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American Journal of Pathology, Vol 152, 75-82, Copyright © 1998 by American Society for Investigative Pathology

REGULAR ARTICLES

The expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin

DA Dillon, T D'Aquila, AB Reynolds, ER Fearon and DL Rimm
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.

Several studies have reported loss or alteration of expression of E- cadherin in breast cancer and more recently changes in levels of expression of the catenins. We used immunofluorescence to examine E- cadherin, alpha-catenin, beta-catenin, and p120ctn (formerly p120CAS) expression in 91 cases of invasive ductal carcinoma. As expected, all four proteins co-localize to the junctional regions of the cells. Although nuclear localization has been described for beta-catenin in colonic polyps, no examples were found in these breast cancer cases. We found that, although alteration is common in the catenins and E- cadherin, complete loss, as exemplified by E-cadherin in lobular carcinoma (where E-cadherin is frequently mutated), is rarely seen. In contrast, the catenin-related protein p120ctn shows an expression pattern that is significantly unrelated to the other catenins (or E- cadherin), including complete loss of expression in approximately 10% of the cases. No statistically significant correlations with traditional prognostic indicators were observed with any of these proteins. We conclude 1) that expression of E-cadherin and alpha- and beta-catenin are generally retained at the membrane although frequently reduced or altered, 2) that complete loss of p120ctn expression is seen in approximately 10% of the cases, and 3) that there is a significant correlation in the expression of E-cadherin and the catenins but no correlation between these molecules and p120ctn, suggesting an absence of coordinate regulation.

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