Cloning and expression of two proopiomelanocortin mRNAs in the common carp ( Cyprinus carpio L.)
Identifieur interne : 000D97 ( Istex/Corpus ); précédent : 000D96; suivant : 000D98Cloning and expression of two proopiomelanocortin mRNAs in the common carp ( Cyprinus carpio L.)
Auteurs : R. J Arends ; H. Vermeer ; G. J. M Martens ; J. A. M Leunissen ; S. E Wendelaar Bonga ; G. FlikSource :
- Molecular and Cellular Endocrinology [ 0303-7207 ] ; 1998.
English descriptors
Abstract
Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), α-melanocyte-stimulating hormone (α-MSH) and β-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and β-MSH domain, two amino acid substitutions are found, whereas α-MSH and β-endorphin are identical. For β-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.
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DOI: 10.1016/S0303-7207(98)00139-7
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M Martens</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Leunissen, J A M" sort="Leunissen, J A M" uniqKey="Leunissen J" first="J. A. M" last="Leunissen">J. A. M Leunissen</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Wendelaar Bonga, S E" sort="Wendelaar Bonga, S E" uniqKey="Wendelaar Bonga S" first="S. E" last="Wendelaar Bonga">S. E Wendelaar Bonga</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Flik, G" sort="Flik, G" uniqKey="Flik G" first="G" last="Flik">G. 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J" last="Arends">R. J Arends</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Vermeer, H" sort="Vermeer, H" uniqKey="Vermeer H" first="H" last="Vermeer">H. Vermeer</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Martens, G J M" sort="Martens, G J M" uniqKey="Martens G" first="G. J. M" last="Martens">G. J. M Martens</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Leunissen, J A M" sort="Leunissen, J A M" uniqKey="Leunissen J" first="J. A. M" last="Leunissen">J. A. M Leunissen</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Wendelaar Bonga, S E" sort="Wendelaar Bonga, S E" uniqKey="Wendelaar Bonga S" first="S. E" last="Wendelaar Bonga">S. E Wendelaar Bonga</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Flik, G" sort="Flik, G" uniqKey="Flik G" first="G" last="Flik">G. Flik</name><affiliation><mods:affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular and Cellular Endocrinology</title><title level="j" type="abbrev">MCE</title><idno type="ISSN">0303-7207</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">143</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="23">23</biblScope><biblScope unit="page" to="31">31</biblScope></imprint><idno type="ISSN">0303-7207</idno></series><idno type="istex">29245DA3823A5D9BAB4C7241325AA5A42F046044</idno><idno type="DOI">10.1016/S0303-7207(98)00139-7</idno><idno type="PII">S0303-7207(98)00139-7</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0303-7207</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning</term><term>Common carp</term><term>Phylogeny</term><term>Proopiomelanocortin</term><term>Sequence analysis</term><term>mRNA expression</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), α-melanocyte-stimulating hormone (α-MSH) and β-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and β-MSH domain, two amino acid substitutions are found, whereas α-MSH and β-endorphin are identical. For β-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>R.J Arends</name><affiliations><json:string>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</json:string></affiliations></json:item><json:item><name>H Vermeer</name><affiliations><json:string>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</json:string></affiliations></json:item><json:item><name>G.J.M Martens</name><affiliations><json:string>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</json:string></affiliations></json:item><json:item><name>J.A.M Leunissen</name><affiliations><json:string>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</json:string></affiliations></json:item><json:item><name>S.E Wendelaar Bonga</name><affiliations><json:string>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</json:string></affiliations></json:item><json:item><name>G Flik</name><affiliations><json:string>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Proopiomelanocortin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cloning</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Common carp</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mRNA expression</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Sequence analysis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Phylogeny</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), α-melanocyte-stimulating hormone (α-MSH) and β-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and β-MSH domain, two amino acid substitutions are found, whereas α-MSH and β-endorphin are identical. For β-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.</abstract><qualityIndicators><score>7.1</score><pdfVersion>1.2</pdfVersion><pdfPageSize>552 x 768 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>6</keywordCount><abstractCharCount>1105</abstractCharCount><pdfWordCount>5061</pdfWordCount><pdfCharCount>31352</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>175</abstractWordCount></qualityIndicators><title>Cloning and expression of two proopiomelanocortin mRNAs in the common carp ( Cyprinus carpio L.)