Conversion of big endothelin isopeptides to mature endothelin isopeptides by cultured bovine endothelial cells

K. Ohnaka, R. Takayanagi, M. Ohashi, H. Nawata

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Both the soluble and membrane fractions prepared from cultured bovine endothelial cells (ECs) possessed the converting activities to metabolize big endothelin-1 (big ET-1) to endothelin-1 (ET-1) at neutral pH. Metal chelators inhibited the activities of both fractions, whereas phosphoramidon, a metalloprotease inhibitor, strongly inhibited only the activity of the membrane fraction. Phosphoramidon reduced the secretion of ET-1 and concomitantly enhanced the release of big ET-1 from cultured ECs. The incubations of big ET-1, big ET-2, and big ET-3 with cultured ECs resulted in their conversions to mature ETs. Phosphoramidon also abolished these conversions. These results indicate that vascular endothelium can convert not only endogenous big ET-1 but also exogenous big ET isopeptides to their mature ETs through a phosphoramidon-sensitive neutral metalloprotease.

Original languageEnglish
Pages (from-to)S17-S19
JournalJournal of Cardiovascular Pharmacology
Volume17
Publication statusPublished - Jan 1 1991

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Endothelins
Endothelin-1
Endothelial Cells
Metalloproteases
Cultured Cells
Membranes
Vascular Endothelium
Chelating Agents
Metals
phosphoramidon

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Cardiology and Cardiovascular Medicine

Cite this

Conversion of big endothelin isopeptides to mature endothelin isopeptides by cultured bovine endothelial cells. / Ohnaka, K.; Takayanagi, R.; Ohashi, M.; Nawata, H.

In: Journal of Cardiovascular Pharmacology, Vol. 17, 01.01.1991, p. S17-S19.

Research output: Contribution to journalArticle

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