Structure-activity relationships of endothelin: Importance of the C-terminal moiety

Sadao Kimura, Yoshitoshi Kasuya, Tatsuya Sawamura, Osamu Shinmi, Yoshiki Sugita, Masashi Yanagisawa, Katsutoshi Goto, Tomoh Masaki

Research output: Contribution to journalArticlepeer-review

221 Scopus citations

Abstract

The vasoconstrictor activities of various forms of derivatives of endothelin (ET) were characterized in vitro by measuring the contraction of porcine coronary artery strips. The removal of the C-terminal Trp21 reduced the molar potency of the peptide by nearly 3 orders of magnitude. The removal of amino acid residues from the C-terminus of ET(1-20) further attenuated the activity. Replacement of Trp21 with D-Trp, reduction and carboxamidomethylation of the four Cys residues, or cleavage at Lys9 by lysyl endopeptidase all lowered the potency approximately 200 fold. While both native ET and [D-Trp21]ET induced a very slow and sustained vasoconstriction, the other derivatives of ET listed above showed a much more rapid kinetics of vasoconstriction. These results indicate that the C-terminal Trp of ET is especially important for the potent and extremely long-lasting vasoconstrictor activity characteristic to ET.

Original languageEnglish (US)
Pages (from-to)1182-1186
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume156
Issue number3
DOIs
StatePublished - Nov 15 1988

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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