</title><pii><json:string>S0303-7207(98)00139-7</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>143</volume><pii><json:string>S0303-7207(00)X0058-5</json:string></pii><pages><last>31</last><first>23</first></pages><issn><json:string>0303-7207</json:string></issn><issue>1–2</issue><genre><json:string>journal</json:string></genre><language><json:string>unknown</json:string></language><title>Molecular and Cellular Endocrinology</title><publicationDate>1998</publicationDate></host><categories><wos><json:string>science</json:string><json:string>endocrinology & metabolism</json:string><json:string>cell biology</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>1998</publicationDate><copyrightDate>1998</copyrightDate><doi><json:string>10.1016/S0303-7207(98)00139-7</json:string></doi><id>29245DA3823A5D9BAB4C7241325AA5A42F046044</id><score>0.023452204</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/29245DA3823A5D9BAB4C7241325AA5A42F046044/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/29245DA3823A5D9BAB4C7241325AA5A42F046044/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/29245DA3823A5D9BAB4C7241325AA5A42F046044/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Cloning and expression of two proopiomelanocortin mRNAs in the common carp ( Cyprinus carpio L.)</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>©1998 Elsevier Science Ireland Ltd</p></availability><date>1998</date></publicationStmt><notesStmt><note type="content">Fig. 1: Nucleotide and deduced amino acid sequences of two carp POMC cDNAs. Nucleotides and amino acids are numbered at the end of each lane. The deduced POMC-I amino acid sequence is shown above the cDNA sequence, and the POMC-II amino acid sequence is shown beneath the cDNA sequence. Hyphens indicate identical nucleotides between POMC-I and POMC-II. Gaps (dots) have been introduced to achieve maximum homology. Primers used for PCR are bold and underlined. Target sequence for restriction enzymes PvuII (CAG CTG) and SacI (GAG CTC) are in italics and underlined. Potential proteolytic cleavage sites are boxed. The polyadenylation signal AATAAA is shown in italics and the stop codon is indicated by asterisks (***). Accession numbers from EMBL data base are for POMC-I: Y14618 and for POMC-II: Y14617.</note><note type="content">Fig. 2: Alignment of POMC amino acid sequences from different species. Gaps (dash) have been introduced to achieve maximum homology. Amino acids identical in at least six sequences are colored gray. Differences between the two carp POMC sequences are boxed. Cyprinus carpio POMC-derived peptides, ACTH (151–191), α-MSH (151–164), CLIP (169–191), β-LPH (194–285), β-MSH (233–249) and β-endorphin (252–281). Pairs of basic amino acids where cleavage may occur flank all peptides. Carp signal peptide corresponds to amino acids 9–36, N-terminal peptide from 37–148 (Kawauchi, 1983). All sequences are from SWISS-PROT data base: accession numbers are for trout-A, Q04617; trout-B, Q04618; salmon-II, P10000; xenopus-A, P06298; xenopus-B, P06299; rat, P01194; and human: P01189. The amino acid sequence of salmon-I has been taken from; Kawauchi (1983)and Kitahara et al. (1988). Note: γ-MSH is absent in carp.</note><note type="content">Fig. 3: Northern blot analysis of carp POMC mRNA. Total pituitary RNA (10 μg) was electrophoresed on a 1% denaturated formaldehyde agarose gel, blotted, and the blot was hybridized with 32P-labeled ccPOMC cDNA. The blot was exposed for 24 h at −70°C to an X-ray film. Only one band with an estimated size of ∼1 kb was detected.</note><note type="content">Fig. 4: Digestion patterns of RT-PCR products of ccPOMC-I and ccPOMC-II. RT-PCR products generated with carp POMC primers were digested for 3 h at 37°C. Lane 1 undigested products derived from pituitary mRNA; lane 2, products derived from pituitary mRNA digested with SacI; lane 3, products derived from pituitary mRNA digested with PvuII; lane 4, products derived from pituitary mRNA digested with SacI and PvuII; lane 5, products derived from hypothalamus mRNA digested with SacI and PvuII and lane 6, products derived from mRNA of the rest of the brain digested with SacI and PvuII. cDNAs were fractionated on a 2% agarose gel, and an inverted scan of the gel is shown. Molecular weights of the intact and the digested products are given on the right.</note><note type="content">Fig. 5: Phylogenetic tree of the POMC family. Numbers in branches indicate the bootstrap values calculated with the neighbor-joining method. For details on accession numbers in the SWISS-PROT, TrEMBL or PIR data bases see Section 2.</note><note type="content">Table 1: Nucleotide and amino acid sequence identity between POMC sequences from various species</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Cloning and expression of two proopiomelanocortin mRNAs in the common carp ( Cyprinus carpio L.)