Ranking as the fourth commonest
cancer, esophageal squamous cell carcinoma (ESCC) represents one of the leading causes of
cancer death in China. One of the main reasons for the low survival rate is that
neoplasms in esophagus are not detected until they have invaded into surrounding tissues or spread throughout the body at advanced stages. A better understanding of the malignant mechanism and early diagnosis are important for fighting ESCC. In this study, we used proteomics to analyze ESCC tissues, aiming at defining the proteomic features implicated in the multistage progression of esophageal
carcinogenesis.
Proteins that exhibited significantly different expressions were identified by
peptide mass fingerprinting and validated by Western blotting and
reverse transcriptase-polymerase chain reaction. The
protein changes were then correlated to the different grades of disease differentiation. Compared to those in adjacent normal epitheliums, the expression of 15
proteins including
enolase,
elongation factor Tu,
isocitrate dehydrogenase,
tubulin alpha-1 chain,
tubulin beta-5 chain, actin (cytoplasmic 1), glyceraldehyde-3
phosphate dehydrogenase,
tropomyosin isoform 4 (TPM4),
prohibitin,
peroxiredoxin 1 (PRX1),
manganese-containing
superoxide dismutase (MnSOD), neuronal
protein, and
transgelin was up-regulated; and the expression of five
proteins including TPM1,
squamous cell carcinoma antigen 1 (SCCA1), stratifin,
peroxiredoxin 2 isoform a, and alpha B crystalline was down-regulated in
cancer tissues with a statistical significance (p < 0.05). In addition, the differential expression of SCCA1, PRX1, MnSOD, TPM4, and
prohibitin can be observed in precancerous lesions of ESCC. The expression of stratifin,
prohibitin, and SCCA1 dropped with increasing dedifferentiation of ESCC. These data may suggest that these
proteins contribute to the multistage process of
carcinogenesis,
tumor progression, and invasiveness of ESCC.