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Effect of phosphoramidon on big endothelin-2 conversion into endothelin-2 in human renal adenocarcinoma (ACHN) cells. Analysis of endothelin-2 biosynthetic pathway.

Abstract
The biosynthetic pathway of endothelin (ET)-2 was analyzed in cultured ACHN cells. In the supernatant, we detected three ET-2-related peptides, ET-2, big ET-2(1-38) and big ET-2(22-38). Phosphoramidon decreased the amount of ET-2 and increased that of big ET-2(1-38) dose-dependently. The amount of big ET-2(1-37) did not significantly change. These results suggest that big ET-2 is composed of 38 and not 37 amino acid residues, and that a putative ET-2-converting enzyme (ECE-2) should be classified as a phosphoramidon-sensitive neutral metalloprotease, bearing a resemblance to the putative ET-1-converting enzyme (ECE-1) in endothelial cells.
AuthorsK Yorimitsu, O Shinmi, M Nishiyama, K Moroi, Y Sugita, T Saito, Y Inagaki, T Masaki, S Kimura
JournalFEBS letters (FEBS Lett) Vol. 314 Issue 3 Pg. 395-8 (Dec 21 1992) ISSN: 0014-5793 [Print] England
PMID1468574 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Endothelin-1
  • Endothelins
  • Glycopeptides
  • Protein Precursors
  • Aspartic Acid Endopeptidases
  • Metalloendopeptidases
  • ECE1 protein, human
  • ECE2 protein, human
  • Endothelin-Converting Enzymes
  • phosphoramidon
Topics
  • Adenocarcinoma
  • Aspartic Acid Endopeptidases (metabolism)
  • Chromatography, High Pressure Liquid
  • Cross Reactions
  • Endothelin-1
  • Endothelin-Converting Enzymes
  • Endothelins (biosynthesis, metabolism)
  • Glycopeptides (pharmacology)
  • Humans
  • Kidney Neoplasms (metabolism)
  • Metalloendopeptidases
  • Protein Precursors (metabolism)
  • Radioimmunoassay
  • Tumor Cells, Cultured

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