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Proteomic analysis of differential protein expression in a human hepatoma revertant cell line by using an improved two‐dimensional electrophoresis procedure combined with matrix assisted laser desorption/ionization‐time of flight‐mass spectrometry
Author(s) -
Yuan Quan,
An Jie,
Liu Dinggan,
Sun Li,
Ge Yingzi,
Huang Yingling,
Xu Genjun,
Zhao Fukun
Publication year - 2004
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200305769
Subject(s) - gel electrophoresis , microbiology and biotechnology , cell culture , chemistry , reversion , mass spectrometry , proteomics , electrophoresis , sodium dodecyl sulfate , matrix assisted laser desorption/ionization , phenotype , chromatography , biology , biochemistry , desorption , gene , genetics , organic chemistry , adsorption
The proteomic profiles of a human hepatoma revertant, CL1, and its original cell line, SMMC7721, were compared by using an improved two‐dimensional electrophoresis (2‐DE) procedure, with multi‐IPGstrips gels (length ≤ 13 cm) run simultaneously on one sodium dodecyl sulfate (SDS) gel (shortened MSOG method). Nineteen proteins, showing significant difference in expression ( P < 0.01), were selected and identified by matrix assisted laser desorption/ionization‐time of flight‐mass spectrometry (MALDI‐TOF‐MS) and database search. In the revertant CL1 cells, compared to human hepatoma SMMC7721 cells, upregulated expression levels of some proteins related to tumor suppression, like maspin, were found, whereas some proteins related to tumor growth, like cathepsin D, were downregulated. These facts suggest that the phenotypic reversion of the CL1 cells was at least partially due to changes at the translational level of the proteins which favored the reconstruction of the normal phenotype of the cell.