Journal
FEBS LETTERS
Volume 581, Issue 23, Pages 4501-4506Publisher
WILEY
DOI: 10.1016/j.febslet.2007.08.028
Keywords
endothelin; ECE-1; fluorescence; ectodomain shedding; mass spectrometry
Ask authors/readers for more resources
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. (c) 2007 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available