Abstract
Endothelin (ET), originally isolated from cultured porcine aortic endothelial cells, is a highly potent vasoconstricting peptide with 21-amino acid residues.1 Three distinct members of the ET family, namely, ET-1, ET-2 and ET-3, have been identified in humans through cloning.2 The effects of ETs on mammalian organs and cells are initiated by their binding to high affinity G-protein linked receptors. ET receptors are found in various tissues such as brain, lung, and kidney.3 Two major types of ET receptors in the mammalian system, ETA and ETB, have been characterized, isolated and their cDNAs cloned.4–7 ETA receptors are selective for ET-1 and ET-2, while ETB receptors bind to ET-1, ET-2 and ET-3 with equal affinity. Pharmacologically defined subtypes of ETA and ETB receptors have also been reported.8,9 Various antagonists and agonists for ET receptors have been developed. Comprehensive reviews on the pharmacological properties of these ligands are available.10–13 For discussion purposes, some of the ET receptor ligands along with the IC50. values against ETA and ETB receptors are listed in Table 4.1.14–27
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