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

Masashi Yanagisawa1, Akihiro Inoue1, Tomohisa Ishikawa1, Yoshitoshi Kasuya1, Sadao Kimura1, S Kumagaye1, Kiichiro Nakajima1, Teruo Watanabe1, Shin‐ichi Sakakibara1, Katsutoshi Goto1
1Institute of Basic Medical Sciences, University of Tsukuba, Ibaraki, Japan

Tóm tắt

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.

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