Jawhari A U, Farthing M J, Pignatelli M
J Pathol. 1999 Jan;187(2):155-7. doi: 10.1002/(SICI)1096-9896(199901)187:2<155::AID-PATH193>3.0.CO;2-E.
The E-cadherin/catenin complex is a calcium-dependent cell-cell adhesion molecule, whose function is critical to the integrity of the adherens junction and which plays a role in the establishment and maintenance of normal epithelial morphology and differentiation. Loss of E-cadherin-mediated adhesion appears to be a fundamental aspect of the neoplastic phenotype which in some cases appears to be mediated by post-translational modifications (i.e. tyrosine phosphorylation) of its interacting proteins, the catenins which link E-cadherin to the actin cytoskeleton. There is increasing experimental evidence to suggest that epidermal growth factor receptor tyrosine phosphorylation may lead to the inactivation of the E-cadherin/catenin complex in cancer cells through its interaction with beta- or gamma-catenin in the cytoskeleton. Modulation of epidermal growth factor receptor activity by pharmacological agents has the potential to regulate a variety of cellular processes including adhesion, differentiation, and proliferation.
E-钙黏蛋白/连环蛋白复合体是一种依赖钙的细胞间黏附分子，其功能对于黏着连接的完整性至关重要，并且在正常上皮形态的建立和维持以及分化过程中发挥作用。E-钙黏蛋白介导的黏附丧失似乎是肿瘤表型的一个基本方面，在某些情况下，这似乎是由其相互作用蛋白连环蛋白（将E-钙黏蛋白与肌动蛋白细胞骨架相连）的翻译后修饰（即酪氨酸磷酸化）介导的。越来越多的实验证据表明，表皮生长因子受体酪氨酸磷酸化可能通过其与细胞骨架中β-或γ-连环蛋白的相互作用导致癌细胞中E-钙黏蛋白/连环蛋白复合体失活。通过药物制剂调节表皮生长因子受体活性有可能调节包括黏附、分化和增殖在内的多种细胞过程。
