or Y2 or Y5) are also highly conserved, but the subtype that is primarily activated by PP (Y4), shows remarkable diversity. Also, between receptor subtypes there can be remarkable diversity. This is evident in several neuropeptide families, where a neuropeptide sequence is highly conserved across a wide range of species but where the receptor homology of subtypes with species tends to be much lower than homology between species. For example, human and rat vasopressin are identical, but the human V1- or V2-vasopressin receptors are approximately 80% homologous with rat V1- or V2-receptors, but within humans or rats the V1-receptor is less than 50% homologous with the V2-receptor. Furthermore, duplication of an ancestral gene is thought to have led to the co-presence in eutherian mammals of oxytocin and vasopressin, which have maintained a close structural similarity, yet in many species the oxytocin receptor is only 30 to 50% homologous with vasopressin receptors. Thus it appears that there has been greater evolutionary pressure to conserve the signal molecule, than to conserve the structure of the receptor. Evaluation of the evolution of neuropeptides and their receptors may be useful in determining phyletic relationships. Traditional classification places the guinea pig as a hystricomorph rodent within the same order (Rodentia) as the muriform or myomorph rat and mouse. However, molecular analyses of polypeptides have led to the suggestion that guinea pigs belong to a distinct order. Analysis of several neuropeptide sequences and the Y4 receptor supports this view. In general terms for both neuropeptides and receptors, sequence homology reflects phylogeny and taxonomy as based on morphological features. Within the oxytocin/vasopressin family in which peptides and receptors have been characterised in invertebrate representatives as well as fish and amphibia in addition to mammals, the molecular diversity correlates well with evolutionary diversity.
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DOI: 10.1016/S0006-8993(99)01975-7
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Hoyle</name><affiliation><mods:affiliation>Department of Anatomy and Developmental Biology, and Centre for Neuroscience, University College London, Gower Street, London WC1E 6BT, UK</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773</idno><date when="1999" year="1999">1999</date><idno type="doi">10.1016/S0006-8993(99)01975-7</idno><idno type="url">https://api.istex.fr/document/4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000889</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Neuropeptide families and their receptors: evolutionary perspectives</title><author><name sortKey="Hoyle, Charles H V" sort="Hoyle, Charles H V" uniqKey="Hoyle C" first="Charles H. V." last="Hoyle">Charles H. V. Hoyle</name><affiliation><mods:affiliation>Department of Anatomy and Developmental Biology, and Centre for Neuroscience, University College London, Gower Street, London WC1E 6BT, UK</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Brain Research</title><title level="j" type="abbrev">BRES</title><idno type="ISSN">0006-8993</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999">1999</date><biblScope unit="volume">848</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="25">25</biblScope></imprint><idno type="ISSN">0006-8993</idno></series><idno type="istex">4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773</idno><idno type="DOI">10.1016/S0006-8993(99)01975-7</idno><idno type="PII">S0006-8993(99)01975-7</idno><idno type="ArticleID">19074</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-8993</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Evolution</term><term>Neuropeptide</term><term>Neuropeptide Y</term><term>Oxytocin</term><term>Receptor</term><term>Vasopressin</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Examination of families of neuropeptides and their receptors can provide information about phyletic relationships and evolutionary processes. Within an individual a given signal molecule may serve many diverse functions, mediated via subtypes of the receptor which may be coupled to their transduction mechanisms in different ways. The rate of evolution of a peptide may reflect or be reflected in the rate of evolution of its receptor. For example, in the neuropeptide Y (NPY) family, pancreatic polypeptide (PP) shows significant structural diversity, while NPY is highly conserved. Molecular forms of a given subtype of NPY receptor that is selectively activated by NPY (Y1 or Y2 or Y5) are also highly conserved, but the subtype that is primarily activated by PP (Y4), shows remarkable diversity. Also, between receptor subtypes there can be remarkable diversity. This is evident in several neuropeptide families, where a neuropeptide sequence is highly conserved across a wide range of species but where the receptor homology of subtypes with species tends to be much lower than homology between species. For