Identification and characterization of endothelin converting activity in cultured bovine endothelial cells

Keizo Ohnaka, Ryoichi Takayanagi, Teruaki Yamauchi, Hiroshi Okazaki, Masao Ohashi, Fumio Umeda, Hajime Nawata

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103 Citations (Scopus)

Abstract

Using a specific and sensitive radioimmunoassay (RIA) for the carboxyl terminal tail of endothelin (ET) (His16-Trp21), we have confirmed the presence of the converting activity from synthetic human big ET-1 to ET-1 in the homogenate of cultured bovine aortic endothelial cells. The optimal pHs for the converting activities were found at pH 3.0 and pH 7.0. The activity at pH 3.0 was completely inhibited by pepstatin A, whereas the activity at pH 7.0 was not affected by known various protease inhibitors except EDTA and EGTA. When the products from big ET-1 were analyzed on an ODS and a CN columns, only ET-1 was detected at pH 7.0, but various ET-like immunoreactivities other than ET-1 were detected at pH 3.0. These findings strongly suggest that mature ET-1 is formed from big ET-1 in the endothelial cells by a metal-dependent neutral protease.

Original languageEnglish
Pages (from-to)1128-1136
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume168
Issue number3
DOIs
Publication statusPublished - May 16 1990

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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