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. 1991 Jan 31;174(2):446-51.
doi: 10.1016/0006-291x(91)91436-g.

Endothelin converting enzyme of bovine carotid artery smooth muscles

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Endothelin converting enzyme of bovine carotid artery smooth muscles

Y Hioki et al. Biochem Biophys Res Commun. .

Abstract

This is the first report clearly demonstrating the presence of endothelin (ET) converting enzyme in vascular smooth muscle. Like cultured endothelial cells, noncultured vascular smooth muscle homogenate of bovine carotid arteries, converts human big ET- 1 to ET-1 at pH 3.0, pH 5.0 and pH 7.0, and the apparent ratio of these three activities is about 6:5:1, respectively. Peptides generated during incubation of the homogenate and big ET- 1 at the three pHs were identified as ET- 1 by radioimmunoassay and high performance liquid chromatography. The two acid enzymes are in the cytosol (103,000xg sup) and are inhibited by pepstatin A, while the neutral enzyme is sensitive to EDTA or phosphoramidon; 73% of the neutral enzyme activity was membrane-bound and the remainder (27%) cytosolic.

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