example, human and rat vasopressin are identical, but the human V1- or V2-vasopressin receptors are approximately 80% homologous with rat V1- or V2-receptors, but within humans or rats the V1-receptor is less than 50% homologous with the V2-receptor. Furthermore, duplication of an ancestral gene is thought to have led to the co-presence in eutherian mammals of oxytocin and vasopressin, which have maintained a close structural similarity, yet in many species the oxytocin receptor is only 30 to 50% homologous with vasopressin receptors. Thus it appears that there has been greater evolutionary pressure to conserve the signal molecule, than to conserve the structure of the receptor. Evaluation of the evolution of neuropeptides and their receptors may be useful in determining phyletic relationships. Traditional classification places the guinea pig as a hystricomorph rodent within the same order (Rodentia) as the muriform or myomorph rat and mouse. However, molecular analyses of polypeptides have led to the suggestion that guinea pigs belong to a distinct order. Analysis of several neuropeptide sequences and the Y4 receptor supports this view. In general terms for both neuropeptides and receptors, sequence homology reflects phylogeny and taxonomy as based on morphological features. Within the oxytocin/vasopressin family in which peptides and receptors have been characterised in invertebrate representatives as well as fish and amphibia in addition to mammals, the molecular diversity correlates well with evolutionary diversity.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Charles H.V. Hoyle</name><affiliations><json:string>Department of Anatomy and Developmental Biology, and Centre for Neuroscience, University College London, Gower Street, London WC1E 6BT, UK</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Neuropeptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Evolution</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Oxytocin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Vasopressin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Neuropeptide Y</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Receptor</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Examination of families of neuropeptides and their receptors can provide information about phyletic relationships and evolutionary processes. Within an individual a given signal molecule may serve many diverse functions, mediated via subtypes of the receptor which may be coupled to their transduction mechanisms in different ways. The rate of evolution of a peptide may reflect or be reflected in the rate of evolution of its receptor. For example, in the neuropeptide Y (NPY) family, pancreatic polypeptide (PP) shows significant structural diversity, while NPY is highly conserved. Molecular forms of a given subtype of NPY receptor that is selectively activated by NPY (Y1 or Y2 or Y5) are also highly conserved, but the subtype that is primarily activated by PP (Y4), shows remarkable diversity. Also, between receptor subtypes there can be remarkable diversity. This is evident in several neuropeptide families, where a neuropeptide sequence is highly conserved across a wide range of species but where the receptor homology of subtypes with species tends to be much lower than homology between species. For example, human and rat vasopressin are identical, but the human V1- or V2-vasopressin receptors are approximately 80% homologous with rat V1- or V2-receptors, but within humans or rats the V1-receptor is less than 50% homologous with the V2-receptor. Furthermore, duplication of an ancestral gene is thought to have led to the co-presence in eutherian mammals of oxytocin and vasopressin, which have maintained a close structural similarity, yet in many species the oxytocin receptor is only 30 to 50% homologous with vasopressin receptors. Thus it appears that there has been greater evolutionary pressure to conserve the signal molecule, than to conserve the structure of the receptor. Evaluation of the evolution of neuropeptides and their receptors may be useful in determining phyletic relationships. Traditional classification places the guinea pig as a hystricomorph rodent within the same order (Rodentia) as the muriform or myomorph rat and mouse. However, molecular analyses of polypeptides have led to the suggestion that guinea pigs belong to a distinct order. Analysis of several neuropeptide sequences and the Y4 receptor supports this view. In general terms for both neuropeptides and receptors, sequence homology reflects phylogeny and taxonomy as based on morphological features. Within the oxytocin/vasopressin family in which peptides and receptors have been characterised in invertebrate representatives as well as fish and amphibia in addition to mammals, the molecular diversity correlates well with evolutionary diversity.