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Review
. 2007 Feb 12;96(3):417-23.
doi: 10.1038/sj.bjc.6603494. Epub 2007 Jan 9.

EpCAM (CD326) finding its role in cancer

P A Baeuerle  1 , O Gires
Affiliations
Review

EpCAM (CD326) finding its role in cancer

P A Baeuerle et al. Br J Cancer. .

Erratum in

  • Br J Cancer. 2007 May 7;96(9):1491

Abstract

Although epithelial cell adhesion/activating molecule (EpCAM/CD326) is one of the first tumour-associated antigens identified, it has never received the same level of attention as other target proteins for therapy of cancer. It is also striking that ever since its discovery in the late 1970s the actual contribution of EpCAM to carcinogenesis remained unexplored until very recently. With a First International Symposium on EpCAM Biology and Clinical Application this is now changing. Key topics discussed at the meeting were the frequency and level of EpCAM expression on various cancers and its prognostic potential, the role of EpCAM as an oncogenic signalling molecule for cancer cells, recent progress on EpCAM-directed immunotherapeutic approaches in clinical development and the interaction of EpCAM with other proteins, which may provide a basis for a therapeutic window and repression of its growth-promoting signalling in carcinoma. Future research on EpCAM may benefit from a unified nomenclature and more frequent exchange among those who have been working on this cancer target during the past 30 years and will do so in the future.

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Figures

Figure 1
Figure 1
Revised structural model of EpCAM. (A) Sequence homology between the second EGF-like domain of EpCAM and a repeat from human thyroglobulin (TY). EpCAM is shown with N- (N) and C-terminus (C), signal peptide (SP), transmembrane domain (TM), N-linked carbohydrates (CHO), EGF-like domain (EGF) and TY repeat domain (TY). Sequence identity (red amino acid residues) between EpCAM and a selected TY repeat is 54%. Conserved exchanges are shown in blue. The cognate motif of all TY domains, QCNxCWCV, is highlighted by pink boxes. (B) Old (left) and revised domain model of EpCAM (right). EpCAM is depicted as a tetramer showing three additional subunits with dotted lines. Structural analysis of many TY domains from different proteins has shown that N- and C-termini are in close proximity. This is why the polypeptide chain is depicted with a bent within the TY domain that would orient the EGF-like domain towards the cell membrane. Cleavage sites for two proteases releasing the intracellular portion of EpCAM are indicated by red arrows, and the domain of EpCAM interacting with the listed proteins is shown by a bracket.
See this image and copyright information in PMC

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