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Submitted on September 7, 2001
Revised on October 23, 2001
Accepted on October 22, 2001

2-D differential in-Gel electrophoresis for the identification of human esophageal squamous cell cancer specific protein markers

Ge Zhou, Hongmei Li, Dianne DeCamp, She Chen, Hongjun Shu, Yi Gong, Michael Flag, John Gillespie, Nan Hu, Philip Taylor, Michaeal Emmert Buck, Lance A. Liotta, Emanuel C. Petricoin III, and Yingming Zhao

Laboratory of Pathology, National Cancer Institute, Bethesda, MD 20892

Corresponding Author: lance{at}helix.nih.gov

The reproducibility of conventional 2D-gel electrophoresis can be improved using Differential In-gel Electrophoresis (DIGE), a new emerging technology for proteomic analysis. In DIGE, two pools of proteins are labeled with Cy3 and Cy5 fluorescent dyes, respectively. The labeled proteins are mixed and separated in the same 2D-gel. 2D DIGE was applied to quantify the differences in protein expression between laser-capture-microdissection (LCM) procured esophageal carcinoma cells and normal epithelial cells, and to define cancer-specific and normal- specific protein markers. Analysis of the 2D images from protein lysates of ~ 250,000 cancer cells and normal cells identified 1038 protein spots in cancer cell lysates and 1088 protein spots in normal cell lysates. Of the detected proteins, 58 spots were up-regulated by > 3 fold and 107 down-regulated by > 3 fold in cancer cells. In addition to previously identified down-regulated protein annexin I, tumor rejection antigen (gp96) was found up-regulated in esophageal squamous cell cancer. Global quantification of protein expression between laser capture microdissected patient-matched cancer cells and normal cells using 2D DIGE in combination with mass spectrometry is a powerful tool for the molecular characterization of cancer progression and identification of cancer-specific protein markers.


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