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Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Recent Structure-Activity Studies of the Peptide Hormone Urotensin-II, a Potent Vasoconstrictor

Author(s): P. Grieco, P. Rovero and E. Novellino

Volume 11 , Issue 8 , 2004

Page: [969 - 979] Pages: 11

DOI: 10.2174/0929867043455495

Price: $65

Abstract

Human Urotensin-II is a potent vasoconstrictor and binds with high affinity to GPR14 receptor, recently cloned and renamed UT receptor. U-II vasoconstrictive potency is reported to be an order of magnitude greater than that of endothelin-1 (ET-1), which would make it the most potent mammalian vasoconstrictor identified to date. Urotensin-II is a neuropeptide “somatostatin-like” cyclic peptide, which was originally isolated from fish spinal cords, and which has recently been cloned from human. Human U-II is composed of only 11 amino acids residues, while fish and frog U-II possess 12 and 13 amino acids residues, respectively. The cyclic region of U-II, which is responsible for the biological activity of the peptide, has been fully conserved from fish to human. This review focuses on recent structure-activity relationships studies performed on Urotensin-II with the aim to provide the required structural elements to design new ligands as agonists and antagonists for UT receptor.

Keywords: urotensin-II, sars studies, nmr studies, ligands


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