Key result
A novel 140 kDa endothelin-converting enzyme (ECE-3) purified from bovine iris microsomes specifically converted big ET-3 to ET-3 with a Km of 0.14 microM, distinct from ECE-1 and ECE-2.
Population
Bovine iris microsomes and CHO-K1 cells expressing recombinant human ET(B) receptors
Design
Preclinical
Authors
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Novel ECE-3 may mediate tissue-specific ET-3 production; leaves open its human cardiovascular relevance and therapeutic targeting.
The identification of ECE-3 reveals a novel metalloprotease specifically responsible for the production of the vasoactive peptide ET-3.
Hasegawa et al. (1998) studied this question. Purification of ECE-3 was evaluated on Conversion of big ET-3 to ET-3. A novel 140 kDa endothelin-converting enzyme (ECE-3) purified from bovine iris microsomes specifically converted big ET-3 to ET-3 with a Km of 0.14 microM, distinct from ECE-1 and ECE-2.
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