Abstract
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 language | English (US) |
|---|---|
| Pages (from-to) | 1138-1144 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 169 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jun 29 1990 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Characterization of endothelin converting enzyme activities in soluble fraction of bovine cultured endothelial cells. / Sawamura, Tatsuya; Kimura, Sadao; Shinmi, Osamu; Sugita, Yoshiki; Kobayashi, Mieko; Mitsui, Youji; Yanagisawa, Masashi; Goto, Katsutoshi; Masaki, Tomoh.
In: Biochemical and Biophysical Research Communications, Vol. 169, No. 3, 29.06.1990, p. 1138-1144.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of endothelin converting enzyme activities in soluble fraction of bovine cultured endothelial cells
AU - Sawamura, Tatsuya
AU - Kimura, Sadao
AU - Shinmi, Osamu
AU - Sugita, Yoshiki
AU - Kobayashi, Mieko
AU - Mitsui, Youji
AU - Yanagisawa, Masashi
AU - Goto, Katsutoshi
AU - Masaki, Tomoh
PY - 1990/6/29
Y1 - 1990/6/29
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(90)92014-Q
DO - 10.1016/0006-291X(90)92014-Q
M3 - Article
C2 - 2194455
AN - SCOPUS:0025296232
VL - 169
SP - 1138
EP - 1144
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -