Characterization of endothelin converting enzyme activities in soluble fraction of bovine cultured endothelial cells

Tatsuya Sawamura, Sadao Kimura, Osamu Shinmi, Yoshiki Sugita, Mieko Kobayashi, Youji Mitsui, Masashi Yanagisawa, Katsutoshi Goto, Tomoh Masaki

Research output: Contribution to journalArticlepeer-review

66 Scopus citations


Endothelin converting enzyme activities in the soluble fraction of cultured bovine aortic endothelial cells were characterized. The two major endothelin converting enzyme activities were eluted from a hydrophobic chromatography column and the elution profile of the endothelin converting enzyme activities was the same as that of cathepsin D activities. These activities had a same pH optimum at pH 3.5 and were effectively inhibited by pepstatin A. Furthermore, anti-cathepsin D antiserum absorbed these activities as well as cathepsin D activity. Immunoblotting analysis using the antiserum showed the major active fractions have immunostainable components of identical molecular weights with cathepsin D. From these results, we concluded that the major endothelin converting activities in the soluble fraction of endothelial cells are due to cathepsin D. In addition to these cathepsin D activities, a minor endothelin converting enzyme activity with an optimum pH at 3.5 was found, which does not have angiotensin I generating (cathepsin D) activity from renin substrate and needs much higher concentrations of pepstatin A to inhibit the activity than cathepsin D.

Original languageEnglish (US)
Pages (from-to)1138-1144
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Jun 29 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Characterization of endothelin converting enzyme activities in soluble fraction of bovine cultured endothelial cells'. Together they form a unique fingerprint.

Cite this