Liver Cancer

Studies from Fudan University in the area of hepatocellular cancer described

"Heat shock protein 27(HSP27) is confirmed as an apoptosis regulator, but its antiapoptotic mechanism in metastatic hepatocellular carcinoma (HCC) cells remains unclear. Levels of HSP27 protein and its phosphorylation in Hep3B, MHCC97L to MHCC97H cells with different metastatic potentials were determined by western blot analysis. MHCC97H cells were transfected with specific small interference RNA (siRNA) against HSP27. The in vitro migration and invasion potentials of cells were evaluated by Transwell assay. The apoptosis ratio of MHCC97H cells was analyzed by TUNEL staining and Flow Cytometry. Alteration of signal transduction pathway after HSP27 knockdown in MHCC97H cells was evaluated through a Human Q Series Signal Transduction in Cancer Gene Array analysis. Nuclear NF-kappa B contentration and endogenous IKK activity were demonstrated by ELISA assay. The association of IKK alpha, IKK beta, I kappa B alpha with HSP27 and the association between IKK beta and IKK alpha in MHCC97H cells were determined by co-immunoprecipitation assay followed by western blot analysis. HSP27 protein and its phosphorylation increased in parallel with enhanced metastatic potentials of HCC cells. siRNA-mediated HSP27 knockdown in MHCC97H significantly suppressed cells migration and invasion in vitro and induced cell apoptosis; the prominently altered signal transduction pathway was NF-kappa B pathway after HSP27 knockdown in MHCC97H cells. Furthermore, inhibition of HSP27 expression led to a significant decrease of nuclear NF-kappa B contentration and endogenous IKK activity. In addition, HSP27 was associated with IKK alpha, IKK beta, I kappa B alpha in three HCC cells above. ELISA assay and western blot analysis also showed a decrease of the association between IKK beta and IKK alpha, the association between phosphor-HSP27 and IKK complex, and an increase of total I kappa B alpha but reducing tendency of phosphor-I kappa B alpha when HSP27 expression was efficiently knocked down in MHCC97H cells," wrote K. Guo and colleagues, Fudan University.

The researchers concluded: "Altogether, these findings revealed a possible effect of HSP27 on apoptosis in metastatic HCC cells, in which HSP27 may regulate NF-kB pathway activation.."

Guo and colleagues published their study in BMC Cancer (Regulation of HSP27 on NF-kappa B pathway activation may be involved in metastatic hepatocellular carcinoma cells apoptosis. BMC Cancer, 2009;9():100).

For additional information, contact K.Y. Liu, Fudan University, Liver Cancer Institute, Zhongshan Hospital, Shanghai 200032, People's Republic of China.

Publisher contact information for the journal BMC Cancer is: Biomedical Central Ltd., Current Science Group, Middlesex House, 34-42 Cleveland St., London W1T 4LB, England.

Keywords: People's Republic of China, Shanghai, Apoptosis, Biotechnology, Cytometry, Gene Therapy, Hepatocellular Cancer, Hepatocellular Carcinoma, Oncology, Fudan University.

This article was prepared by Clinical Oncology Week editors from staff and other reports. Copyright 2009, Clinical Oncology Week via NewsRx.com.