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

CD82是Tetraspanin超家族的成员，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(DPP)4是一种结合纤维连接蛋白和小窝蛋白-1的II型跨膜蛋白，提示DPP基因家族的成员作为黏附分子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。将pZeoSV/CD82基因导入h1299细胞，获得CD82基因表达的h1299/CD82细胞株。进行间接免疫荧光染色、免疫印迹分析、实时定量聚合酶链式反应。H1299/CD82细胞DPP9表达降低。小窝蛋白-1在h1299/CD82细胞骨架部分有表达。此外，DPP9的氨基末端区域较弱，其催化区在细胞骨架部分有显著表达。本研究提示CD82诱导DPP9在细胞骨架部分重新定位，并与Caveolin-1共表达与改变细胞黏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.