RESUMO
BACKGROUND: Thymosin ß4 (Tß4) is a highly conserved actin binding protein associated with the metastatic potential of tumor cells by stimulating cell migration. The role of Tß4 and its derived fragment peptides in migration of ovarian cancer cells has not been studied. OBJECTIVE: To analyze the effects of Tß4 and its derived fragment peptides on ovarian cancer cell migration and invasion, we applied Tß4 and three Tß4-derived synthetic peptides to SKOV3 ovarian cancer cells. METHOD: The migration and invasion of SKOV3 cells treated with Tß4(1-43), Tß4(1-15), Tß4(12-26), Tß4(23-), and untreated control were analyzed by in vitro migration and invasion assay with transwell plate. Cell proliferation assay was conducted to identify the effect of Tß4 and its derived peptide on SKOV3 cell proliferation. The expression of Tß4 related proteins related with cell proliferation was analyzed by Western blot after treatment with Tß4 and its derived peptides. RESULTS: Cell migration and invasion were significantly increased in Tß4 peptide-treated SKOV3 cells compared with untreated control. All three Tß4-derived fragment peptides including those without an actin binding site significantly stimulated migration and invasion of SKOV3 cells. Tß4 and its derived peptide significantly stimulated SKOV3 cell proliferation and up-regulated the expression of RACK-1 protein. CONCLUSIONS: The Tß4 peptide and all of its derived fragment peptides including those without an actin binding motif stimulate migration and invasion of SKOV3 ovarian cancer cells. All peptides significantly increased RACK-1 expression and cell proliferation of SKOV3 cells. These results suggest that Tß4 stimulates migration and invasion of SKOV3 cells by stimulation of cell proliferation through up-regulation of RACK-1 protein.
