Urotensin Family Related Drug Discovery Products
Creative Biolabs has the assays you can rely on for high throughput screening, lead optimization, characterizing and discovering targets, and uncovering the complexity of disease pathways. We can offer membrane protein in vitro assay kits that save valuable laboratory time and is ideal for high throughput screening.
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
Urotensin-II (U-II) is a group of cyclic peptides found in a variety of animal taxa, including frogs, fish, and humans. These peptides range in size from 8 to 14 amino acids. The disulfide-linked cyclic array that contains amino acid residues 5 through 10 in human U-II is highly species-conserved, in contrast to the N-terminal section from other species, which varies in length and make-up. It has been discovered that the U-II peptides are among of the most effective known vasoconstrictors. U-II peptides cause the urotensin-II receptor (UT), a GPCR found in a variety of species, to become active. Numerous tissues, including blood vessels, the heart, liver, kidney, skeletal muscle, and the lung, express this receptor. Cardiorenal and metabolic disorders, such as hypertension, heart failure, chronic renal failure, diabetes, and atherosclerosis, have been linked to U-II and its receptor.
Fig.1. U-II peptides. (Maryanoff & Kinney, 2010)
Creative Biolabs can offer high-quality urotensin family drug discovery assays and related tools to meet the needs of drug discovery:
Overview of Urotensin Family
The pertussis toxin-insensitive G protein Gαq/11 is the main link connecting UT to phospholipase C (PLC) activation. Phosphatidylinositol-4-5 bisphosphate (PIP2) is hydrolyzed to inositol-1-4-5 triphosphate (IP3) and diacylglycerol upon UII attachment to UT. A rise in cytoplasmic calcium levels happens when IP3 binds to the IP3 receptor. Numerous cell types, including the human aorta endothelial cells, the pig renal epithelial cell line LLCPK1, and the rat aorta vascular smooth muscle cells, have recently been shown to be subject to UII-induced intracellular calcium mobilization.
Additionally, UT and Gαi/o are coupled, which activates the mitogen-activated protein kinase (MAPK) pathway. Thus, in UT-transfected cell lines, cardiac myocytes, vascular smooth muscle cells, airway smooth muscle cells, endothelial cells, and endothelium-denuded rat aorta, UII promotes P38MAPK and extracellular signal-regulated kinase 1/2. Through the activation of p38 and p44/42 MAPK, UII also promotes the growth of endothelial progenitor cells.
Fig.2. Signaling pathways of UII receptor. (Vaudry, 2015)
Urotensin Family Drug Discovery
Significant study has been done to comprehend the role of UII in human physiology and disease since the discovery of the powerful vasoconstrictor and biologic effects of UII. Nonpeptidic UII antagonists are alluring substitutes for peptidic antagonists and present a chance to assess the function of UII in chronic diseases. With the help of these pharmacological methods, the function of endogenous UII in pathophysiology has been investigated. The clinical symptoms that have received the most research is diabetes, atherosclerosis, pulmonary hypertension, asthma, heart failure, and hypertension. Clinical investigations have not fully established the understanding of the role of UII in human pathophysiology, and there is currently a dearth of human inquiry with UT antagonists.
References
- Maryanoff, B.E.; Kinney, W. A. Urotensin-II receptor modulators as potential drugs. Journal of medicinal chemistry. 2010, 53(7): 2695-2708.
- Vaudry, H.; et al. International Union of Basic and Clinical Pharmacology. XCII. Urotensin II, urotensin II–related peptide, and their receptor: From structure to function. Pharmacological reviews. 2015, 67(1): 214-258.
