Abstract
Endothelin, originally isolated from culture media of porcine aortic endothelial cells, is one of the most potent vasoactive peptide known to date and consists of 21 amino acids containing two intracellular disulfide bonds.21 In addition to vasoconstrictor activity, it has been found that endothelin has a variety of biological actions: it increases blood pressure;21,22 stimulates release of atrial natriuretic peptide,4 prostacyclin, thromboxane A2, and endothelial cell—derived relaxing factor3; and inhibits renin release.12 Moreover, three isopeptides of endothelin have been identified based on the analysis of a human genomic library and named endothelin-1, endothelin-2, and endothelin-3.5 These findings raise the question of how the endothelin isopeptides and their various biological actions are related. It is also of great interest to know whether the three endothelin isopeptides have their own specific receptors, respectively, or bind in common to a homologous population of endothelin receptors. The elucidation of these problems is essential for understanding the physiological roles of endothelin.
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© 1992 American Physiological Society
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Miyazaki, H., Kondoh, M., Masuda, Y., Watanabe, H., Murakami, K. (1992). Endothelin Receptors and Receptor Subtypes. In: Rubanyi, G.M. (eds) Endothelin. Clinical Physiology Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-7514-9_5
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DOI: https://doi.org/10.1007/978-1-4614-7514-9_5
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