Yorimitsu K, Shinmi O, Nishiyama M, Moroi K, Sugita Y, Saito T, Inagaki Y, Masaki T, Kimura S
Third Department of Internal Medicine, School of Medicine, Chiba University, Japan.
FEBS Lett. 1992 Dec 21;314(3):395-8. doi: 10.1016/0014-5793(92)81513-l.
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.
