Processing of proendothelin-1 by members of the subtilisin-like pro-protein convertase family.

@article{Blais2002ProcessingOP,
  title={Processing of proendothelin-1 by members of the subtilisin-like pro-protein convertase family.},
  author={V{\'e}ronique Blais and Martin Fug{\`e}re and Jean-Bernard Denault and Klaus Klarskov and Robert Day and Richard Leduc},
  journal={FEBS letters},
  year={2002},
  volume={524 1-3},
  pages={43-8}
}
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 pairs of basic amino acids. Here, we wished to examine the role of mammalian convertases in this event. Northern blot analysis shows that only furin and PC7 are expressed in ECs. In vitro cleavage of proET-1 by furin or PC7 demonstrated that both enzymes efficiently and specifically process proET-1… CONTINUE READING