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Ectodomain shedding of the EGF‐receptor ligand epigen is mediated by ADAM17
Author(s) -
Sahin Umut,
Blobel Carl P.
Publication year - 2007
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/j.febslet.2006.11.074
Subject(s) - ectodomain , disintegrin , metalloproteinase , epidermal growth factor receptor , ligand (biochemistry) , microbiology and biotechnology , receptor , chemistry , transmembrane protein , epidermal growth factor , matrix metalloproteinase , biochemistry , biology
All ligands of the epidermal growth factor receptor (EGFR), which has important roles in development and disease, are made as transmembrane precursors. Proteolytic processing by ADAMs (a disintegrin and metalloprotease) regulates the bioavailability of several EGFR‐ligands, yet little is known about the enzyme responsible for processing the recently identified EGFR ligand, epigen. Here we show that ectodomain shedding of epigen requires ADAM17, which can be stimulated by phorbol esters, phosphatase inhibitors and calcium influx. These results suggest that ADAM17 might be a good target to block the release of bioactive epigen, a highly mitogenic ligand of the EGFR which has been implicated in wound healing and cancer.