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Peptide ligand binding properties of the corticotropin-releasing factor (CRF) type 2 receptor: pharmacology of endogenously expressed receptors, G-protein-coupling sensitivity and determinants of CRF2 receptor selectivity

Peptide ligand binding properties of the corticotropin-releasing factor (CRF) type 2 receptor: pharmacology of endogenously expressed receptors, G-protein-coupling sensitivity and determinants of CRF2 receptor selectivity. Hoare, Sam R. J.; Sullivan, Susan K.; Fan, Jun; Khongsaly, Khamkeo; Grigoriadis, Dimitri E. (Department of Pharmacology, Neurocrine Biosciences Inc., San Diego, CA 92130, USA). Peptides (New York, NY, United States), 26(3), 457-470 (English) 2005 Elsevier Inc.Some commonly used reagents like 9015-71-8 and 220673-95-0 are used in this experiment. CODEN: PPTDD5. ISSN: 0196-9781. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) The CRF2 receptor is involved in stress responses, cardiovascular function and gastric motility. Endogenous agonists (Urocortin (UCN) 2, UCN 3) and synthetic antagonists (astressin2-B, Antisauvagine-30) are selective for CRF2 over the CRF1 receptor. Peptide ligand binding properties of the CRF2 receptor require further investigation, including ligand affinity for endogenously expressed receptors, the effect of receptor-G-protein coupling on ligand affinity, and the mol. basis of ligand selectivity. Ligand affinity for rat CRF2(a) in olfactory bulb and CRF2(b) in A7r5 cells was similar to that for the cloned human CRF2(a) receptor (within three-fold), except for oCRF (9.4- and 5.4-fold higher affinity in olfactory bulb and A7r5 cells, resp.). Receptor-G-protein uncoupling reduced agonist affinity only 1.2- to 6.5-fold (compared with 92-1300-fold for the CRF1 receptor). Ligand selectivity mechanisms were investigated using chimeric CRF2/CRF1 receptors. The juxtamembrane receptor domain detd. selectivity of Antisauvagine-30, the N-terminal-extracellular domain contributed to selectivity of UCN 3, and both domains contributed to selectivity of UCN 2 and astressin2-B. Therefore ligands differ in the contribution of receptor domains to their selectivity, and CRF2-selective antagonists bind the juxtamembrane domain. These findings will be important for identifying the CRF2 receptor in tissues and for developing ligands targeting the receptor, both of which will be useful in identifying the emerging physiol. functions of the CRF2 receptor. .