Urotensin II from the river lamprey (Lampetra fluviatilis), the sea lamprey (Petromyzon marinus), and the paddlefish (Polyodon spathula).
Identifieur interne : 000869 ( Ncbi/Checkpoint ); précédent : 000868; suivant : 000870Urotensin II from the river lamprey (Lampetra fluviatilis), the sea lamprey (Petromyzon marinus), and the paddlefish (Polyodon spathula).
Auteurs : D. Waugh [États-Unis] ; J. Youson ; S D Mims ; S. Sower ; J M ConlonSource :
- General and comparative endocrinology [ 0016-6480 ] ; 1995.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Urotensins.
- chemical , isolation & purification : Urotensins.
- metabolism : Fishes, Lampreys.
- Amino Acid Sequence, Animals, Biological Evolution, Female, Male, Molecular Sequence Data, Species Specificity.
Abstract
Urotensin II was isolated from extracts of the whole brain of the river lamprey (Lampetra fluviatilis) and the sea lamprey (Petromyzon marinus). The primary structure of the peptide from both species is the same (Asn-Asn-Phe-Ser-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val) and this amino acid sequence is identical to that of urotensin II from the dogfish and skate. Consistent with previous morphological studies indicating that the Agnatha lack a caudal neurosecretory system, urotensin II was not detected in an extract of P. marinus spinal cord. The data suggest that the urotensin II may have functioned in the earliest vertebrates as a neurotransmitter/neuromodulator in the central nervous system rather than as a neurohormone of the caudal neurosecretory system. Urotensin II was also isolated from an extract of the spinal cord of a chondrostean fish, the paddlefish (Polyodon spathula). The primary structure of the paddlefish urotensin II (Gly-Ser-Thr-Ser-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val) is the same as that of another chondrostean, the sturgeon (Acipenser ruthenus). The study provides further evidence for a widespread distribution of urotensin II in vertebrate species and suggests that the primary structure of the peptide is better conserved in these phylogenetically ancient fish than in teleosts.
DOI: 10.1006/gcen.1995.1116
PubMed: 8536944
Affiliations:
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pubmed:8536944Le document en format XML
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<author><name sortKey="Waugh, D" sort="Waugh, D" uniqKey="Waugh D" first="D" last="Waugh">D. Waugh</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska 68178, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska 68178</wicri:regionArea>
<wicri:noRegion>Nebraska 68178</wicri:noRegion>
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<author><name sortKey="Youson, J" sort="Youson, J" uniqKey="Youson J" first="J" last="Youson">J. Youson</name>
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<author><name sortKey="Mims, S D" sort="Mims, S D" uniqKey="Mims S" first="S D" last="Mims">S D Mims</name>
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<author><name sortKey="Sower, S" sort="Sower, S" uniqKey="Sower S" first="S" last="Sower">S. Sower</name>
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<author><name sortKey="Conlon, J M" sort="Conlon, J M" uniqKey="Conlon J" first="J M" last="Conlon">J M Conlon</name>
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<affiliation wicri:level="1"><nlm:affiliation>Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska 68178, USA.</nlm:affiliation>
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<series><title level="j">General and comparative endocrinology</title>
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<term>Animals</term>
<term>Biological Evolution</term>
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<term>Fishes (metabolism)</term>
<term>Lampreys (metabolism)</term>
<term>Male</term>
<term>Molecular Sequence Data</term>
<term>Species Specificity</term>
<term>Urotensins (chemistry)</term>
<term>Urotensins (isolation & purification)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Urotensins</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term>
<term>Lampreys</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Biological Evolution</term>
<term>Female</term>
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<term>Molecular Sequence Data</term>
<term>Species Specificity</term>
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<front><div type="abstract" xml:lang="en">Urotensin II was isolated from extracts of the whole brain of the river lamprey (Lampetra fluviatilis) and the sea lamprey (Petromyzon marinus). The primary structure of the peptide from both species is the same (Asn-Asn-Phe-Ser-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val) and this amino acid sequence is identical to that of urotensin II from the dogfish and skate. Consistent with previous morphological studies indicating that the Agnatha lack a caudal neurosecretory system, urotensin II was not detected in an extract of P. marinus spinal cord. The data suggest that the urotensin II may have functioned in the earliest vertebrates as a neurotransmitter/neuromodulator in the central nervous system rather than as a neurohormone of the caudal neurosecretory system. Urotensin II was also isolated from an extract of the spinal cord of a chondrostean fish, the paddlefish (Polyodon spathula). The primary structure of the paddlefish urotensin II (Gly-Ser-Thr-Ser-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val) is the same as that of another chondrostean, the sturgeon (Acipenser ruthenus). The study provides further evidence for a widespread distribution of urotensin II in vertebrate species and suggests that the primary structure of the peptide is better conserved in these phylogenetically ancient fish than in teleosts.</div>
</front>
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<name sortKey="Sower, S" sort="Sower, S" uniqKey="Sower S" first="S" last="Sower">S. Sower</name>
<name sortKey="Youson, J" sort="Youson, J" uniqKey="Youson J" first="J" last="Youson">J. Youson</name>
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<country name="États-Unis"><noRegion><name sortKey="Waugh, D" sort="Waugh, D" uniqKey="Waugh D" first="D" last="Waugh">D. Waugh</name>
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