Processing of proendothelin‐1 by members of the subtilisin‐like pro‐protein convertase family
Open Access
- 29 June 2002
- journal article
- Published by Wiley in FEBS Letters
- Vol. 524 (1-3) , 43-48
- https://doi.org/10.1016/s0014-5793(02)02998-8
Abstract
Endothelial cells (ECs) secrete numerous bioactive peptides that are initially synthesized as inactive precursor proteins. One of these, proendothelin‐1 (proET‐1), undergoes proteolysis at specific p...Keywords
This publication has 18 references indexed in Scilit:
- Inhibitory Potency and Specificity of Subtilase-like Pro-protein Convertase (SPC) ProdomainsJournal of Biological Chemistry, 2002
- Comparative Characterization of Two Forms of Recombinant Human SPC1 Secreted from Schneider 2 CellsProtein Expression and Purification, 2000
- Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides1Published on the World Wide Web on 17 August 1999.1Brain Research, 1999
- The proprotein convertasesCurrent Opinion in Chemical Biology, 1998
- Processing of Proendothelin‐1 at the C‐Terminus of Big Endothelin‐1 is Essential for Proteolysis by Endothelin‐Converting Enzyme‐1 in vivoEuropean Journal of Biochemistry, 1997
- Processing of proendothelin‐1 by human furin convertaseFEBS Letters, 1995
- The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substratesCell and tissue research, 1995
- ErratumBiochemical and Biophysical Research Communications, 1994
- ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1Published by Elsevier ,1994
- The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functionsBiochimie, 1994