Curcumin (CM), a well-known dietary pigment derived from Curcuma longa L., possess anticancer activities against a variety of tumors including human breast carcinoma. In combination with docetaxel, CM has been used in breast cancer management in the clinic. In order to explore the possible mechanism of anticancer activity of CM, in the present study, we aimed to identify proteins involved in the anticancer activity of CM in human breast cancer cell line MCF-7 using the two-dimensional electrophoresis (2-DE)-based proteomic analysis. MCF-7 cells were cultured at 37°C in an atmosphere of 5.0% CO2. All the following experiments were repeated three times. Cell viability assay showed that after a 48-h incubation CM dose-dependently inhibited cell growth with an IC50 value of 47.42μM. Treatment of CM at 47.42μM for 48h induced apoptosis as determined by nuclear morphologic changes of Hoechst stained cells and flow cytometric analysis of Annexin V-FITC/PI stained cells. Proteomic analysis identified 12 differentially expressed proteins which contributed to multiple functional activities such as DNA transcription, mRNA splicing and translation, amino acid synthesis, protein synthesis, folding and degradation, lipid metabolism, glycolysis, and cell motility. Among them 7 proteins were up-regulated and 5 down-regulated. The up-regulated ones were verified by quantitative real-time PCR. The down-regulated proteins, TDP-43, SF2/ASF and eIF3i, as well as up-regulated ones, 3-PGDH, ERP29, and platelet-activating factor acetylhydrolase IB subunit beta positively contribute to the anticancer activity of CM in MCF-7 cells. These molecules are implicated in the bioactivities of CM for the first time. The findings of this study would shed new insights for systematically understanding the mechanisms of CM in breast cancer intervention.
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