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Gene Review

ECE1  -  endothelin converting enzyme 1

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Disease relevance of ECE1


High impact information on ECE1

  • We report the identification of ECE-1, a novel membrane-bound neutral metalloprotease that is expressed abundantly in endothelial cells in vivo and is structurally related to neutral endopeptidase 24.11 and Kell blood group protein [2].
  • ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1 [2].
  • When transfected into cultured cells that normally secrete only big ET-1, the ECE-1 cDNA conferred the ability to secrete mature ET-1 [2].
  • Endothelin-converting enzyme-1 (ECE-1) cleaves big endothelins, as well as bradykinin and beta-amyloid peptide [3].
  • Several isoforms of ECE-1 (a-d) have been identified to date; they differ only in their NH(2) terminus but share the catalytic domain located in the COOH-terminal end [3].

Biological context of ECE1


Anatomical context of ECE1


Associations of ECE1 with chemical compounds

  • Co-expression of the cloned cDNA of bovine ECE with human preproET-1 cDNA in CHO-K1 cells resulted in the production of mature ET-1 and this production was inhibited by phosphoramidon [5].
  • Treatment with chlorophenyl-thio cyclic AMP (200 microM) for 24 h decreased ECE-1 and -2 expression to approximately 50% and approximately 40% of the control value, respectively [10].
  • These increases in ECE-1 and -2 expression with TPA were inhibited by cotreatment with calphostin C (10(-7) M) [10].
  • Treatment of BPASMC with a phosphorothioate antisense ODN to ECE-1c caused a marked reduction in ECE-1c mRNA levels and ECE-1 protein levels [8].
  • We have established a novel method of molecular cloning of endothelin converting enzyme, a key enzyme in the production of a potent vasoconstrictor endothelin-1, by modification of the reverse hemolytic plaque assay [9].

Regulatory relationships of ECE1


Other interactions of ECE1

  • Analyses of chimeric ECE-1/transferrin receptors demonstrate that the cytoplasmic tail of bovine ECE-1a is sufficient for the lysosomal delivery and rapid degradation [12].
  • Ribonuclease protection assay revealed the expression of ECE-1 and -2 in cultured GEN, and the expression was increased approximately 2.5- and approximately 1.8-fold, respectively, by treatment with 10(-7) M 12-O-tetradecanocyl-phorbol-13-acetate (TPA) for 4 hours [10].

Analytical, diagnostic and therapeutic context of ECE1

  • The novel protein, designated ECE-1 sv, has an apparent molecular mass of 75 kDa; by using site-directed mutagenesis its start site was identified in a region common to all ECE-1 forms suggesting that ECE-1 b-d SV mRNAs are translated into the same protein [3].
  • Northern blot analysis revealed that ECE mRNA was abundantly expressed in lung [5].
  • Sequencing of cloned ECE-1 cDNA products and semiquantitative RT-PCR demonstrated that ECE-1b and ECE-1c were expressed in BPASMC, with ECE-1c being the predominant isoform [8].
  • The ECE-1 and ET(A) proteins were evaluated by semiquantitative Western blot analysis [13].
  • Genetic transfer of endothelin converting enzyme activity to CHO-K1 cells: detection of positive cells by reverse hemolytic plaque assay [9].


  1. Relationship between soluble intracellular endothelin-converting enzyme and endothelin-1 synthesis: effect of inhibitors of the secretory pathway. Corder, R., Khan, N.Q., Harrison, V.J., Wood, E.G., Lees, D.M., Barker, S. J. Cardiovasc. Pharmacol. (2000) [Pubmed]
  2. ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Xu, D., Emoto, N., Giaid, A., Slaughter, C., Kaw, S., deWit, D., Yanagisawa, M. Cell (1994) [Pubmed]
  3. Endothelin-converting enzyme-1, abundance of isoforms a-d and identification of a novel alternatively spliced variant lacking a transmembrane domain. Meidan, R., Klipper, E., Gilboa, T., Muller, L., Levy, N. J. Biol. Chem. (2005) [Pubmed]
  4. Hormonal regulation and cell-specific expression of endothelin-converting enzyme 1 isoforms in bovine ovarian endothelial and steroidogenic cells. Levy, N., Gordin, M., Smith, M.F., Bolden-Tiller, O.U., Meidan, R. Biol. Reprod. (2003) [Pubmed]
  5. cDNA cloning and expression of bovine endothelin converting enzyme. Ikura, T., Sawamura, T., Shiraki, T., Hosokawa, H., Kido, T., Hoshikawa, H., Shimada, K., Tanzawa, K., Kobayashi, S., Miwa, S. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  6. Distinct cellular localization and regulation of endothelin-1 and endothelin-converting enzyme-1 expression in the bovine corpus luteum: implications for luteolysis. Levy, N., Gordin, M., Mamluk, R., Yanagisawa, M., Smith, M.F., Hampton, J.H., Meidan, R. Endocrinology (2001) [Pubmed]
  7. Effect of cell density on endothelin release from endothelial cells and phosphoramidon dependent inhibition. Zaragoza, R., Budzik, G.P., Dillon, T.P., Opgenorth, T.J. Biochem. Pharmacol. (1992) [Pubmed]
  8. Effect of an antisense oligodeoxynucleotide to endothelin-converting enzyme-1c (ECE-1c) on ECE-1c mRNA, ECE-1 protein and endothelin-1 synthesis in bovine pulmonary artery smooth muscle cells. Barker, S., Khan, N.Q., Wood, E.G., Corder, R. Mol. Pharmacol. (2001) [Pubmed]
  9. Genetic transfer of endothelin converting enzyme activity to CHO-K1 cells: detection of positive cells by reverse hemolytic plaque assay. Shiraki, T., Sawamura, T., Ikura, T., Kobayashi, S., Miwa, S., Masaki, T. FEBS Lett. (1994) [Pubmed]
  10. Regulated expression of endothelin converting enzymes in glomerular endothelial cells. Uchida, K., Uchida, S., Nitta, K., Yumura, W., Nihei, H. J. Am. Soc. Nephrol. (1997) [Pubmed]
  11. Effects of endothelin-converting enzyme inhibitors on hemolysate-induced morphological changes and production of endothelin-1 in bovine cerebrovascular endothelial cells. Kwan, A.L., Lin, C.L., Chang, C.Z., Winardi, D., Yen, C.P., Howng, S.L., Jeng, A.Y. J. Cardiovasc. Pharmacol. (2000) [Pubmed]
  12. Constitutive lysosomal targeting and degradation of bovine endothelin-converting enzyme-1a mediated by novel signals in its alternatively spliced cytoplasmic tail. Emoto, N., Nurhantari, Y., Alimsardjono, H., Xie, J., Yamada, T., Yanagisawa, M., Matsuo, M. J. Biol. Chem. (1999) [Pubmed]
  13. Prostaglandin F(2alpha) regulation of the bovine corpus luteum endothelin system during the early and midluteal phase. Wright, M.F., Sayre, B., Keith Inskeep, E.K., Flores, J.A. Biol. Reprod. (2001) [Pubmed]
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