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Processing of proendothelin‐1 by members of the subtilisin‐like pro‐protein convertase family
Author(s) -
Blais Véronique,
Fugère Martin,
Denault Jean-Bernard,
Klarskov Klaus,
Day Robert,
Leduc Richard
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02998-8
Subject(s) - furin , proteolysis , subtilisin , enzyme , western blot , biochemistry , biology , secretion , cleavage (geology) , microbiology and biotechnology , gene , paleontology , fracture (geology)
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.