Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.
Identifieur interne : 000853 ( Ncbi/Merge ); précédent : 000852; suivant : 000854Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.
Auteurs : H. Keller [États-Unis] ; J M Redding ; G. Moberg ; R M DoresSource :
- General and comparative endocrinology [ 0016-6480 ] ; 1994.
English descriptors
- KwdEn :
- Acetylation, Animals, Biological Evolution, Chromatography, High Pressure Liquid, Fishes (metabolism), Male, Peptide Fragments (analysis), Peptide Fragments (isolation & purification), Peptide Fragments (metabolism), Pituitary Gland (metabolism), Protein Processing, Post-Translational (physiology), Radioimmunoassay, Species Specificity, alpha-MSH (analogs & derivatives), alpha-MSH (immunology), alpha-MSH (metabolism).
- MESH :
- chemical , analogs & derivatives : alpha-MSH.
- chemical , analysis : Peptide Fragments.
- chemical , immunology : alpha-MSH.
- chemical , isolation & purification : Peptide Fragments.
- metabolism : Fishes, Peptide Fragments, Pituitary Gland, alpha-MSH.
- physiology : Protein Processing, Post-Translational.
- Acetylation, Animals, Biological Evolution, Chromatography, High Pressure Liquid, Male, Radioimmunoassay, Species Specificity.
Abstract
Multiple forms of alpha-MSH were isolated from the pituitaries of the white sturgeon, Acipenser transmontanus, and the paddlefish, Polyodon spathula, following fractionation of the pituitary extracts by reversed-phase HPLC. In both species, immunoreactive forms which eluted with the same retention times as synthetic mammalian ACTH(1-13)NH2, monoacetylated alpha-MSH, and diacetylated alpha-MSH were detected. In the pituitary of the sturgeon, N-acetylated forms of alpha-MSH represented 91% of the total alpha-MSH isolated. However, in the pituitary of the paddlefish, N-acetylated forms of alpha-MSH accounted for only 45% of the total alpha-MSH isolated. The presence of N-acetylated forms of alpha-MSH in the pituitaries of representatives of the two extant genera of chondrostean fish coupled with the observation that N-acetylated forms of alpha-MSH are present in the pituitaries of cladistian and neopterygian fishes indicates that the alpha-MSH specific N-acetylation mechanism evolved prior to the radiation of the Actinopterygii. A conspicuous feature of the chondrostean alpha-MSH N-acetylation reaction was the low levels of diacetylated alpha-MSH produced relative to the levels of monoacetylated alpha-MSH. Similar observations have been made for the cladistian fish, Calamoichthys calabaricus, and the cartilaginous fish, Hydrolagus colliei. However, in holostean fishes, lungfishes, and tetrapods, the diacetylated form of alpha-MSH is the major end product produced in the intermediate pituitary. The phylogenetic implications of these observations will be discussed.
DOI: 10.1006/gcen.1994.1071
PubMed: 7926625
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.</title><author><name sortKey="Keller, H" sort="Keller, H" uniqKey="Keller H" first="H" last="Keller">H. Keller</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, University of Denver, Colorado 80208.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Colorado</region></placeName><wicri:cityArea>Department of Biological Sciences, University of Denver</wicri:cityArea></affiliation></author><author><name sortKey="Redding, J M" sort="Redding, J M" uniqKey="Redding J" first="J M" last="Redding">J M Redding</name></author><author><name sortKey="Moberg, G" sort="Moberg, G" uniqKey="Moberg G" first="G" last="Moberg">G. Moberg</name></author><author><name sortKey="Dores, R M" sort="Dores, R M" uniqKey="Dores R" first="R M" last="Dores">R M Dores</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:7926625</idno><idno type="pmid">7926625</idno><idno type="doi">10.1006/gcen.1994.1071</idno><idno type="wicri:Area/PubMed/Corpus">000708</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000708</idno><idno type="wicri:Area/PubMed/Curation">000708</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000708</idno><idno type="wicri:Area/PubMed/Checkpoint">000708</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000708</idno><idno type="wicri:Area/Ncbi/Merge">000853</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.</title><author><name sortKey="Keller, H" sort="Keller, H" uniqKey="Keller H" first="H" last="Keller">H. Keller</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, University of Denver, Colorado 80208.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Colorado</region></placeName><wicri:cityArea>Department of Biological Sciences, University of Denver</wicri:cityArea></affiliation></author><author><name sortKey="Redding, J M" sort="Redding, J M" uniqKey="Redding J" first="J M" last="Redding">J M Redding</name></author><author><name sortKey="Moberg, G" sort="Moberg, G" uniqKey="Moberg G" first="G" last="Moberg">G. Moberg</name></author><author><name sortKey="Dores, R M" sort="Dores, R M" uniqKey="Dores R" first="R M" last="Dores">R M Dores</name></author></analytic><series><title level="j">General and comparative endocrinology</title><idno type="ISSN">0016-6480</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylation</term><term>Animals</term><term>Biological Evolution</term><term>Chromatography, High