Objectives: Oral cancer is one of the ten most common cancers worldwide with a high morbidity and mortality. It is currently consider that dysregulated cell proliferation and apoptosis leads to the development of cancer. The aim of the present study was to elucidate the biological role of heat shock protein 27 (Hsp27) in oral carcinogenesis. Methods: An oral cancer cell line, OC2, was treated with staurosporine (STS) for 24 h and then subjected to Hotech33258 staining, DNA fragmentation assay, semi-quantitative reverse-transcriptase polymerase chain reaction (RT-PCR) and Western blot analysis for apoptosis. Results: Our data showed that OC2 cells exhibited apoptotic features and fragmentation of DNA after being treated with STS for 24 h. Furthermore, such STS induced apoptosis was through an increased expression of proapoptotic protein Bad and Bax together with a decreased expression of antiapoptotic protein Bcl-2. In addition, STS reduced the heat shock response, leading to decreased levels of Hsp27.Conclusion: Our results suggest that STS specifically suppresses Hsp27 expression in OC2 cells and blocks the inhibitory effects of this molecular chaperone on apoptotic cell death. Taken together, the data present here demonstrated that Hsp27 may participate in the STS-induced sensitization of oral cancer cells to anticancer drugs.

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