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Characterisation of endothelin converting enzyme‐1 shedding from endothelial cells
Author(s) -
Kuruppu Sanjaya,
Reeve Shane,
Ian Smith A.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.028
Subject(s) - ectodomain , umbilical vein , cleavage (geology) , enzyme , chemistry , endothelin 1 , metalloproteinase , matrix metalloproteinase , substrate (aquarium) , endothelins , microbiology and biotechnology , biochemistry , biophysics , biology , in vitro , paleontology , ecology , receptor , fracture (geology)
The aim of this study was to determine if endothelin converting enzyme‐1 (ECE‐1) like other members of this metalloprotease family undergoes ectodomain shedding. The release/shedding of catalytically active ECE‐1 was measured by monitoring the fluorescence resulting from the cleavage of a specific quenched fluorescent substrate. Catalytically active ECE‐1 was detected in the media of human umbilical vein endothelial cells, and was confirmed by mass spectrometry based assays. Specificity of cleavage was confirmed by using both narrow and broad specificity inhibitors. In conclusion we demonstrate and characterize for the first time, ECE‐1 shedding from the surface of endothelial cells.