Pressure Liquid</term><term>Fishes (metabolism)</term><term>Male</term><term>Peptide Fragments (analysis)</term><term>Peptide Fragments (isolation & purification)</term><term>Peptide Fragments (metabolism)</term><term>Pituitary Gland (metabolism)</term><term>Protein Processing, Post-Translational (physiology)</term><term>Radioimmunoassay</term><term>Species Specificity</term><term>alpha-MSH (analogs & derivatives)</term><term>alpha-MSH (immunology)</term><term>alpha-MSH (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>alpha-MSH</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>alpha-MSH</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term><term>Peptide Fragments</term><term>Pituitary Gland</term><term>alpha-MSH</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Acetylation</term><term>Animals</term><term>Biological Evolution</term><term>Chromatography, High Pressure Liquid</term><term>Male</term><term>Radioimmunoassay</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Multiple forms of alpha-MSH were isolated from the pituitaries of the white sturgeon, Acipenser transmontanus, and the paddlefish, Polyodon spathula, following fractionation of the pituitary extracts by reversed-phase HPLC. In both species, immunoreactive forms which eluted with the same retention times as synthetic mammalian ACTH(1-13)NH2, monoacetylated alpha-MSH, and diacetylated alpha-MSH were detected. In the pituitary of the sturgeon, N-acetylated forms of alpha-MSH represented 91% of the total alpha-MSH isolated. However, in the pituitary of the paddlefish, N-acetylated forms of alpha-MSH accounted for only 45% of the total alpha-MSH isolated. The presence of N-acetylated forms of alpha-MSH in the pituitaries of representatives of the two extant genera of chondrostean fish coupled with the observation that N-acetylated forms of alpha-MSH are present in the pituitaries of cladistian and neopterygian fishes indicates that the alpha-MSH specific N-acetylation mechanism evolved prior to the radiation of the Actinopterygii. A conspicuous feature of the chondrostean alpha-MSH N-acetylation reaction was the low levels of diacetylated alpha-MSH produced relative to the levels of monoacetylated alpha-MSH. Similar observations have been made for the cladistian fish, Calamoichthys calabaricus, and the cartilaginous fish, Hydrolagus colliei. However, in holostean fishes, lungfishes, and tetrapods, the diacetylated form of alpha-MSH is the major end product produced in the intermediate pituitary. The phylogenetic implications of these observations will be discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7926625</PMID><DateCreated><Year>1994</Year><Month>10</Month><Day>28</Day></DateCreated><DateCompleted><Year>1994</Year><Month>10</Month><Day>28</Day></DateCompleted><DateRevised><Year>2010</Year><Month>11</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0016-6480</ISSN><JournalIssue CitedMedium="Print"><Volume>94</Volume><Issue>2</Issue><PubDate><Year>1994</Year><Month>May</Month></PubDate></JournalIssue><Title>General and comparative endocrinology</Title><ISOAbbreviation>Gen. Comp. Endocrinol.</ISOAbbreviation></Journal><ArticleTitle>Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.</ArticleTitle><Pagination><MedlinePgn>159-65</MedlinePgn></Pagination><Abstract><AbstractText>Multiple forms of alpha-MSH were isolated from the pituitaries of the white sturgeon, Acipenser transmontanus, and the paddlefish, Polyodon spathula, following fractionation of the pituitary extracts by reversed-phase HPLC. In both species, immunoreactive forms which eluted with the same retention times as synthetic mammalian ACTH(1-13)NH2, monoacetylated alpha-MSH, and diacetylated alpha-MSH were detected. In the pituitary of the sturgeon, N-acetylated forms of alpha-MSH represented 91% of the total alpha-MSH isolated. However, in the pituitary of the paddlefish, N-acetylated forms of alpha-MSH accounted for only 45% of the total alpha-MSH isolated. The presence of N-acetylated forms of alpha-MSH in the pituitaries of representatives of the two extant genera of chondrostean fish coupled with the observation that N-acetylated forms of alpha-MSH are present in the pituitaries of cladistian and neopterygian fishes indicates that the alpha-MSH specific N-acetylation mechanism evolved prior to the radiation of the Actinopterygii. A conspicuous feature of the chondrostean alpha-MSH N-acetylation reaction was the low levels of diacetylated alpha-MSH produced relative to the levels of monoacetylated alpha-MSH. Similar observations have been made for the cladistian fish, Calamoichthys calabaricus, and the cartilaginous fish, Hydrolagus colliei. However, in holostean fishes, lungfishes, and tetrapods, the diacetylated form of alpha-MSH is the major end product produced in the intermediate pituitary. 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Moberg</name><name sortKey="Redding, J M" sort="Redding, J M" uniqKey="Redding J" first="J M" last="Redding">J M Redding</name></noCountry><country name="États-Unis"><region name="Colorado"><name sortKey="Keller, H" sort="Keller, H" uniqKey="Keller H" first="H" last="Keller">H. Keller</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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