Positive expression of E-cadherin suppresses cell adhesion to fibronectin via reduction of alpha5beta1 integrin in human breast carcinoma cells.

Abstract:

:E-cadherin mainly mediated the epithelial cell-cell adhesion, and integrin signaling can modulate the signaling pathway of E-cadherin in the different levels. Up to now, however, it is still unclear that whether E-cadherin could interfere with cell-matrix interaction, a typical adhesion through integrins. In this study we investigated the effects of E-cadherin on cell-matrix adhesion and alpha5beta1 integrin expression in human breast carcinoma cells. It was found that either mRNA or protein level of alpha5 and beta1 subunits of integrin decreased in E-cad-231 compared with Mock-231. Furthermore, the promoter activity of alpha5 gene was inhibited in E-cad-231 compared with Mock-231. Consistently, phosphorylated focal adhesion kinase, a closer key downstream protein kinase of integrin signaling, were also down-regulated in E-cad-231. Furthermore, distribution of beta-catenin was observed and data showed beta-catenin was accumulated in the nucleus in Mock-231, while disappeared from the nucleus and mainly accumulated near the cell surface membrane in E-cad-231. LiCl, a molecule that can inhibit the GSK-3beta activity and down-regulate beta-catenin degradation, could inversely stimulate expression of alpha5 and beta1 integrin. Taken together, these results indicated that positive expression of E-cadherin inhibits the cell adhesion to extracellular matrix mediated by alpha5beta1 integrin signaling.

authors

Wu H,Liang YL,Li Z,Jin J,Zhang W,Duan L,Zha X

doi

10.1007/s00432-006-0128-2

subject

Has Abstract

pub_date

2006-12-01 00:00:00

pages

795-803

issue

12

eissn

0171-5216

issn

1432-1335

journal_volume

132

pub_type

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