Comparative proteomic analysis of esophageal squamous cell carcinoma

• Published in: Proteomics (Weinheim) 2005-07, Vol.5 (11), p.2960-2971
• Main Authors: Qi, Yijun, Chiu, Jen-Fu, Wang, Lidong, Kwong, Dora L. W., He, Qing-Yu
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Blotting, Western; Carcinoma, Squamous Cell - metabolism; Carcinoma, Squamous Cell - pathology; Electrophoresis, Gel, Two-Dimensional; Esophageal cancer; Esophageal Neoplasms - metabolism; Esophageal Neoplasms - pathology; Esophagus; Fundamental and applied biological sciences. Psychology; Gastroenterology. Liver. Pancreas. Abdomen; Gene Expression Regulation, Neoplastic; Humans; Image Processing, Computer-Assisted; Mass Spectrometry; Medical sciences; Miscellaneous; Neoplasm Invasiveness; Neoplasm Proteins - isolation & purification; Neoplasm Proteins - metabolism; Neoplasm Staging; Peptide Mapping; Peroxiredoxin; Protein profiling; Proteins; Reverse Transcriptase Polymerase Chain Reaction; RNA, Neoplasm - isolation & purification; Squamous cell carcinoma antigen 1; Transgelin; Tumor-associated proteins; Tumors; Two-dimensional gel electrophoresis
• ISSN: 1615-9853; 1615-9861
• DOI: 10.1002/pmic.200401175

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