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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). Seventyone
gene products were identified among these spots.
Members of the heat shock protein 70 and 90 families
were simultaneously up-regulated, whereas metabolismassociated
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 ofHCC carcinogenesis. Molecular & Cellular Proteomics
6:1798–1808, 2007.

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