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Characterization of endothelin converting enzyme from intact cells of a permanent human endothelial cell line EA.hy926
Author(s) -
Ahn Kyunghye,
Pan Sharon M.,
Zientek Michael A.,
Guy Pamela M.,
Sisneros Andre M.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201631
Subject(s) - phosphoramidon , thiorphan , neprilysin , endothelin receptor , chemistry , enzyme , endothelin 1 , enzyme inhibitor , cell culture , biochemistry , biology , genetics , receptor
Endothelin converting enzyme (ECE) from intact cells of a permanent human endothelial cell line, EA.hy926, was studied by examining the effects of phosphoramidon, an endothelin converting enzyme inhibitor, on the levels of secreted endothelin‐1 and big endothelin‐1. The specific ECE activity was demonstrated by a phosphoramidon dose‐dependent decrease in ET‐1 level with a concomitant increase in big ET‐1 level. By using a specific neutral endopeptidase 24.11 (NEP 24.11) inhibitor, thiorphan, it was also shown that the phosphoramidon‐sensitive ET‐1 degrading activity in this cell line is due to the NEP 24.11 activity. Other serine, acid, and cysteine protease inhibitors had no effect on the endogenous synthesis of ET‐1 and big ET‐1 supporting the evidence that ECE is insensitive to these protease inhibitors as has been demonstrated with the isolated enzyme.