Publication

EpCAM proteolysis: new fragments with distinct functions?

Schnell, U., Kuipers, J. & Giepmans, B. N. G., 1-Apr-2013, In : Bioscience reports. 33, p. 321-332 14 p., e00030.

Research output: Contribution to journalArticleAcademicpeer-review

Copy link to clipboard

Documents

  • EpCAM

    Final publisher's version, 1 MB, PDF-document

DOI

EpCAM [epithelial cell adhesion molecule; CD326 (cluster of differentiation 326)] is highly expressed on epithelium-derived tumours and can play a role in cell proliferation. Recently, RIP (regulated intramembrane proteolysis) has been implicated as the trigger for EpCAM-mediated proliferative signalling. However, RIP does not explain all EpCAM-derived protein fragments. To shed light on how proteolytic cleavage is involved in EpCAM signalling, we characterized the protein biochemically using antibodies binding to three different EpCAM domains. Using a newly generated anti-EpCAM antibody, we find that EpCAM can be cleaved at multiple positions within its ectodomain in addition to described peptides, revealing that EpCAM is processed via distinct proteolytic pathways. Here, we report on four new peptides, but also discuss the previously described cleavage products to provide a comprehensive picture of EpCAM cleavage at multiple positions. The complex regulation of EpCAM might not only result in the absence of full-length EpCAM, but the newly formed EpCAM-derived proteins may have their own signalling properties.

Original languageEnglish
Article numbere00030
Pages (from-to)321-332
Number of pages14
JournalBioscience reports
Volume33
Publication statusPublished - 1-Apr-2013

    Keywords

  • cell-cell contact, EpCAM, notch-like signalling, regulated intramembrane proteolysis, polypeptides, shedding, AMYLOID PRECURSOR PROTEIN, REGULATED INTRAMEMBRANE PROTEOLYSIS, CELL ADHESION MOLECULE, ANTIGEN EP-CAM, LIPID RAFTS, SURFACE-ANTIGEN, CANCER-PATIENTS, EXPRESSION, CLEAVAGE, ECTODOMAIN

View graph of relations

Download statistics

No data available

ID: 5902386