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Molecular & Cellular Proteomics 6:1798-1808, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proteome Analysis of Hepatocellular Carcinoma by Two-dimensional Difference Gel Electrophoresis

Novel Protein Markers in Hepatocellular Carcinoma Tissues^*,S

Wei Sun^,¶, Baocai Xing^¶,||, Yi Sun^||, Xiaojuan Du^**, Min Lu, Chunyi Hao^||, Zhuang Lu, Wei Mi, Songfeng Wu, Handong Wei, Xue Gao, Yunping Zhu, Ying Jiang, Xiaohong Qian and Fuchu He^,,¶¶

From the State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing 102206, P.R. China, ^|| Beijing Cancer Hospital, Beijing 100036, China, Departments of ^** Cell Biology and Pathology, Peking University Health Science Center, Beijing 100083, China, and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China

Hepatocellular carcinoma (HCC) is a highly malignant tumor, and chronic infection with hepatitis B virus is one of its major risk factors. To identify the proteins involved in HCC carcinogenesis, we used two-dimensional fluorescence DIGE to study the differentially expressed proteins in tumor and adjacent nontumor tissue samples. Samples from 12 hepatitis B virus-associated HCC patients were analyzed. A total of 61 spots were significantly up-regulated (ratio 2, p 0.01) in tumor samples, whereas 158 spots were down-regulated (ratio –2, p 0.01). Seventy-one gene products were identified among these spots. Members of the heat shock protein 70 and 90 families were simultaneously up-regulated, whereas metabolism-associated proteins were decreased in HCC samples. The down-regulation of mitochondrial and peroxisomal proteins in these results suggested loss of special organelle functions during HCC carcinogenesis. Four metabolic enzymes involved in the methylation cycle in the liver were down-regulated in HCC tissues, indicating S-adenosylmethionine deficiency in HCC. Two gene products, glyceraldehyde-3-phosphate dehydrogenase and formimidoyltransferase-cyclodeaminase, were identified from inversely altered spots, suggesting that different isoforms or post-translational modifications of these two proteins might play different roles in HCC. For the first time, the overexpression of Hcp70/Hsp90-organizing protein and heterogeneous nuclear ribonucleoproteins C1/C2 in HCC tissues was confirmed by Western blot and then by immunohistochemistry staining in 70 HCC samples, suggesting their potential as protein tumor markers. In summary, we profiled proteome alterations in HCC tissues, and these results may provide useful insights for understanding the mechanism involved in the process of HCC carcinogenesis.

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