title: Binding characteristics of [125I]endothelin-1 in guinea-pig trachea and its displacement by endothelin-1, endothelin-3 and endothelin (16-21).
abstract: The presence of binding sites for endothelin-1 (ET-1) and endothelin-3 (ET-3) in airway epithelium, submucosa and smooth muscle of guinea-pig trachea was investigated using in vitro autoradiography. We also examined the ability of the C-terminal hexapeptide of endothelin, ET(16-21) to inhibit specific [125I]ET-1, binding. ET-1 appeared to bind to a single class of binding sites (nH not different from unity). In contrast, nH values for ET-3 displacement of [125I]ET-1 specific binding were different from unity, suggesting that these peptides bound to more than one site. ET (16-21) did not affect [125I]ET-1 binding. The present results suggest that the binding sites identified in guinea pig airway smooth muscle may be related to receptors mediating contractile responses to the endothelins.
authors.affiliation: Merrell Dow Research Institute, Strasbourg, France.
authors.forename: E J
authors.initials: EJ
authors.lastname: Tschirhart
authors.forename: J T
authors.initials: JT
authors.lastname: Pelton
authors.forename: C R
authors.initials: CR
authors.lastname: Jones
mesh_terms: D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D016232:Endothelins / Q000378:metabolism*; D006168:Guinea Pigs; D007457:Iodine Radioisotopes; D010446:Peptide Fragments / Q000378:metabolism*; D014018:Tissue Distribution; D014132:Trachea / Q000378:metabolism*
chemical_list: D016232:Endothelins; D007457:Iodine Radioisotopes; D010446:Peptide Fragments; C061533:endothelin (16-21)