Different pressor and bronchoconstrictor properties of human big-endothelin-1, 2 (1-38) and 3 in ketamine/xylazine-anaesthetized guinea-pigs

Br J Pharmacol. 1995 Feb;114(3):720-6. doi: 10.1111/j.1476-5381.1995.tb17198.x.

Abstract

1. In the present study, the precursors of endothelin-1, endothelin-2 and endothelin-3 were tested for their pressor and bronchoconstrictor properties in the anaesthetized guinea-pig. In addition, the effects of big-endothelin-1 and endothelin-1 were assessed under urethane or ketamine/xylazine anaesthesia. 2. When compared to ketamine/xylazine, urethane markedly depressed the pressor and bronchoconstrictor properties of endothelin-1 and big-endothelin-1. 3. Under ketamine/xylazine anaesthesia, the three endothelins induced a biphasic increase of mean arterial blood pressure. In contrast, big-endothelin-1, as well as big-endothelin-2 (1-38), induced only sustained increase in blood pressure whereas big-endothelin-3 was inactive at doses up to 25 nmol kg-1. 4. Big-endothelin-1, but not big-endothelin-2, induced a significant increase in airway resistance. Yet, endothelin-1, endothelin-2 and endothelin-3 were equipotent as bronchoconstrictor agents. 5. Big-endothelin-1, endothelin-1 and endothelin-2, but not big-endothelin-2, triggered a marked release of prostacyclin and thromboxane A2 from the guinea-pig perfused lung. 6. Our results suggest the presence of a phosphoramidon-sensitive endothelin-converting enzyme (ECE) which is responsible for the conversion of big-endothelin-1 and big-endothelin-2 to their active moieties, endothelin-1 and 2. However, the lack of bronchoconstrictor and eicosanoid-releasing properties of big-endothelin-2, as opposed to endothelin-2 or big-endothelin-1, suggests the presence of two distinct phosphoramidon-sensitive ECEs in the guinea-pig. The ECE responsible for the systemic conversion of big-endothelins possesses the same affinity for big-endothelin-l and 2 but not big-endothelin-3. In contrast, in the pulmonary vasculature is localized in the vicinity of the sites responsible for eicosanoid release, an ECE which converts more readily big-endothelin-1 than big-endothelin-2.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Analysis of Variance
  • Animals
  • Aspartic Acid Endopeptidases / metabolism
  • Blood Pressure / drug effects*
  • Bronchoconstriction / drug effects*
  • Dose-Response Relationship, Drug
  • Endothelin-1
  • Endothelin-Converting Enzymes
  • Endothelins / pharmacology*
  • Epoprostenol / metabolism
  • Female
  • Glycopeptides / pharmacology
  • Guinea Pigs
  • Humans
  • In Vitro Techniques
  • Ketamine
  • Lung / drug effects
  • Lung / metabolism
  • Male
  • Metalloendopeptidases / metabolism
  • Muscle, Smooth / drug effects*
  • Protease Inhibitors / pharmacology
  • Protein Precursors / pharmacology*
  • Thromboxane A2 / metabolism
  • Urethane
  • Xylazine

Substances

  • Endothelin-1
  • Endothelins
  • Glycopeptides
  • Protease Inhibitors
  • Protein Precursors
  • Xylazine
  • Urethane
  • Thromboxane A2
  • Ketamine
  • Epoprostenol
  • Aspartic Acid Endopeptidases
  • Metalloendopeptidases
  • Endothelin-Converting Enzymes
  • phosphoramidon