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

APA

Schnell, U., Kuipers, J., & Giepmans, B. N. G. (2013). EpCAM proteolysis: new fragments with distinct functions? Bioscience reports, 33, 321-332. [e00030]. https://doi.org/10.1042/BSR20120128

Author

Schnell, Ulrike ; Kuipers, Jeroen ; Giepmans, Ben N. G. / EpCAM proteolysis : new fragments with distinct functions?. In: Bioscience reports. 2013 ; Vol. 33. pp. 321-332.

Harvard

Schnell, U, Kuipers, J & Giepmans, BNG 2013, 'EpCAM proteolysis: new fragments with distinct functions?', Bioscience reports, vol. 33, e00030, pp. 321-332. https://doi.org/10.1042/BSR20120128

Standard

EpCAM proteolysis : new fragments with distinct functions? / Schnell, Ulrike; Kuipers, Jeroen; Giepmans, Ben N. G.

In: Bioscience reports, Vol. 33, e00030, 01.04.2013, p. 321-332.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Schnell U, Kuipers J, Giepmans BNG. EpCAM proteolysis: new fragments with distinct functions? Bioscience reports. 2013 Apr 1;33:321-332. e00030. https://doi.org/10.1042/BSR20120128


BibTeX

@article{ef552c7acc024cb480220b4e378378c5,
title = "EpCAM proteolysis: new fragments with distinct functions?",
abstract = "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.",
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",
author = "Ulrike Schnell and Jeroen Kuipers and Giepmans, {Ben N. G.}",
year = "2013",
month = "4",
day = "1",
doi = "10.1042/BSR20120128",
language = "English",
volume = "33",
pages = "321--332",
journal = "Bioscience reports",
issn = "0144-8463",

}

RIS

TY - JOUR

T1 - EpCAM proteolysis

T2 - new fragments with distinct functions?

AU - Schnell, Ulrike

AU - Kuipers, Jeroen

AU - Giepmans, Ben N. G.

PY - 2013/4/1

Y1 - 2013/4/1

N2 - 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.

AB - 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.

KW - cell-cell contact

KW - EpCAM

KW - notch-like signalling

KW - regulated intramembrane proteolysis

KW - polypeptides

KW - shedding

KW - AMYLOID PRECURSOR PROTEIN

KW - REGULATED INTRAMEMBRANE PROTEOLYSIS

KW - CELL ADHESION MOLECULE

KW - ANTIGEN EP-CAM

KW - LIPID RAFTS

KW - SURFACE-ANTIGEN

KW - CANCER-PATIENTS

KW - EXPRESSION

KW - CLEAVAGE

KW - ECTODOMAIN

U2 - 10.1042/BSR20120128

DO - 10.1042/BSR20120128

M3 - Article

VL - 33

SP - 321

EP - 332

JO - Bioscience reports

JF - Bioscience reports

SN - 0144-8463

M1 - e00030

ER -

ID: 5902386