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AIM:To identify the differentially secreted proteins orpolypeptides associated with tumorigenesis of esophagealsquamous cell carcinoma(ESCC)from serum and to findpotential tumor secreted biomarkers.METHODS:Proteins from human ESCC tissue and itsmatched adjacent normal tissue;pre-surgery and post-surgery serum;and pre-surgery and normal control serumwere separated by two-dimensional electrophoresis(2-DE)to identify differentially expressed proteins.The silver-stained 2-DE were scanned with digital ImageScanner andanalyzed with ImageMaster 2D Elite 3.10 software.A clusterof protein spots differentially expressed were selected andidentified with matrix-assisted laser desorption/ionizationtime-of-flight mass spectrometry(MALDI-TOF-MS).One ofthe differentially expressed proteins,clusterin,was down-regulated in cancer tissue and pre-surgery serum,but itwas reversed in post-surgery serum.The results wereconfirmed by semi-quantitative reverse-transcription(RT)-PCR and western blot.RESULTS:Comparisons of the protein spots identified onthe 2-DE maps from human matched sera showed that someproteins were differentially expressed,with most of themshowing no differences in composition,shape or density.Being analyzed by MALDI-TOF-MS and database searching,clusterin was differentially expressed and down-regulated in both cancer tissue and pre-surgery serum compared withtheir counterparts.The results were also validated by RT-PCR and western blot.CONCLUSION:The differentially expressed clusterin mayplay a key role during tumorigenesis of ESCC.The 2DE-MSbased proteomic approach is one of the powerful tools fordiscovery of secreted markers from peripheral.
AIM: To identify the differentially secreted proteins or peptide-associated tumors with tumorigenesis of esophageal squamous cell carcinoma (ESCC) from serum and to findpotential tumor secreted biomarkers. METHODS: Proteins from human ESCC tissue and itsmatched adjacent normal tissue; pre-surgery and post-surgery serum; and pre-surgery and normal control serumwere separated by two-dimensional electrophoresis (2-DE) to identify differentially expressed proteins. The silver-stained 2-DE were scanned with digital ImageScanner andalyzed with ImageMaster 2D Elite 3.10 software.A clusterof protein spots differentially expressed were selected andidentified with matrix-assisted laser desorption / ionizationtime-of-flight mass spectrometry (MALDI-TOF-MS). One of the differentially expressed proteins, clusterin, was down-regulated in cancer tissue and pre-surgery serum, in post-surgery serum.The results wereconfirmed by semi-quantitative reverse-transcription (RT) -PCR and western blot.RESULTS: Comp arisons of the protein spots identified on the 2-DE maps from human matched sera showed that someproteins were differentially expressed, with most of themshowing no differences in composition, shape or density.Being analyzed by MALDI-TOF-MS and database searching, clusterin was differentially expressed expressed and down-regulated in both cancer tissue and pre-surgery serums compared with the counterparts.The results were also were validated by RT-PCR and western blot. CONCLUSION: The differentially expressed clusterin may play a key role during tumorigenesis of ESCC. The 2DE-MSbased proteomic approach is one of the powerful tools for discovery of secreted markers from peripheral.