</abstract><qualityIndicators><score>8</score><pdfVersion>1.2</pdfVersion><pdfPageSize>595 x 758 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>6</keywordCount><abstractCharCount>2659</abstractCharCount><pdfWordCount>15802</pdfWordCount><pdfCharCount>103248</pdfCharCount><pdfPageCount>25</pdfPageCount><abstractWordCount>397</abstractWordCount></qualityIndicators><title>Neuropeptide families and their receptors: evolutionary perspectives</title><pii><json:string>S0006-8993(99)01975-7</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>848</volume><pii><json:string>S0006-8993(00)X0246-6</json:string></pii><pages><last>25</last><first>1</first></pages><issn><json:string>0006-8993</json:string></issn><issue>1–2</issue><genre></genre><language><json:string>unknown</json:string></language><title>Brain Research</title><publicationDate>1999</publicationDate></host><publicationDate>1999</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1016/S0006-8993(99)01975-7</json:string></doi><id>4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Neuropeptide families and their receptors: evolutionary perspectives</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1999</date></publicationStmt><notesStmt><note type="content">Section title: Interactive report</note><note type="content">Fig. 1: Schematic diagram of the evolution of NPY/PYY/PY/PP family genes. Relationships are based on known peptide sequences and cDNA sequences.</note><note type="content">Fig. 2: Phylogenetic relationships amongst NPY-family receptors. The dendrogram was obtained from G-Protein Coupled Receptor Database http://www.gcrdb.uthscsa.edu.</note><note type="content">Fig. 3: Schematic diagram of the evolution of vertebrate oxytocin/vasopressin family genes. Relationships are based on known peptide sequences, cDNA sequences and phylogenetic relationships. Variants that appear to be evolutionary endings, and are not involved in progression, are indicated by dashed connectors. AspT, aspargtocin; AsvT, asvatocin; AVP, Arg8-vasopressin; Hyd, hydrins; IT, isotocin; LVP, Lys8-vasopressin; MT, mesotocin; OT, oxytocin; PhaT, phasvatocin; SIT, [Ser3, Ile8]oxytocin; ST, seritocin.</note><note type="content">Fig. 4: Phylogenetic relationships amongst oxytocin/vasopressin family receptors. V1A, V1B, V2 are vasopressin receptors V1A, V1B and V2; IT, MT and OT are isotocin, mesotocin and oxytocin receptors, respectively; LCSPR1 and LSCPR2 are Lymnaea stagnalis conopressin receptors. The dendrogram was obtained from G-Protein Coupled Receptor Database http://www.gcrdb.uthscsa.edu.</note><note type="content">Table 1: NPY superfamily: molecular forms of neuropeptide Y (NPY), peptide YY (PYY), peptide Y (PY) and pancreatic polypeptide (PP)</note><note type="content">Table 2: Sequences of signal peptides of prepro-NPY family peptides</note><note type="content">Table 3: Architecture of NPY, PPY, PYY, PY and PP precursors</note><note type="content">Table 4: Sequences of C-terminals of NPY family prepropepetides</note><note type="content">Table 5: Comparison of amino acid sequences of Drosophila melanogaster NPY-receptor (YR) and Mus musculus Y2 receptor (Y2R)</note><note type="content">Table 6: Amino acid sequences of oxytocin and vasopressin homologs</note><note type="content">Table 7: Architecture of oxytocin/vasopressin family precursors</note><note type="content">Table 8: Comparison of the amino acid sequences of the human vasopressin V2 receptor (V2R) with the Lymnaea stagnalis conopressin receptor-1 (LSCPR1)</note><note type="content">Table 9: Comparison of the amino acid sequences of the Catostomus commersoni isotocin receptor (ITR) and vasotocin receptor (VTR) with the Lymnaea stagnalis conopressin receptor-2 (LSCPR2)</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Neuropeptide families and their receptors: evolutionary perspectives</title><author><persName><forename type="first">Charles H.V.</forename><surname>Hoyle</surname></persName><note type="biography">Tel.: +44-171-504-2215, Fax: +44-171-380-7349, E-mail: c.hoyle@ucl.ac.uk</note><affiliation>Department of Anatomy and Developmental Biology, and Centre for Neuroscience, University College London, Gower Street, London WC1E 6BT, UK</affiliation></author></analytic><monogr><title level="j">Brain Research</title><title level="j" type="abbrev">BRES</title><idno type="pISSN">0006-8993</idno><idno type="PII">S0006-8993(00)X0246-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999"></date><biblScope unit="volume">848</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="25">25</biblScope></imprint></monogr><idno type="istex">4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773</idno><idno type="DOI">10.1016/S0006-8993(99)01975-7</idno><idno type="PII">S0006-8993(99)01975-7</idno><idno type="ArticleID">19074</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1999</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Examination of families of neuropeptides and their receptors can provide information about phyletic relationships and evolutionary processes. Within an individual a given signal molecule may serve many diverse