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(American Journal of Pathology. 1998;153:1521-1530.)
© 1998 American Society for Investigative Pathology

Regular Articles

Cytoplasmic Redistribution of E-Cadherin-Catenin Adhesion Complex Is Associated with Down-Regulated Tyrosine Phosphorylation of E-Cadherin in Human Bronchopulmonary Carcinomas

Béatrice Nawrocki* , Myriam Polette* , Jolanda Van Hengel , Jean-Marie Tournier* , Frans Van Roy and Philippe Birembaut*

From INSERM U.314,* IFR 53, Unité de Biologie Cellulaire, Laboratoire Pol Bouin, CHU, Reims, France; and the Department of Molecular Biology, Molecular Cell Biology Unit, VIB-University of Ghent, Ghent, Belgium

The E-cadherin-catenin complex, by mediating intercellular adhesion, regulates the architectural integrity of epithelia. Down-regulation of its expression is thought to contribute to invasion of carcinoma cells. To investigate the involvement of the E-cadherin-catenin adhesion system in the progression of human bronchopulmonary carcinomas, we compared the immunohistochemical distribution of E-cadherin, -catenin, and ß-catenin in four human bronchial cancer cell lines with different invasive abilities and in 44 primary bronchopulmonary tumors. Although invasive bronchial cell lines did not express E-cadherin and -catenin, complete down-regulation of cadherin-catenin complex expression was a rare event in vivo in bronchopulmonary carcinomas. Nevertheless, a spotty and cytoplasmic pattern of E-cadherin and catenins was observed in 32 primary tumors, only in invasive tumor clusters. Immunoprecipitation experiments showed that this redistribution was not related to a disruption of cadherin-catenin interaction but to down-regulated tyrosine phosphorylation of E-cadherin. We conclude that loss of E-cadherin and/or catenins is not a prominent early event in the invasive progression of human bronchopulmonary carcinomas in vivo. The decreased tyrosine phosphorylation of E-cadherin may reflect a loss of functionality of the complex and implicates a major role in tumor invasion.

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