Isolation and amino acid sequence of urotensin II from the sturgeon Acipenser ruthenus.
Identifieur interne : 001D50 ( Main/Merge ); précédent : 001D49; suivant : 001D51Isolation and amino acid sequence of urotensin II from the sturgeon Acipenser ruthenus.
Auteurs : D. Mcmaster [Canada] ; M A Belenky ; A L Polenov ; K. LederisSource :
- General and comparative endocrinology [ 0016-6480 ] ; 1992.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Urotensins.
- chemical , isolation & purification : Urotensins.
- metabolism : Spinal Cord.
- Amino Acid Sequence, Animals, Chromatography, High Pressure Liquid, Fishes, Molecular Sequence Data, Radioimmunoassay, Sequence Homology.
Abstract
Urotensin II (UII) peptides have previously been isolated from the urophysis (the neurohemal organ of the caudal neurosecretory system) of several teleost fish, and the UII amino acid sequences have been determined. Chondrostean fish, such as the Acipenseridae (sturgeon), though without a distinct urophysis, also have a caudal neurosecretory system, which has been indicated by bioassay and immunological evidence to contain UII-like peptides. In the present studies, we investigated by UII radioimmunoassay the UII-like peptides in the spinal cord of three Acipenser species, and isolated and sequenced UII from one of them. As expected, much more UII immunoreactivity (UII-IR) was found in caudal than in anterior spinal cord extracts. In addition, caudal extracts from A. ruthenus were found to contain much more UII-IR (whether determined on a UII-IR/weight or UII-IR/fish basis) than those from the larger A. stellatus and A. guldenstadti. UII was therefore isolated from A. ruthenus and its amino acid sequence was shown to be H-Gly-Ser-Thr-Ser-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH. This sequence is identical at positions 6-11 (the disulfide ring) with the known teleost UII peptides, and has acidic and hydrophobic amino acids at positions 5 and 12, respectively, as do the teleost UII peptides. Overall sequence identity with the various forms of teleost UII was 58-83%.
PubMed: 1398021
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Mcmaster</name><affiliation wicri:level="4"><nlm:affiliation>Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta</wicri:regionArea><orgName type="university">Université de Calgary</orgName><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Belenky, M A" sort="Belenky, M A" uniqKey="Belenky M" first="M A" last="Belenky">M A Belenky</name></author><author><name sortKey="Polenov, A L" sort="Polenov, A L" uniqKey="Polenov A" first="A L" last="Polenov">A L Polenov</name></author><author><name sortKey="Lederis, K" sort="Lederis, K" uniqKey="Lederis K" first="K" last="Lederis">K. 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Mcmaster</name><affiliation wicri:level="4"><nlm:affiliation>Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta</wicri:regionArea><orgName type="university">Université de Calgary</orgName><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Belenky, M A" sort="Belenky, M A" uniqKey="Belenky M" first="M A" last="Belenky">M A Belenky</name></author><author><name sortKey="Polenov, A L" sort="Polenov, A L" uniqKey="Polenov A" first="A L" last="Polenov">A L Polenov</name></author><author><name sortKey="Lederis, K" sort="Lederis, K" uniqKey="Lederis K" first="K" last="Lederis">K. Lederis</name></author></analytic><series><title level="j">General and comparative endocrinology</title><idno type="ISSN">0016-6480</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chromatography, High Pressure Liquid</term><term>Fishes</term><term>Molecular Sequence Data</term><term>Radioimmunoassay</term><term>Sequence Homology</term><term>Spinal Cord (metabolism)</term><term>Urotensins (chemistry)</term><term>Urotensins (isolation & purification)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Urotensins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Urotensins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Spinal Cord</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chromatography, High Pressure Liquid</term><term>Fishes</term><term>Molecular Sequence Data</term><term>Radioimmunoassay</term><term>Sequence Homology</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Urotensin II (UII) peptides have previously been isolated from the urophysis (the neurohemal organ of the caudal neurosecretory system) of several teleost fish, and the UII amino acid sequences have been determined. Chondrostean fish, such as the Acipenseridae (sturgeon), though without a distinct urophysis, also have a caudal neurosecretory system, which has been indicated by bioassay and immunological evidence to contain UII-like peptides. In the present studies, we investigated by UII radioimmunoassay the UII-like peptides in the spinal cord of three Acipenser species, and isolated and sequenced UII from one of them. As expected, much more UII immunoreactivity (UII-IR) was found in caudal than in anterior spinal cord extracts. In addition, caudal extracts from A. ruthenus were found to contain much more UII-IR (whether determined on a UII-IR/weight or UII-IR/fish basis) than those from the larger A. stellatus and A. guldenstadti. UII was therefore isolated from A. ruthenus and its amino acid sequence was shown to be H-Gly-Ser-Thr-Ser-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH. This sequence is identical at positions 6-11 (the disulfide ring) with the known teleost UII peptides, and has acidic and hydrophobic amino acids at positions 5 and 12, respectively, as do the teleost UII peptides. Overall sequence identity with the various forms of teleost UII was 58-83%.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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