functions, mediated via subtypes of the receptor which may be coupled to their transduction mechanisms in different ways. The rate of evolution of a peptide may reflect or be reflected in the rate of evolution of its receptor. For example, in the neuropeptide Y (NPY) family, pancreatic polypeptide (PP) shows significant structural diversity, while NPY is highly conserved. Molecular forms of a given subtype of NPY receptor that is selectively activated by NPY (Y1 or Y2 or Y5) are also highly conserved, but the subtype that is primarily activated by PP (Y4), shows remarkable diversity. Also, between receptor subtypes there can be remarkable diversity. This is evident in several neuropeptide families, where a neuropeptide sequence is highly conserved across a wide range of species but where the receptor homology of subtypes with species tends to be much lower than homology between species. For example, human and rat vasopressin are identical, but the human V1- or V2-vasopressin receptors are approximately 80% homologous with rat V1- or V2-receptors, but within humans or rats the V1-receptor is less than 50% homologous with the V2-receptor. Furthermore, duplication of an ancestral gene is thought to have led to the co-presence in eutherian mammals of oxytocin and vasopressin, which have maintained a close structural similarity, yet in many species the oxytocin receptor is only 30 to 50% homologous with vasopressin receptors. Thus it appears that there has been greater evolutionary pressure to conserve the signal molecule, than to conserve the structure of the receptor. Evaluation of the evolution of neuropeptides and their receptors may be useful in determining phyletic relationships. Traditional classification places the guinea pig as a hystricomorph rodent within the same order (Rodentia) as the muriform or myomorph rat and mouse. However, molecular analyses of polypeptides have led to the suggestion that guinea pigs belong to a distinct order. Analysis of several neuropeptide sequences and the Y4 receptor supports this view. In general terms for both neuropeptides and receptors, sequence homology reflects phylogeny and taxonomy as based on morphological features. Within the oxytocin/vasopressin family in which peptides and receptors have been characterised in invertebrate representatives as well as fish and amphibia in addition to mammals, the molecular diversity correlates well with evolutionary diversity.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Neuropeptide</term></item><item><term>Evolution</term></item><item><term>Oxytocin</term></item><item><term>Vasopressin</term></item><item><term>Neuropeptide Y</term></item><item><term>Receptor</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1999-08-13">Registration</change><change when="1999">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773/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="fx1" NDATA="IMAGE" name="fx1"></istex:entity><istex:entity SYSTEM="fx2" NDATA="IMAGE" name="fx2"></istex:entity><istex:entity SYSTEM="fx3" NDATA="IMAGE" name="fx3"></istex:entity><istex:entity SYSTEM="fx4" NDATA="IMAGE" name="fx4"></istex:entity><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:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>BRES</jid><aid>19074</aid><ce:pii>S0006-8993(99)01975-7</ce:pii><ce:doi>10.1016/S0006-8993(99)01975-7</ce:doi><ce:copyright year="1999" type="full-transfer">Elsevier Science B.V.</ce:copyright></item-info><head><ce:dochead><ce:textfn>Interactive report</ce:textfn></ce:dochead><ce:title>Neuropeptide families and their receptors: evolutionary perspectives</ce:title><ce:author-group><ce:author><ce:given-name>Charles H.V.</ce:given-name><ce:surname>Hoyle</ce:surname><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Department of Anatomy and Developmental Biology, and Centre for Neuroscience, University College London, Gower Street, London WC1E 6BT, UK</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Tel.: +44-171-504-2215, Fax: +44-171-380-7349, E-mail: c.hoyle@ucl.ac.uk</ce:text></ce:correspondence></ce:author-group><ce:date-accepted day="13" month="8" year="1999"></ce:date-accepted><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0120">Examination of families of neuropeptides and their receptors can provide information about phyletic relationships and evolutionary processes. Within an individual a given signal molecule may serve many diverse functions, mediated via subtypes of the receptor which may be coupled to their transduction mechanisms in different ways. The rate of evolution of a peptide may reflect or be reflected in the rate of evolution of its receptor. For example, in the neuropeptide Y (NPY) family, pancreatic polypeptide (PP) shows significant structural diversity, while NPY is highly conserved. Molecular forms of a given subtype of NPY receptor that is selectively activated by NPY (Y1 or Y2 or Y5) are also highly conserved, but the subtype that is primarily activated by PP (Y4), shows remarkable