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Endothelin (ET) is a potent vasoconstrictor/ pressor peptide consisting of 21 amino acid residues isolated from the cultures of porcine aortic endothelial cells1}. Analysis of a human genomic library reveals three forms of ET (ET-1, ET-2 and ET-3) which have more than 70% homology with one another2). In various organs, high affinity and specific receptors for ET have been found3). They have been distinguished as receptors ETA and ETB4-5). ET-1 exhibits potent and long-lasting vasoconstrictive activity in vivo and in vitro1"1, as a

Asterric acid, a new endothelin binding inhibitor.