Downregulation of SENP1 inhibits cell proliferation, migration and promotes apoptosis in human glioma cells

Small ubiquitin-related modifier protein (SUMO) is an evolutionarily conserved protein in a broad range of eukaryotic organisms. De-SUMOylation, the reverse reaction of SUMOylation, is regulated by a family of SUMO-specific proteases (SENPs). SENN is a member of the de-SUMOylation protease family involved in the de-SUMOylation of a variety of SUMOylated proteins. The present study demonstrates that small hairpin RNA (shRNA)-mediated downregulation of SENN inhibits cell proliferation and migration, and promotes apoptosis in human glioma cells. Firstly, LN-299 cells were transfected with a plasmid expressing SENN shRNA (pGenesii-ll-SENP1). The messenger RNA and protein expression of SENN was detected by reverse transcription-quantitative polymerase chain reaction and western blot analysis, respectively. Cell proliferation in vitro was assessed using a methyl thiazolyl tetrazolium assay. Flow cytmnetry (FCM) was used to detect the apoptosis of LN-299 cells. The effect of the downregulation of SENN on cell migration was detected by a Transwell migration system. The present results showed that, compared with the control shRNA group, the expression of SENRI was significantly reduced in the SENP1 shRNA group. The proliferation was markedly inhibited in the SENP1 shRNA group. FCM findings revealed that apoptosis increased significantly in the SENN shRNA group. In addition, it was found that downregulation of SENP1 evidently suppressed tumor cell migration. Downregulation of SENN expression Inhibited the proliferation and migration and promoted apoptosis in 1,N-299 cells. These results indirectly demonstrate that SENN. is likely to play a critical role in human glioma cells.