Characterization of the endothelin-converting enzyme in guinea pig upper bronchus

J Cardiovasc Pharmacol. 1995:26 Suppl 3:S81-3.

Abstract

We studied the pharmacologic effects of big endothelin-1 (big ET-1), big endothelin-2 (big ET-2), and big endothelin-3 (big ET-3), and characterized the enzyme involved in the conversion of the three peptides in guinea pig upper bronchus (GPUB). ET-1, ET-2 and ET-3 (0.1-300 nM) elicited similar concentration-dependent contractions of GPUB. Big ET-1 and big ET-2, but not big ET-3, also elicited potent concentration-dependent contractions of GPUB. The conversion of big ET-1 to ET-1 in the GPUB is sensitive to phosphoramidon but not to thiorphan or captopril. Phosphoramidon inhibited the conversion of big ET-2 to ET-2, thiorphan had minimal effect, and captopril was without effect. These results suggest that the putative endothelin-converting enzyme (ECE) is involved in the conversion of big ET-1 to ET-1 in GPUB and the conversion of big ET-2 to ET-2 by a nonselective enzymatic process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspartic Acid Endopeptidases / metabolism*
  • Bronchi / drug effects
  • Bronchi / enzymology*
  • Dose-Response Relationship, Drug
  • Endothelin-Converting Enzymes
  • Endothelins / pharmacology
  • Glycopeptides / pharmacology
  • Guinea Pigs
  • Metalloendopeptidases
  • Thiorphan / pharmacology

Substances

  • Endothelins
  • Glycopeptides
  • Thiorphan
  • Aspartic Acid Endopeptidases
  • Metalloendopeptidases
  • Endothelin-Converting Enzymes
  • phosphoramidon