Primary structure, synthesis, and biological activity of rat endothelin, an endothelium-derived vasoconstrictor peptide.

TLDR

Endothelin is a potent vasoconstrictor/pressor peptide, recently characterized from conditioned medium of porcine aortic endothelial cells. We report the cloning and partial sequencing of the rat endothelin gene. Synthetic rat endothelin was prepared according to its deduced amino acid sequence. The synthetic 21‑residue peptide, sharing 15 residues with porcine endothelin, produced potent vasoconstriction in rat aortic strips and perfused hearts and elicited a long‑lasting pressor response when injected intraaortically into conscious rats.

Abstract

Endothelin is a potent vasoconstrictor/pressor peptide, which we recently characterized from the conditioned culture medium of porcine aortic endothelial cells. We report here the cloning and partial sequencing of the rat endothelin gene. The nucleotide sequence predicted a 21-residue peptide similar to, but distinct from, porcine endothelin; 15 residues of rat endothelin were identical and 3 residues were substitutions by chemically similar amino acid residues to those in the porcine peptide. Synthetic rat endothelin was then prepared according to its deduced amino acid sequence. This synthetic peptide had (i) potent vasoconstrictor activity in the rat aortic strip and in perfused rat heart and (ii) a characteristically long-lasting in vivo pressor activity by intraaortic bolus injection in the conscious rat.