The analysis and clinical applications of cellular adhesion controlmechanisms by a metastasis suppressor CD82 in an oral cancer

已经提出转移抑制因子CD 82通过与细胞表面受体或蛋白质结合来调节生物活性。我们先前报道了CD 82-c-Met复合物通过c-Met衔接蛋白灭活Rho家族的小GTP结合蛋白来抑制肝细胞生长因子（HGF）诱导的癌细胞迁移。另一方面，β-catenin与E-cadherin的胞浆区结合，并通过α-actinin将E-cadherin连接到肌动蛋白细胞骨架上，形成牢固的细胞间连接。另外，E-cadherin的功能是通过p120与其胞质结构域的结合来调节的，E-cadherin不仅参与细胞粘附，还参与细胞迁移的信号转导。我们的研究结果表明，CD 82调节E-cadherin-catenin-actinin-actin细胞骨架的信号传导，并通过支持细胞粘附抑制细胞迁移。

It has been proposed that the metastasis suppressor CD82 regulates biological activity by associating with cell surface receptors or proteins. We reported previously that the CD82-c-Met complex inhibits hepatocyte growth factor (HGF)-induced cancer cell migration by the inactivation of small GTP-binding proteinsof the Rho family via c-Met adapter proteins. On the other hand, β-catenin binds tothe cytoplasmic domain of E-cadherin and links E-cadherin to the actin cytoskeleton through α-actinin, forming strong intercellular junction. In addition, the function of E-cadherin is regulated by binding p120 to the cytoplasmic domain of E-cadherin.E-cadherin has been implicated not only in cell adhesion but also in the signaling of cell migration. Our results suggested that CD82 regulated the signaling ofE-cadherin-catenin-actinin-actin cell cytoskeleton and inhibited cell migration withsupporting cell adhesion.