Abstract:

Objective
 To explore the mechanism of ginsenoside-Rh2(G-Rh2) on inhibition of glioma by identifying differential proteins with proteomic technique. Methods   The total proteins were extracted from SHG-44 cells treated with 32 μmol?L-1 G-Rh2 for 72 h and the cells in control group,then were subjected to two-dimensional gel electrophoresis.Only spots with a fold change equal or above 1.5 and P<0.05 were selected  as differential proteins.Afterwards the differential proteins were analyzed by the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) for peptide mass fingerprint (PMF) identification. 
Results  Compared with those of control group,20 differential protein spots were identified by the two-dimensional electrophoresis in SHG-44 cells treated with G-Rh2,including 16 down-regulated ones and 4 up-regulated ones.Five remarkably down-regulated proteins analyzed by mass spectrometry were cofilin 1,phosphoglycerate kinase (PGK),peroxiredoxin 1 (Prx 1),heat shock proteins (HSP) and proliferation cell nuclear antigen (PCNA). Conclusion  These differential proteins may be involved in the proliferation inhibition of human glioma cells by G-Rh2.

Key words: panaxosides;glioma;proteomics