</title><author xml:id="author-1"><persName><forename type="first">R.J</forename><surname>Arends</surname></persName><note type="correspondence"><p>Corresponding author. Tel.: +31 80 243652741; fax: +31 80 243652714; e-mail: rarends@sci.kun.nl</p></note><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation></author><author xml:id="author-2"><persName><forename type="first">H</forename><surname>Vermeer</surname></persName><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation></author><author xml:id="author-3"><persName><forename type="first">G.J.M</forename><surname>Martens</surname></persName><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation></author><author xml:id="author-4"><persName><forename type="first">J.A.M</forename><surname>Leunissen</surname></persName><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation></author><author xml:id="author-5"><persName><forename type="first">S.E</forename><surname>Wendelaar Bonga</surname></persName><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation></author><author xml:id="author-6"><persName><forename type="first">G</forename><surname>Flik</surname></persName><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation></author></analytic><monogr><title level="j">Molecular and Cellular Endocrinology</title><title level="j" type="abbrev">MCE</title><idno type="pISSN">0303-7207</idno><idno type="PII">S0303-7207(00)X0058-5</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">143</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="23">23</biblScope><biblScope unit="page" to="31">31</biblScope></imprint></monogr><idno type="istex">29245DA3823A5D9BAB4C7241325AA5A42F046044</idno><idno type="DOI">10.1016/S0303-7207(98)00139-7</idno><idno type="PII">S0303-7207(98)00139-7</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), α-melanocyte-stimulating hormone (α-MSH) and β-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and β-MSH domain, two amino acid substitutions are found, whereas α-MSH and β-endorphin are identical. For β-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Proopiomelanocortin</term></item><item><term>Cloning</term></item><item><term>Common carp</term></item><item><term>mRNA expression</term></item><item><term>Sequence analysis</term></item><item><term>Phylogeny</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/29245DA3823A5D9BAB4C7241325AA5A42F046044/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:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>MCE</jid><aid>4376</aid><ce:pii>S0303-7207(98)00139-7</ce:pii><ce:doi>10.1016/S0303-7207(98)00139-7</ce:doi><ce:copyright year="1998" type="full-transfer">Elsevier Science Ireland Ltd</ce:copyright></item-info><head><ce:title>Cloning and expression of two proopiomelanocortin mRNAs in the common carp (<ce:italic>Cyprinus carpio</ce:italic> L.)</ce:title><ce:author-group><ce:author><ce:given-name>R.J</ce:given-name><ce:surname>Arends</ce:surname><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:author><ce:given-name>H</ce:given-name><ce:surname>Vermeer</ce:surname></ce:author><ce:author><ce:given-name>G.J.M</ce:given-name><ce:surname>Martens</ce:surname></ce:author><ce:author><ce:given-name>J.A.M</ce:given-name><ce:surname>Leunissen</ce:surname></ce:author><ce:author><ce:given-name>S.E</ce:given-name><ce:surname>Wendelaar Bonga</ce:surname></ce:author><ce:author><ce:given-name>G</ce:given-name><ce:surname>Flik</ce:surname></ce:author><ce:affiliation><ce:textfn>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Tel.: +31 80 243652741; fax: +31 80 243652714; e-mail: rarends@sci.kun.nl</ce:text></ce:correspondence></ce:author-group><ce:date-received day="11" month="5" year="1998"></ce:date-received><ce:date-accepted day="3" month="7" year="1998"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), <ce:italic>α</ce:italic>-melanocyte-stimulating hormone (<ce:italic>α</ce:italic>-MSH) and <ce:italic>β</ce:italic>-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and <ce:italic>β</ce:italic>-MSH domain, two amino acid substitutions are found, whereas <ce:italic>α</ce:italic>-MSH and <ce:italic>β</ce:italic>-endorphin are identical. For <ce:italic>β</ce:italic>-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Proopiomelanocortin</ce:text></ce:keyword><ce:keyword><ce:text>Cloning</ce:text></ce:keyword><ce:keyword><ce:text>Common carp</ce:text></ce:keyword><ce:keyword><ce:text>mRNA expression</ce:text></ce:keyword><ce:keyword><ce:text>Sequence analysis</ce:text></ce:keyword><ce:keyword><ce:text>Phylogeny</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Cloning and expression of two proopiomelanocortin mRNAs in the common carp ( Cyprinus carpio L.)</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Cloning and expression of two proopiomelanocortin mRNAs in the common carp (</title></titleInfo><name type="personal"><namePart type="given">R.J</namePart><namePart type="family">Arends</namePart><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation><description>Corresponding author. Tel.: +31 80 243652741; fax: +31 80 243652714; e-mail: rarends@sci.kun.nl</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H</namePart><namePart type="family">Vermeer</namePart><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.J.M</namePart><namePart type="family">Martens</namePart><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.A.M</namePart><namePart type="family">Leunissen</namePart><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.E</namePart><namePart type="family">Wendelaar Bonga</namePart><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G</namePart><namePart type="family">Flik</namePart><affiliation>Department of Animal Physiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands</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">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</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">Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), α-melanocyte-stimulating hormone (α-MSH) and β-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and β-MSH domain, two amino acid substitutions are found, whereas α-MSH and β-endorphin are identical. For β-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.