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

研究成果: Contribution to journalArticle査読

103 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)1128-1136
ページ数9
ジャーナルBiochemical and Biophysical Research Communications
168
3
DOI
出版ステータス出版済み - 5 16 1990

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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