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

CD 82是四跨膜蛋白超家族的成员，在Caveolin-1存在下通过与细胞表面蛋白结合来调节生物活性。二肽基肽酶（DPP）4是一种II型跨膜蛋白，结合纤连蛋白和小窝蛋白-1，表明DPP基因家族的成员作为粘附分子和调节细胞骨架的一个组成部分。我们重点研究了CD 82对DPP基因家族酶表达的影响。通过用pZeoSV /CD 82转染h1299细胞来产生CD 82基因转染的h1299（h1299/CD 82）。采用间接免疫荧光染色、免疫印迹分析、实时定量聚合酶链反应等方法。h1299/CD 82细胞DPP 9表达降低。Caveolin-1表达于h1299/CD 82细胞的细胞骨架部分。此外，DPP 9的氨基末端区域在细胞骨架部分表达较少，而DPP 9的催化结构域在细胞骨架部分表达显著。目前的研究表明，CD 82诱导的细胞骨架组分中的DPP 9重新定位和与小窝蛋白-1的共表达与改变细胞粘附和迁移的机制有关。

CD82 is a member of the tetraspanin superfamily, regulates biological activity by associating with cell surface proteins in the presence of Caveolin-1. Dipeptidyl peptidase (DPP) 4 is a type II transmembrane protein that binds fibronectin and Caveolin-1, suggesting that members of the DPP gene family act as adhesion molecule and modulate a component of the cytoskeleton. We focused on the effect of CD82 on the DPP gene family enzyme expression. CD82 gene transfected h1299 (h1299/CD82) was generated by transfection of h1299 cells with pZeoSV / CD82. Indirect immunofluorescence staining, immunoblot analysis, Real-time polymerase chain reaction have been performed. h1299/CD82 cells decreased DPP9 expression. Caveolin-1 was expressed in cytoskeletal fraction of h1299/CD82 cells. Moreover, the amino terminal region of DPP9 was slightly and the catalytic domain of DPP9 was remarkably expressed in the cytoskeletal fraction. The present study suggests that CD82 induced DPP9-relocalization in the cytoskeletal fraction and co-expression with Caveolin-1 was associated with a mechanism for altering cell adhesion and migration.