Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17. Academic Article uri icon

Overview

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.

publication date

  • December 6, 2006

Research

keywords

  • ADAM Proteins
  • Epidermal Growth Factor
  • ErbB Receptors
  • Fibroblasts
  • Growth Substances
  • Membrane Proteins
  • Protein Precursors

Identity

Scopus Document Identifier

  • 33845729910

Digital Object Identifier (DOI)

  • 10.1016/j.febslet.2006.11.074

PubMed ID

  • 17169360

Additional Document Info

volume

  • 581

issue

  • 1