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Complete Amino Acid Sequence of Urotensin I, a Hypotensive and Corticotropin-Releasing Neuropeptide from Catostomus

Lederis, K., Letter, A., McMaster, D., Moore, G., Schlesinger, D.·1982·Science

Abstract

Urotensin I, purified from extracts of the urophysis of a teleost fish ( Catostomus commersoni ), exhibits potent hypotensive activity (mammals and birds) and corticotropin-releasing activity (both fish and mammals). The primary structure of this 41-residue peptide was determined to be 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-Asp-Glu-Val-NH2. Extraction with 0.1 N HCl at 100°C cleaves the amino-terminal tripeptide, yielding a fully active analog, urotensin I(4-41). The amino acid sequence was confirmed by measuring the biological activity of synthetic urotensin I(4-41). Urotensin I exhibits a striking sequence homology with ovine corticotropin-releasing factor and with frog sauvagine. These three peptides exhibit similar activities in biological test systems.

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Metadata

Authors
Lederis, K., Letter, A., McMaster, D., Moore, G., & Schlesinger, D.
Venue
Science
Published
1982-10-08
Volume
218
Issue
4568
Pages
162-165
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2052530157
Cited by
286
References
0
FWCI
5.60
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Complete Amino Acid Sequence of Urotensin I, a Hypotensive and Corticotropin-Releasing Neuropeptide from Catostomus. https://app.cochat.ai/papers/10.1126/science.6981844
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Lederis, K., Letter, A., McMaster, D., Moore, G., & Schlesinger, D. (1982). Complete Amino Acid Sequence of Urotensin I, a Hypotensive and Corticotropin-Releasing Neuropeptide from Catostomus. Science. https://doi.org/10.1126/science.6981844

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