The down-regulation of TAPP2 inhibits the migration of esophageal squamous cell carcinoma and predicts favorable outcome.

Tandem pH domain-containing proteins TAPP1 and TAPP2 are adaptor proteins that specifically bind to phosphatidylinositol-3,4-bisphosphate, or PI(3,4)P2, a product of phosphoinositide 3-kinases (PI3K). Although PI3K enzymes have multiple functions in cell biology, including cell migration, the functions of PI (3, 4) P2 and its binding proteins are not well understood. Previously studies found that TAPP2 is highly expressed in primary leukemic B cells that have strong migratory capacity. However, the function and underlying mechanisms of TAPP2 in ESCC remain largely unknown. In the present study, we investigated the level of TAPP2 in human esophageal squamous cell carcinoma (ESCC) tissues and in corresponding adjacent non-tumor tissues by immunohistochemistry (IHC) and western blot analyses. TAPP2 protein level was increased in ESCC tissues compared with corresponding adjacent non-tumor tissues. In vitro experiments showed that under-expression of TAPP2 reduced ESCC cell TE1 migration by wound-healing assays and transwell migration assays, and it was concurrent with the decreased expression of the phosphorylation of AKT. Taken together, these findings suggested that TAPP2 serves as oncogenic gene in ESCC and may serve as a new target for ESCC therapy.