</abstract><note type="content">Fig. 1: Nucleotide and deduced amino acid sequences of two carp POMC cDNAs. Nucleotides and amino acids are numbered at the end of each lane. The deduced POMC-I amino acid sequence is shown above the cDNA sequence, and the POMC-II amino acid sequence is shown beneath the cDNA sequence. Hyphens indicate identical nucleotides between POMC-I and POMC-II. Gaps (dots) have been introduced to achieve maximum homology. Primers used for PCR are bold and underlined. Target sequence for restriction enzymes PvuII (CAG CTG) and SacI (GAG CTC) are in italics and underlined. Potential proteolytic cleavage sites are boxed. The polyadenylation signal AATAAA is shown in italics and the stop codon is indicated by asterisks (***). Accession numbers from EMBL data base are for POMC-I: Y14618 and for POMC-II: Y14617.</note><note type="content">Fig. 2: Alignment of POMC amino acid sequences from different species. Gaps (dash) have been introduced to achieve maximum homology. Amino acids identical in at least six sequences are colored gray. Differences between the two carp POMC sequences are boxed. Cyprinus carpio POMC-derived peptides, ACTH (151–191), α-MSH (151–164), CLIP (169–191), β-LPH (194–285), β-MSH (233–249) and β-endorphin (252–281). Pairs of basic amino acids where cleavage may occur flank all peptides. Carp signal peptide corresponds to amino acids 9–36, N-terminal peptide from 37–148 (Kawauchi, 1983). All sequences are from SWISS-PROT data base: accession numbers are for trout-A, Q04617; trout-B, Q04618; salmon-II, P10000; xenopus-A, P06298; xenopus-B, P06299; rat, P01194; and human: P01189. The amino acid sequence of salmon-I has been taken from; Kawauchi (1983)and Kitahara et al. (1988). Note: γ-MSH is absent in carp.</note><note type="content">Fig. 3: Northern blot analysis of carp POMC mRNA. Total pituitary RNA (10 μg) was electrophoresed on a 1% denaturated formaldehyde agarose gel, blotted, and the blot was hybridized with 32P-labeled ccPOMC cDNA. The blot was exposed for 24 h at −70°C to an X-ray film. Only one band with an estimated size of ∼1 kb was detected.</note><note type="content">Fig. 4: Digestion patterns of RT-PCR products of ccPOMC-I and ccPOMC-II. RT-PCR products generated with carp POMC primers were digested for 3 h at 37°C. Lane 1 undigested products derived from pituitary mRNA; lane 2, products derived from pituitary mRNA digested with SacI; lane 3, products derived from pituitary mRNA digested with PvuII; lane 4, products derived from pituitary mRNA digested with SacI and PvuII; lane 5, products derived from hypothalamus mRNA digested with SacI and PvuII and lane 6, products derived from mRNA of the rest of the brain digested with SacI and PvuII. cDNAs were fractionated on a 2% agarose gel, and an inverted scan of the gel is shown. Molecular weights of the intact and the digested products are given on the right.</note><note type="content">Fig. 5: Phylogenetic tree of the POMC family. Numbers in branches indicate the bootstrap values calculated with the neighbor-joining method. For details on accession numbers in the SWISS-PROT, TrEMBL or PIR data bases see Section 2.</note><note type="content">Table 1: Nucleotide and amino acid sequence identity between POMC sequences from various species</note><subject lang="en"><genre>Keywords</genre><topic>Proopiomelanocortin</topic><topic>Cloning</topic><topic>Common carp</topic><topic>mRNA expression</topic><topic>Sequence analysis</topic><topic>Phylogeny</topic></subject><relatedItem type="host"><titleInfo><title>Molecular and Cellular Endocrinology</title></titleInfo><titleInfo type="abbreviated"><title>MCE</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19980825</dateIssued></originInfo><identifier type="ISSN">0303-7207</identifier><identifier type="PII">S0303-7207(00)X0058-5</identifier><part><date>19980825</date><detail type="volume"><number>143</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>182</end></extent><extent unit="pages"><start>23</start><end>31</end></extent></part></relatedItem><identifier type="istex">29245DA3823A5D9BAB4C7241325AA5A42F046044</identifier><identifier type="DOI">10.1016/S0303-7207(98)00139-7</identifier><identifier type="PII">S0303-7207(98)00139-7</identifier><accessCondition type="use and reproduction" contentType="copyright">©1998 Elsevier Science Ireland Ltd</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Elsevier Science Ireland Ltd, ©1998</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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