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

M. Yanagisawa, A. Inoue, T. Ishikawa, Y. Kasuya, S. Kimura, S. Kumagaye, K. Nakajima, T. X. Watanabe, S. Sakakibara, K. Goto, T. Masaki

Research output: Contribution to journalArticle

531 Scopus citations

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 endothelium; 15 residues of rat endothelium 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.

Original languageEnglish (US)
Pages (from-to)6964-6967
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number18
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Primary structure, synthesis, and biological activity of rat endothelin, an endothelium-derived vasoconstrictor peptide'. Together they form a unique fingerprint.

  • Cite this