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J Biol Chem. 1994 Jul 15;269(28):18275-8.

Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells.

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Biological Research Laboratories, Sankyo Co., Ltd., Tokyo, Japan.


Endothelin (ET) is a 21-residue potent vasoconstrictive peptide produced by vascular endothelial cells and formed from its precursor, big endothelin (big ET), by endothelin-converting enzyme (ECE). Here we report the cloning and functional expression of a complementary DNA encoding a rat ECE from endothelial cells. Rat ECE is a highly glycosylated protein consisting of 10 possible N-linked glycosylation sites, a zinc-binding domain, and a single membrane-spanning region. It has structural and sequence homology to neutral endopeptidase and Kell blood group protein, a putative neutral endopeptidase. Monoclonal antibody risen against purified rat lung ECE recognized broad glycosylated bands in membrane fractions prepared from both rat lung and COS cells transfected with a rat ECE expression vector. Expressed ECE was inhibited by phosphoramidon, but not by thiorphan. It also cleaved big ET-1 efficiently but not big ET-2 or big ET-3. Northern blot analysis revealed that ECE messenger RNA is widely expressed in many tissues.

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