Key result
In vitro cleavage of proendothelin-1 by furin or PC7 demonstrated that both enzymes efficiently and specifically process proET-1, suggesting they participate in its maturation in endothelial cells.
Why the study?
The role of mammalian subtilisin-like pro-protein convertases in processing proendothelin-1 in endothelial cells was unclear.
Furin and PC7 are expressed in endothelial cells and can efficiently process proendothelin-1, suggesting their role in its maturation.
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. These data reveal that furin and PC7 have similar specificities towards proET-1 and suggest that both enzymes may participate in the maturation of proET-1 in ECs.
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Blais et al. (2002) studied this question. Furin and PC7 was evaluated on Cleavage of proET-1. In vitro cleavage of proendothelin-1 by furin or PC7 demonstrated that both enzymes efficiently and specifically process proET-1, suggesting they participate in its maturation in endothelial cells.
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