Isolation, analysis of structure, synthesis, and biological actions of urotensin I neuropeptides.
Isolation, analysis of structure, synthesis, and biological actions of urotensin I neuropeptides.
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尾加压素 I 神经肽的分离、结构分析、合成和生物学作用。
DOI:
10.1139/o83-076
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发表时间:
1983
期刊:
影响因子:
--
通讯作者:
Fryer,J
中科院分区:
文献类型:
--
作者:
Lederis,K;Letter,A;McMaster,D;Ichikawa,T;MacCannell,KL;Kobayashi,Y;Rivier,J;Rivier,C;Vale,W;Fryer,J
The 41-residue neuropeptide urotensin I (UI), from the urophyses of two teleost fish species (Cyprinus carpioandCatostomus commersoni), was isolated and purified, and its amino acid sequence was determined and confirmed by synthesis of a fully active peptide. The UI peptide was found to be a close structural and biological homologue of the ovine hypothalamic corticotropin-releasing factor (CRF) and the frog skin peptide sauvagine; UI is, therefore, a phylogenetic prototype of this group of peptides. Extraction of urophyses in hot acetic or hydrochloric acid cleaves an amino terminal tripeptide yielding a fully active UI(4–41). The UI peptides are equipotent with the other two naturally occurring peptides (CRF and sauvagine) in the release of mammalian pituitary corticotropin (ACTH), but UI is several times more potent than the mammalian homologue in the stimulation of release of fish pituitary ACTH. The UI peptide and its mammalian or amphibian homologues have a long-lasting hypotensive action in mammals, via a uniquely selective vasodilatation in the superior (anterior) mesenteric vascular bed only. The significantly lower hypotensive vasodilatory action of the mammalian homologue (CRF) suggests a change in the unknown physiological role of the haemodynamic actions of the UI peptides in the mammalian gastrointestinal tract during phylogenetic progression from fishes to mammals.