|Precautions||SLIGKV-NH2 Protein is for research use only and not for use in diagnostic or therapeutic procedures.|
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Protease-activated receptors (PARs) 1-4 belong to the superfamily of G-protein-coupled receptors (GPCRs) that are self-activated by a tethered sequence exposed by proteolysis of an extracellular domain1. PARs are activated by proteolysis in response to endogenous and exogenous proteases and can contribute to both cellular homeostasis and pathology1-2. In the case of PAR2, the exposed human peptide SLIGVK-NH2 remains tethered on the receptor and activates a primary binding site located on second loop of the receptor1. As an obvious consequence of its activation mechanism, PAR2 is associated with pathologies with a strong protease release. The involvement of PAR2 in inflammatory diseases such as arthritis, lung inflammation (asthma), inflammatory bowel disease, sepsis, and pain disorders4-6makes PAR2 an attractive target for drug intervention3. The extracellular N-terminus of PAR2 (46 residues long) contains a putative trypsin cleavage site R34 and S351, followed by LIGKV. The human-derived SLIGKV-NH2is a small peptide that mimics the ligand binding properties of the tethered ligand exposed by proteolysis of the N-terminus from the natural receptor7 and hence, a significant tool used to study PAR2.
1 . Ossovskaya VS. et al.(2004)Physiol Rev.84,579.
2 . Rattenholl A. et al.(2008)Drug News Perspect. 21,369.
3 . Boitano S. et al.(2011)J. Med. Chem.54,1308.
4 . Barry GD. et al. (2006) Curr. Med. Chem.13,243.
5 . Steinhoff M. et al. (2005) Endocr.Rev.26, 1.
6 . Cottrell GS. et al.(2003)Biochem. Soc.Trans. 31, 1191.
7 . Ramachandran R. et al.(2008)Br. J. Pharmacol.153,S263.
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