diversity. Also, between receptor subtypes there can be remarkable diversity. This is evident in several neuropeptide families, where a neuropeptide sequence is highly conserved across a wide range of species but where the receptor homology of subtypes with species tends to be much lower than homology between species. For example, human and rat vasopressin are identical, but the human V<ce:inf loc="post">1</ce:inf>- or V<ce:inf loc="post">2</ce:inf>-vasopressin receptors are approximately 80% homologous with rat V<ce:inf loc="post">1</ce:inf>- or V<ce:inf loc="post">2</ce:inf>-receptors, but within humans or rats the V<ce:inf loc="post">1</ce:inf>-receptor is less than 50% homologous with the V<ce:inf loc="post">2</ce:inf>-receptor. Furthermore, duplication of an ancestral gene is thought to have led to the co-presence in eutherian mammals of oxytocin and vasopressin, which have maintained a close structural similarity, yet in many species the oxytocin receptor is only 30 to 50% homologous with vasopressin receptors. Thus it appears that there has been greater evolutionary pressure to conserve the signal molecule, than to conserve the structure of the receptor. Evaluation of the evolution of neuropeptides and their receptors may be useful in determining phyletic relationships. Traditional classification places the guinea pig as a hystricomorph rodent within the same order (Rodentia) as the muriform or myomorph rat and mouse. However, molecular analyses of polypeptides have led to the suggestion that guinea pigs belong to a distinct order. Analysis of several neuropeptide sequences and the Y4 receptor supports this view. In general terms for both neuropeptides and receptors, sequence homology reflects phylogeny and taxonomy as based on morphological features. Within the oxytocin/vasopressin family in which peptides and receptors have been characterised in invertebrate representatives as well as fish and amphibia in addition to mammals, the molecular diversity correlates well with evolutionary diversity.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Neuropeptide</ce:text></ce:keyword><ce:keyword><ce:text>Evolution</ce:text></ce:keyword><ce:keyword><ce:text>Oxytocin</ce:text></ce:keyword><ce:keyword><ce:text>Vasopressin</ce:text></ce:keyword><ce:keyword><ce:text>Neuropeptide Y</ce:text></ce:keyword><ce:keyword><ce:text>Receptor</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Neuropeptide families and their receptors: evolutionary perspectives</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Neuropeptide families and their receptors: evolutionary perspectives</title></titleInfo><name type="personal"><namePart type="given">Charles H.V.</namePart><namePart type="family">Hoyle</namePart><affiliation>Department of Anatomy and Developmental Biology, and Centre for Neuroscience, University College London, Gower Street, London WC1E 6BT, UK</affiliation><description>Tel.: +44-171-504-2215, Fax: +44-171-380-7349, E-mail: c.hoyle@ucl.ac.uk</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><dateValid encoding="w3cdtf">1999-08-13</dateValid><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">Examination of families of neuropeptides and their receptors can provide information about phyletic relationships and evolutionary processes. Within an individual a given signal molecule may serve many diverse functions, mediated via subtypes of the receptor which may be coupled to their transduction mechanisms in different ways. The rate of evolution of a peptide may reflect or be reflected in the rate of evolution of its receptor. For example, in the neuropeptide Y (NPY) family, pancreatic polypeptide (PP) shows significant structural diversity, while NPY is highly conserved. Molecular forms of a given subtype of NPY receptor that is selectively activated by NPY (Y1 or Y2 or Y5) are also highly conserved, but the subtype that is primarily activated by PP (Y4), shows remarkable diversity. Also, between receptor subtypes there can be remarkable diversity. This is evident in several neuropeptide families, where a neuropeptide sequence is highly conserved across a wide range of species but where the receptor homology of subtypes with species tends to be much lower than homology between species. For example, human and rat vasopressin are identical, but the human V1- or V2-vasopressin receptors are approximately 80% homologous with rat V1- or V2-receptors, but within humans or rats the V1-receptor is less than 50% homologous with the V2-receptor. Furthermore, duplication of an ancestral gene is thought to have led to the co-presence in eutherian mammals of oxytocin and vasopressin, which have maintained a close structural similarity, yet in many species the oxytocin receptor is only 30 to 50% homologous with vasopressin receptors. Thus it appears that there has been greater evolutionary pressure to conserve the signal molecule, than to conserve the structure of the receptor. Evaluation of the evolution of neuropeptides and their