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The cell-cell adhesion molecule EpCAM interacts directly with the tight junction protein claudin-7.

Abstract：

:We recently described that in the metastasizing rat pancreatic carcinoma line BSp73ASML the cell-cell adhesion molecule EpCAM, CD44 variant isoforms and the tetraspanins D6.1A and CD9 form a complex that is located in glycolipid-enriched membrane microdomains. This complex contains, in addition, an undefined 20 kDa protein. As such complex formation influenced cell-cell adhesion and apoptosis resistance, it became of interest to identify the 20 kDa polypeptide. This 20 kDa protein, which co-precipitated with EpCAM in BSp73ASML lysates, was identified as the tight junction protein claudin-7. Correspondingly, an association between EpCAM and claudin-7 was noted in rat and human tumors and in non-transformed tissues of the gastrointestinal tract. Co-localization of the two molecules was most pronounced at basolateral membranes, but was also observed in tight junctions. Evidence for direct protein-protein interactions between EpCAM and claudin-7 was obtained by co-immunoprecipitation after treatment of tumor cells with a membrane-permeable chemical cross-linker. The complex, which is located in glycolipid-enriched membrane microdomains, is not disrupted by partial cholesterol depletion, but claudin-7 phosphorylation is restricted to the localization in glycolipid-enriched membrane microdomains. This is the first report on an association between EpCAM and claudins in both non-transformed tissues and metastasizing tumor cell lines.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Ladwein M,Pape UF,Schmidt DS,Schnölzer M,Fiedler S,Langbein L,Franke WW,Moldenhauer G,Zöller M

doi

10.1016/j.yexcr.2005.06.013

keywords:

subject

Has Abstract

pub_date

2005-10-01 00:00:00

pages

345-57

issue

2

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(05)00289-2

journal_volume

309

pub_type

杂志文章

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