S100 calcium-binding protein A6 promotes epithelial-mesenchymal transition through ?-catenin in pancreatic cancer cell line.
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ABSTRACT: The pathogenesis of pancreatic ductal adenocarcinoma (PDAC) remains poorly understood. S100 calcium-binding protein A6 (S100A6) has been associated with PDAC; however, the effect of S100A6 on PDAC migration and invasion has not yet been explored. In this study, Panc-1 cells were transfected with a plasmid to induce overexpression of S100A6, and ?-catenin was knocked down using a specific short hairpin RNA (shRNA). The wound-healing and Transwell assays demonstrated that S100A6 promoted PDAC cell migration and invasion. Furthermore, ?-catenin shRNA inhibited the migration and invasion of PDAC cells. We confirmed that S100A6 induces PDAC cell migration and invasion via activation of ?-catenin in vitro. Assessment of mRNA and protein levels revealed that S100A6 induces increased expression of ?-catenin, N-cadherin and vimentin, and decreased expression of E-cadherin in PDAC cells. ?-catenin shRNA also altered the expression of epithelial-mesenchymal transition (EMT)-related markers in PDAC cells. Specifically, expression of E-cadherin was increased, whereas expression of N-cadherin and vimentin was decreased. Finally, we demonstrated that S100A6 alters the expression of EMT-related markers via ?-catenin activation. In conclusion, S100A6 induces EMT and promotes cell migration and invasion in a ?-catenin-dependent manner. S100A6 may therefore represent a novel potential therapeutic target for the treatment of pancreatic cancer.
SUBMITTER: Chen X
PROVIDER: S-EPMC4370615 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
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