Proteomic analysis of cervical cancer cells treated with suberonylanilide hydroxamic acid.

Suberonylanilide hydroxamic acid (SAHA)is an orally administered histone deacetylase inhibitor (HDACI) that has shown significant antitumour activity in a variety of tumour cells.To identify proteins involved in its antitumour activity,we utilized a proteomic approach to reveal protein expression changes in the human cervical cancer cell line HeLa following SAHA treatment.Protein expression profiles were analysed by 2-dimensional polyacrylamide gel electrophoresis (2-DE) and protein identification was performed on a MALDI-Q-TOF MS/MS instrument.As a result,a total of nine differentially expressed proteins were visualized by 2-DE and Coomassie brilliant blue (CBB) staining.Further,all the changed proteins were positively identified via mass spectrometry (MS)/MS analysis. Of these,PGAM1 was significantly downregulated in HeLa cells after treatment with SAHA. Moreover,PGAM1 has been proven to be downregulated in another cervical cancer cell line (CaSki) by western blot analysis.Together,using proteomic tools,we identified several differentially expressed proteins that underwent SAHA-induced apoptosis. These changed proteins may provide some clues to a better understanding of the molecular mechanisms underlying SAHA-induced apoptosis in cervical cancer.