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.
|
Authors | K Yorimitsu, O Shinmi, M Nishiyama, K Moroi, Y Sugita, T Saito, Y Inagaki, T Masaki, S Kimura |
Journal | FEBS letters
(FEBS Lett)
Vol. 314
Issue 3
Pg. 395-8
(Dec 21 1992)
ISSN: 0014-5793 [Print] England |
PMID | 1468574
(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
|