receptors may be useful in determining phyletic relationships. Traditional classification places the guinea pig as a hystricomorph rodent within the same order (Rodentia) as the muriform or myomorph rat and mouse. However, molecular analyses of polypeptides have led to the suggestion that guinea pigs belong to a distinct order. Analysis of several neuropeptide sequences and the Y4 receptor supports this view. In general terms for both neuropeptides and receptors, sequence homology reflects phylogeny and taxonomy as based on morphological features. Within the oxytocin/vasopressin family in which peptides and receptors have been characterised in invertebrate representatives as well as fish and amphibia in addition to mammals, the molecular diversity correlates well with evolutionary diversity.</abstract><note type="content">Section title: Interactive report</note><note type="content">Fig. 1: Schematic diagram of the evolution of NPY/PYY/PY/PP family genes. Relationships are based on known peptide sequences and cDNA sequences.</note><note type="content">Fig. 2: Phylogenetic relationships amongst NPY-family receptors. The dendrogram was obtained from G-Protein Coupled Receptor Database http://www.gcrdb.uthscsa.edu.</note><note type="content">Fig. 3: Schematic diagram of the evolution of vertebrate oxytocin/vasopressin family genes. Relationships are based on known peptide sequences, cDNA sequences and phylogenetic relationships. Variants that appear to be evolutionary endings, and are not involved in progression, are indicated by dashed connectors. AspT, aspargtocin; AsvT, asvatocin; AVP, Arg8-vasopressin; Hyd, hydrins; IT, isotocin; LVP, Lys8-vasopressin; MT, mesotocin; OT, oxytocin; PhaT, phasvatocin; SIT, [Ser3, Ile8]oxytocin; ST, seritocin.</note><note type="content">Fig. 4: Phylogenetic relationships amongst oxytocin/vasopressin family receptors. V1A, V1B, V2 are vasopressin receptors V1A, V1B and V2; IT, MT and OT are isotocin, mesotocin and oxytocin receptors, respectively; LCSPR1 and LSCPR2 are Lymnaea stagnalis conopressin receptors. The dendrogram was obtained from G-Protein Coupled Receptor Database http://www.gcrdb.uthscsa.edu.</note><note type="content">Table 1: NPY superfamily: molecular forms of neuropeptide Y (NPY), peptide YY (PYY), peptide Y (PY) and pancreatic polypeptide (PP)</note><note type="content">Table 2: Sequences of signal peptides of prepro-NPY family peptides</note><note type="content">Table 3: Architecture of NPY, PPY, PYY, PY and PP precursors</note><note type="content">Table 4: Sequences of C-terminals of NPY family prepropepetides</note><note type="content">Table 5: Comparison of amino acid sequences of Drosophila melanogaster NPY-receptor (YR) and Mus musculus Y2 receptor (Y2R)</note><note type="content">Table 6: Amino acid sequences of oxytocin and vasopressin homologs</note><note type="content">Table 7: Architecture of oxytocin/vasopressin family precursors</note><note type="content">Table 8: Comparison of the amino acid sequences of the human vasopressin V2 receptor (V2R) with the Lymnaea stagnalis conopressin receptor-1 (LSCPR1)</note><note type="content">Table 9: Comparison of the amino acid sequences of the Catostomus commersoni isotocin receptor (ITR) and vasotocin receptor (VTR) with the Lymnaea stagnalis conopressin receptor-2 (LSCPR2)</note><subject lang="en"><genre>Keywords</genre><topic>Neuropeptide</topic><topic>Evolution</topic><topic>Oxytocin</topic><topic>Vasopressin</topic><topic>Neuropeptide Y</topic><topic>Receptor</topic></subject><relatedItem type="host"><titleInfo><title>Brain Research</title></titleInfo><titleInfo type="abbreviated"><title>BRES</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19991127</dateIssued></originInfo><identifier type="ISSN">0006-8993</identifier><identifier type="PII">S0006-8993(00)X0246-6</identifier><part><date>19991127</date><detail type="volume"><number>848</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>198</end></extent><extent unit="issue pages"><start>A1</start><end>A47</end></extent><extent unit="pages"><start>1</start><end>25</end></extent></part></relatedItem><identifier type="istex">4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773</identifier><identifier type="DOI">10.1016/S0006-8993(99)01975-7</identifier><identifier type="PII">S0006-8993(99)01975-7</identifier><identifier type="ArticleID">19074</identifier><accessCondition type="use and reproduction" contentType="">© 1999Elsevier Science B.V.</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Elsevier Science B.V., ©1999</recordOrigin></recordInfo></mods></metadata><enrichments><istex:refBibTEI uri="https://api.istex.fr/document/4AE81118CD6FE7EBF0090FE0C4ADE3E30F1F6773/enrichments/refBib"><teiHeader></teiHeader><text><front></front><body></body><back><listBibl><biblStruct><analytic><title level="a" type="main">Holocephalian fish, the ratfish Hydrolagus colliei</title></analytic><monogr><title level="j">Gen. 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