Identification of proteins associated with oral cancer by global proteomic approach.

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Proteomic technologies provide excellent tools for rapid screening of a large number of potential biomarkers in malignant cells. To gain insight into the molecular mechanisms of carcinogenesis and to identify potential biomarkers for oral cancer, we performed proteomic profiling between oral cancer and normal oral mucosa using fluorescent two-dimensional difference in-gel electrophoresis. Proteins with a 【greater than or equal】2-fold change in expression were considered significant. The spots of interest were digested and identified by matrix-assisted laser desorption/ionization time-of-flight peptide mass finger-printing. These results of proteomic analysis were confirmed by Western blotting, immunohistochemical staining, microarray analysis, and real time RT-PCR method.Twenty-two proteins were identified as differentially expressed between oral cancer and normal oral mucosa. Of these, 9 spots were up-regulated and 13 were down-regulated in oral cancer compared to Normal oral mucosa. These spots included the cancer-related proteins ; annexin A1, heat shock protein 27, lamin A/C, interleukin 1 receptor antagonist, serine proteinase inhibitor clade B5, stathmin 1, superoxide dismutase 2. Especially, maspin and stathmin were suggested to be useful biomarkers for oncogenesis.