Abstract
In order to detect molecular markers for the epidermal growth factor inhibitor 4-(3-chloro-benzyl)- 6,7-dimethoxy-quinazoline (tyrphostin), we investigated the kinetics of p120-catenin and periplakin in the human buccal mucosa squamous cancer cell line BICR 10 treated with 3 nM tyrphostin. Growth of BICR 10 cells was inhibited by treatment with tyrphostin. Although changes were not observed in the expression of EGFR and p120-catenin, expression of Akt, Src and periplakin in BICR 10 treated with 3 nM tyrphostin tended to decrease. In addition, phosphorylation of EGFR, Akt and Src was inhibited by treatment with tyrphostin. On immunocytochemical staining, immunoreactions with phosphorylated EGFR, phosphorylated Akt and phosphorylated p120-catenin were weak in BICR 10 treated with tyrphostin. There was a slight immunocy to chemical reaction to periplakin in BICR 10 cells induced by tyrphostin. In conclusion, the decrease in phosphorylation in EGFR and p120-catenin by tyrphostin, following the decrease in Src or Akt phosphorylation, may inhibit expression of several growth factors associated with the proliferation and migration of cancer cells.
Highlights
Epidermal growth factor receptor (EGFR) is a receptor-type protein for tyrosine kinase [1], and EGFR signalingHow to cite this paper: Tamura, I., et al (2014) Effects of 4-(3-Chloro-Benzyl)-6,7-Dimethoxy-Quinazoline on Kinetics of P120-Catenin and Periplakin in Human Buccal Mucosa Squamous Carcinoma Cell Line
Changes were not observed in the expression of EGFR and p120-catenin, the expression of Akt, Src and periplakin in BICR 10 treated with 3 nM tyrphostin tended to decrease
As epithelial mesenchymal transition (EMT) is determined by the kinetics of adhesion molecules and skeletal proteins, it is likely that investigation into the kinetics of adhesion molecules such as p120-catenin and periplakin in cancer cells treated with tyrphostin are available to diagnosis the pharmacological effects of tyrphostin
Summary
Epidermal growth factor receptor (EGFR) is a receptor-type protein for tyrosine kinase [1], and EGFR signaling. P120-cateninis phosphorylated by the EGF-EGFR complex, and phosphorylation of p120-catenin disrupts adherens junction formation and regulation of E- and P-cadherin stability [11]. This likely requires altered kinetics of phosphorylated p120-catenin. 4-(3-Chloro-benzyl)-6,7-dimethoxy-quinazoline,which is known as tyrphostin 1478 (tyrphostin), is currently being used to inhibit EGFR tyrosine kinase activity and has been tested as an anti-cancer drug in vitro and in preclinical models. It has shown anti-proliferative activity in human cancer cells [16] [17]. We used molecular biological and immunocytochemical techniques to investigate the kinetics of p120-catenin and periplakin in the human buccal mucosa squamous cancer cell line BICR 10 treated with tyrphostin in order to detect the relationship between p120-catenin phosphorylation, expression of periplakin and malignancy in a primary human buccal mucosa squamous cancer cell line
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