Scientific Background | Human urotensin-II is described as the most potent mammalian vasoconstrictor identified, acting through the receptor originally catalogued as the orphan GPR14 and now known as the UT receptor. The supplied sequence is the eleven-residue human form, the shortest of the species variants offered here, comprising a short N-terminal extension and the disulfide-bridged cyclic core. That cyclic hexapeptide core is the pharmacophore. It is conserved across every species form of the peptide, and structure-activity work has established that the ring, not the variable N-terminal extension, carries the receptor-binding determinants. The practical implication is that the disulfide is not optional: a reduced or mis-paired preparation loses the constrained conformation the receptor recognises, so disulfide integrity should be confirmed rather than assumed, particularly after storage in reducing conditions. Because it is the human sequence, this is the variant for work on human receptors and tissues, including the cardiovascular and renal systems where the peptide and its receptor have been studied, and where increased expression of urotensin II and GPR14 has been reported in atherosclerotic lesions of the human aorta. For comparative pharmacology across species, the frog, goby and rat forms are offered separately and differ in their N-terminal extensions. |
References | 1. Ames RS, Sarau HM, Chambers JK, et al. Human urotensin-II is a potent vasoconstrictor and agonist for the orphan receptor GPR14. Nature (1999). PMID 10499587 2. Role of urotensin II in health and disease. American Journal of Physiology (2010). Am J Physiol 2010 3. Increased expression of urotensin II and its cognate receptor GPR14 in atherosclerotic lesions of the human aorta. Atherosclerosis expression |
