Grieco P, Rovero P, Novellino E
Department of Pharmaceutical and Toxicological Chemistry, University of Naples Federico II, I-80131 Naples, Italy.
Curr Med Chem. 2004 Apr;11(8):969-79. doi: 10.2174/0929867043455495.
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.
人尿紧张素II是一种强效血管收缩剂，与GPR14受体具有高亲和力，该受体最近被克隆并重新命名为UT受体。据报道，U-II的血管收缩效力比内皮素-1（ET-1）高一个数量级，这将使其成为迄今为止已确定的最有效的哺乳动物血管收缩剂。尿紧张素II是一种神经肽“生长抑素样”环肽，最初从鱼脊髓中分离出来，最近已从人身上克隆出来。人U-II仅由11个氨基酸残基组成，而鱼和蛙的U-II分别拥有12个和13个氨基酸残基。U-II的环区域负责该肽的生物活性，从鱼到人均已完全保守。本综述重点关注最近对尿紧张素II进行的构效关系研究，旨在提供所需的结构元件，以设计新的配体作为UT受体的激动剂和拮抗剂。
