Recent structure-activity studies of the peptide hormone urotensin-II, a potent vasoconstrictor.
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.
Grieco
P
P
Department of Pharmaceutical and Toxicological Chemistry, University of Naples Federico II, I-80131 Naples, Italy. pagrieco@unina.it
Rovero
P
P
Novellino
E
E
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D013329:Structure-Activity Relationship; D014579:Urotensins / Q000378:metabolism / Q000494:pharmacology*; D014662:Vasoconstrictor Agents / Q000378:metabolism / Q000494:pharmacology*
D014579:Urotensins; D014662:Vasoconstrictor Agents; C029677:urotensin II