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

CD82是四跨蛋白超家族的一员，在Caveolin-1存在的情况下通过与细胞表面蛋白结合来调节生物活性。二肽基肽酶（Dipeptidyl peptidase， DPP） 4是一种II型跨膜蛋白，可结合纤维连接蛋白和Caveolin-1，这表明DPP基因家族的成员作为粘附分子并调节细胞骨架的一个组成部分。我们重点研究了CD82对DPP基因家族酶表达的影响。pZeoSV /CD82转染h1299细胞，生成CD82基因转染h1299 （h1299/CD82）。间接免疫荧光染色，免疫印迹分析，实时聚合酶链反应。h1299/CD82细胞DPP9表达降低。Caveolin-1在h1299/CD82细胞骨架部分表达。此外，DPP9的氨基末端区在细胞骨架中表达较少，DPP9的催化结构域在细胞骨架中显著表达。本研究表明，CD82诱导dpp9在细胞骨架部分的重新定位以及与Caveolin-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.