Antcin-H Isolated from Antrodia cinnamomea Inhibits Renal Cancer Cell Invasion Partly through Inactivation of FAK-ERK-C/EBP-β/c-Fos-MMP-7 Pathways

Figure 2

Inhibition of cell migration and modulation of migration-related proteins by antcin-H in vitro. (a) 786-0 cells were treated without or with 20, 50, 100, and 200 M antcin-H for 24 h, and then cells were seeded in the upper part of Transwell. After 16 h, cells on the bottom side of the filter were microphotographed and counted. Data were represented as the mean ± SD of three independent experiments. Statistically significant, . Scale bar, 100 m. (b) Regulation of FAK, paxillin, E-cadherin, and vimentin by antcin-H. 786-0 cells were treated without or with 20, 50, and 100 M antcin-H for 24 h, and then protein lysates were isolated. The levels of phosphorylated-FAK, phosphorylated-paxillin, E-cadherin, and vimentin were examined by Western blot analysis. -Actin was used as an internal loading control. Confocal imaging of (c) phosphorylated-FAK and (d) phosphorylated-paxillin. 786-0 cells were treated without or with 100 M antcin-H for 24 h. The cellular distribution of phosphorylated-FAK and phosphorylated-paxillin was examined by immunofluorescence staining using phosphorylated-FAK and phosphorylated-paxillin specific antibodies. The immunoreactive images were investigated by confocal microscope. Scale bar, 20 m.

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