Proteomic analysis of colon cancer

AIM: To investigate the cancer associated proteins and sensitive biomarkers in colon cancer. METHODS: Two-dimensional gel electrophoresis was used to define patterns of protein expression in cancer and matched morphologically normal colonic mucosa from 8 patients. Proteins that showed differential expression of a 2-fold change were cut and analyzed by MALDI-TOF mass spectrometry. RESULTS: Two-dimensional protein maps of cancer and matched normal tissue were gained successfully. Gel-analysis software identified an average of 3289 spots in cancer while 3066 in matched normal tissue and statistical filtering yielded 31 spots of a 2-fold change, 18 of which were identified by using mass spectrometry, including keratin 8, S100A6, protein disulfide isomerase, etc. Functional analysis revealed that these proteins were associated with cancer cellular oncogenesis, proliferation, differentiation and metastasis. CONCLUSION: Proteomic analysis can identify the proteins with variance of colon cancer versus normal colonic tissue as well as providing probable new biomarkers correlated with biological behavior of colon cancer.