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

有研究认为，转移抑制因子CD82通过与细胞表面受体或蛋白结合来调节生物活性。我们之前报道过，CD82-c-Met复合物通过c-Met适配蛋白使Rho家族的小gtp结合蛋白失活，从而抑制肝细胞生长因子（HGF）诱导的癌细胞迁移。另一方面，β-catenin结合到E-cadherin的细胞质结构域，并通过α-actin将E-cadherin与肌动蛋白细胞骨架连接，形成牢固的细胞间连接。此外，E-cadherin的功能是通过p120结合到E-cadherin的细胞质结构域来调节的。e -钙粘蛋白不仅与细胞粘附有关，而且与细胞迁移的信号传导有关。我们的研究结果表明，CD82调节fe -cadherin-catenin-actin -actin细胞骨架的信号传导，抑制细胞迁移并支持细胞粘附。

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.