Endothelin pp 75-92 | Cite as

Molecular Biology of Endothelin-Converting Enzyme (ECE)

  • Ryoichi Takayanagi
  • Keizo Ohnaka
  • Wei Liu
  • Takeshi Ito
  • Hajime Nawata
Part of the Contemporary Biomedicine book series (CB)


Endothelin (ET) was originally isolated from culture media of aortic endothelial cells as a potent vasoconstrictive peptide (1). An active form of ET, consisting of 21 amino-acid residues, is generated from an inactive form of big ET-1 by a specific enzyme, called endothelin-converting enzyme (ECE). Accelerated production of ET-1 in damaged vascular endothelial cells was strongly suggested to be involved in the development of various fatal cardiovascular disorders, such as acute myocardial infarction, acute renal failure, and posthemorrhagic cerebral vasospasm. The design of specific inhibitors of ECE, along with those of ET receptors, may lead to the development of new treatments for these diseases. Accordingly, many investigators have focused on the identification and characterization of ECE. This chapter describes a history from the discovery of ECE to molecular characterization of this enzyme.


Hydrolysis Rate Aspartic Protease Bovine Aortic Endothelial Cell Putative Transmembrane Domain Bovine Endothelial Cell 
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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Ryoichi Takayanagi
  • Keizo Ohnaka
  • Wei Liu
  • Takeshi Ito
  • Hajime Nawata

There are no affiliations available

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