BQ-123 identifies heterogeneity and allosteric interactions at the rat heart endothelin receptor.
Studies of the binding of endothelin-1 (ET-1) to its receptors in the rat heart, as well as kinetic measurements in the presence and absence of the specific antagonist BQ-123, appear to exclude a scheme of simple competitive inhibition and an interaction of ET-1 with a homogeneous population of receptors. Studies with BQ-123 established the presence of three subtypes of endothelin receptors and an allosteric interaction, suggesting the possible existence of a specific site for BQ-123 that interacts and/or interferes with the properties of endothelin-binding sites.
Sokolovsky
M
M
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
D000494:Allosteric Regulation; D000818:Animals; D002478:Cells, Cultured; D065128:Endothelin Receptor Antagonists; D016232:Endothelins / Q000378:metabolism*; D014644:Genetic Variation; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D009206:Myocardium / Q000378:metabolism*; D010456:Peptides, Cyclic / Q000378:metabolism*; D010716:Phosphatidylinositols / Q000378:metabolism; D051381:Rats; D017466:Receptors, Endothelin / Q000378:metabolism*
D065128:Endothelin Receptor Antagonists; D016232:Endothelins; D010456:Peptides, Cyclic; D010716:Phosphatidylinositols; D017466:Receptors, Endothelin; C072247:cyclo(Trp-Asp-Pro-Val-Leu)