Abstract. Cantharidin (CTD), a component of natural mylabris (Mylabris phalerata Pallas), has been shown to have biological activities and induce cell death in many human
and the results indicated that CTD inhibited the enzymatic activities of MMP-2/-9 of NCI-H460 cells. Western blotting was used to examine the protein expression of NCI-H460 cells after incubation with CTD and the results showed that CTD decreased the expression of MMP-2/-9, focal adhesion kinase (FAK), Ras homolog gene family, member A (Rho A), phospho-protein kinase B (AKT) (Thr308)(p-AKT(308)), phospho-extracellular signal-regulated kinase1/2 (p-ERK1/2), phospho-p38 mitogen-activated protein (MAP) kinase (p-p38), phospho c-Jun N-terminal kinase 1/2 (p-JNK1/2), nuclear factor-ĸB (NF-ĸB) and urokinase plasminogen activator (UPA). Furthermore, confocal laser microscopy was used to confirm that CTD suppressed the expression of NF-ĸB p65, but did not significantly affect protein kinase C (PKC) translocation in NCI-H460 cells. Based on those observations, we suggest that CTD may be used as a novel anticancer metastasis agent for lung cancer in the future.Lung cancer is the most common cancer among women and men in Taiwan and it is the major cause of death in cancerrelated diseases in the developed world. Neoplastic metastasis is a major cause of cancer-mediated death in humans (1, 2). For tumor metastasis, epithelial cancer cells have to migrate from the original primary tumor mass via breaking their cellcell contacts (adherens junctions) to form cancer mass in a new site (3, 4); thus, tumor metastasis involves cell attachment (adhension), migration and invasion in order to form a new tumor in another site of the body. Inhibiting cancer cell metastasis is one of the important steps for cancer therapy and research (5). Numerous evidence have shown that multiple factors involved in tumor metastasis, such as the activation of PI3K/Akt pathway (6), matrix metalloproteinases (MMPs)-enzymes that can degrade the extracellular matrix and 5989