Urotensin I, made pure from distils by the urophysis of a teleostan (genus Catostomus commersoni), demonstrates powerful hypotensive bodily function (mammals and birdies) and corticotropin-releasing activeness (some fish and mammals). The common body structure of these 41-residue peptide constituted checked to constitute H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Asn-Met- Ile-Glu- Met-Ala-Arg-Ile-Glu-Asn-Glu-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-As p-Glu -Val-NH2. Descent with incognizant.1N HCl at C arcdegrees blow adheres the amino-terminal tripeptide, yeilding a full alive analog, urotensin I(4-41). The aminoalkanoic acid chronological sequence constituted corroborated away evaluating the biologic bodily function of man-made urotensin I(4-41). Urotensin I demonstrates a attaining episode homology with ovine corticotropin-releasing component and with batrachian sauvagine. These leash peptides display exchangeable actions inward biologic examination organisations.
Intraperitoneal injections of urotensin I, a CRF-like neuropeptide isolated from the caudal neurosecretory system of the teleost Catostomus commersoni, ovine CRF and sauvagine all produced significant increases in circulating levels of plasma cortisol in goldfish in which endogenous ACTH secretion was suppressed with betamethasone. CRH and urotensin I (UI) are neuroendocrine peptides that belong to the superfamily of corticotropin-releasing factors. In mammals, these peptides regulate the stress response and other central nervous system functions, whereas in fish an involvement for UI in osmoregulation has also been suggested. We have identified, characterized, and localized the genes encoding these peptides in a unique fish neuroendocrine organ, the caudal neurosecretory system (CNSS). The CRH and UI precursors, isolated from a European flounder CNSS library, consist of 168 and 147 amino acid residues, respectively, with an overall homology of approximately 50%. Both precursors contain a signal peptide, a divergent cryptic region and a 41-amino acid mature peptide with cleavage and amidation sites. Genomic organization showed that whole CRH and UI coding sequences are contained in a single exon. Northern blot analysis and quantitative PCR of a range of tissues confirmed the CNSS as a major site of expression of both CRH and UI and thus serves as a likely source of circulating peptides. In situ hybridization demonstrated that CRH and UI colocalize to the same cells of the CNSS. Our findings suggest that, in euryhaline fish, the CNSS is a major site of production of CRH and probably contributes to the high circulating levels observed in response to specific environmental challenges. Furthermore, the localization of CRH and UI within the same cell population suggests an early, possibly shared role for these peptides in controlling stress-mediated adaptive plasticity.In vitro, urotensin I was 2–3 times more potent than CRF or sauvagine in stimulating ACTH release from a superfused goldfish anterior pituitary cell column. These results demonstrate that urotensin I stimulates ACTH release in the goldfish, which suggests that urotensin I or a urotensin I-like peptide may serve as a CRF in teleost fishes.
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Intraperitoneal injections of urotensin I, a CRF-like neuropeptide isolated from the caudal neurosecretory system of the teleost Catostomus commersoni, ovine CRF and sauvagine all produced significant increases in circulating levels of plasma cortisol in goldfish in which endogenous ACTH secretion was suppressed with betamethasone. CRH and urotensin I (UI) are neuroendocrine peptides that belong to the superfamily of corticotropin-releasing factors. In mammals, these peptides regulate the stress response and other central nervous system functions, whereas in fish an involvement for UI in osmoregulation has also been suggested. We have identified, characterized, and localized the genes encoding these peptides in a unique fish neuroendocrine organ, the caudal neurosecretory system (CNSS). The CRH and UI precursors, isolated from a European flounder CNSS library, consist of 168 and 147 amino acid residues, respectively, with an overall homology of approximately 50%. Both precursors contain a signal peptide, a divergent cryptic region and a 41-amino acid mature peptide with cleavage and amidation sites. Genomic organization showed that whole CRH and UI coding sequences are contained in a single exon. Northern blot analysis and quantitative PCR of a range of tissues confirmed the CNSS as a major site of expression of both CRH and UI and thus serves as a likely source of circulating peptides. In situ hybridization demonstrated that CRH and UI colocalize to the same cells of the CNSS. Our findings suggest that, in euryhaline fish, the CNSS is a major site of production of CRH and probably contributes to the high circulating levels observed in response to specific environmental challenges. Furthermore, the localization of CRH and UI within the same cell population suggests an early, possibly shared role for these peptides in controlling stress-mediated adaptive plasticity.In vitro, urotensin I was 2–3 times more potent than CRF or sauvagine in stimulating ACTH release from a superfused goldfish anterior pituitary cell column. These results demonstrate that urotensin I stimulates ACTH release in the goldfish, which suggests that urotensin I or a urotensin I-like peptide may serve as a CRF in teleost fishes.
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