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Kinetics of p120-catenin in a human gingival cancer cell line treated with ZD1839

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Abstract

p120-catenin (p120) is a very critical element in the cadherin/catenin cell-cell adhesion complex. We previously reported that phosphorylated β-catenin disrupts the regulation of E- and P-cadherin stability and adherens junction formation in cancer tissues. In order to study the relationship between p120 phosphorylation and malignancy in a human gingival squamous cancer cell line (BICR78), we investigated the expression of p120 in BICR 78 treated with ZD1839 (Gefitinib), which inhibits epithelial growth factor receptor (EGFR) phosphorylation. BICR78 cells were cultured in Dulbecco's Modified Eagle Medium (DMEM) containing 4μg/mL hydrocortisone and 10% fetal bovine serum. After nearly confluent cells were cultured in serum-free DMEM overnight, they were incubated with 10ng/mL EGF and 1μM ZD1839 for one hour. After cultivation, we performed Western blotting and immunocytochemical analyses to investigate the expression of EGFR, Src, Akt and p120, as well as their phosphorylated forms. We observed a decrease in the number of BrdU-labeled BICR78 cells after treatment with ZD1839. Although the expression of Akt and p120 showed no changes, the phosphorylation of EGFR, Akt and p120 decreased in BICR78 treated with ZD1839. Expression of Src and phosphorylated Src also decreased after treatment with ZD1839. EGFR, p120 and phosphorylated p120 were observed to be distributed on the cellular membrane, while phosphorylated EGFR, both forms of Src and both forms of Akt were localized diffusely in cellular plasma. These results indicate that the inhibition of phosphorylation in EGFR and the downregulation of Src by interception of the Akt-PKB signaling pathway inhibit p120 phosphorylation, thereby controlling the growth of BICR78 cells.

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