Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sahin U,Blobel CPdoi
10.1016/j.febslet.2006.11.074subject
Has Abstractpub_date
2007-01-09 00:00:00pages
41-4issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01417-7journal_volume
581pub_type
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