Urotensin-II
| |
| Names | |
|---|---|
| IUPAC name
L-α-glutamyl-L-threonyl-L-prolyl-L-α-aspartyl-L-cysteinyl-L-phenylalanyl-L-tryptophyl-L-lysyl-L-tyrosyl-L-cysteinyl-L-valine (5→10)-disulfide
| |
| Identifiers | |
3D model (JSmol)
|
|
| ChEMBL | |
| ChemSpider | |
| |
| |
| Properties | |
| C64H85N13O18S2 | |
| Molar mass | 1388.6 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
| |
| Urotensin-II | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | U-II | ||||||
| NCBI gene | 10911 | ||||||
| HGNC | 12636 | ||||||
| OMIM | 604097 | ||||||
| RefSeq | NM_021995 | ||||||
| UniProt | O95399 | ||||||
| Other data | |||||||
| Locus | Chr. 1# p36 | ||||||
| |||||||
Urotensin-II (U-II) is a peptide ligand, initially isolated from the neurosecretory system of the Goby fish (Gillichthys mirabilis).[1] For many years it was thought that U-II does not exhibit significant effects in mammalian systems; a view quickly overturned when it was demonstrated that Goby U-II produces slow relaxation of mouse anococcygeus muscle, in addition to contraction of rat artery segments. In 1998, the cDNA encoding a U-II precursor was cloned in humans, unequivocally demonstrating its existence in mammalian species.The vasoconstriction it induces can cause or exacerbate hypertension, congestive heart failure, and coronary artery disease.
In fish, U-II is secreted at the back part of the spinal cord, in a neurosecretory center called uroneurapophysa, and is involved in the regulation of the renal and cardiovascular systems.[2] In mammals, it is involved in the regulation of the cardiovascular system.[3]
U-II peptide
As with other peptide ligands, U-II is synthesised from a larger precursor molecule known as Prepro-urotensin-II. Two isoforms have been identified in man of lengths 124 and 139 residues. Cleavage of either of these precursors produces identical, eleven residue, mature U-II peptides. The cyclic, C-terminal hexapeptide sequence((-CYS*-TRY-LYS-TRP-PHE-CYS*-), (*bridged CYS residues)), has been conserved through evolution from lamprey to human species, which diverged some 560 million years ago. The fact that such a strong evolutionary pressure has acted to conserve this sequence highlights its physiological importance. Indeed, this hexapeptide sequence confers biological activity.
References
- ^ Bern HA, Lederis K (September 1969). "A reference preparation for the study of active substances in the caudal neurosecretory system of teleosts". J. Endocrinol. 45 (1): Suppl:xi–xii. PMID 5347394.
- ^ L. Fishelson, Zoology, renewed and corrected ed. 1984, Hakibutz Hameuchad Pub. House, Israel 1984. Vol II, p.126 (Hebrew)
- ^ Douglas SA, Dhanak D, Johns DG (2004). "From 'gills to pills': urotensin-II as a regulator of mammalian cardiorenal function". Trends Pharmacol. Sci. 25 (2): 76–85. doi:10.1016/j.tips.2003.12.005. PMID 15102493.
{{cite journal}}: CS1 maint: multiple names: authors list (link)