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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
Published on: August 19, 2025
[Proteomic analysis of proteins related to radiation-induced carcinogenesis]
Jian-Guo Cui1, Jian-Ming Cai, Fu Gao
1Department of Radiomedicine,Second Military Medical University, Shanghai, 200433, PR China.
Background & Objective:
Carcinogenesis is the most serious late effect of radiation, but the mechanism of radiation-induced carcinogenesis remains unknown. This study was to compare the protein expression profiles between radiation-induced cancer cells and normal cells.
Methods:
Immortalized human bronchia epithelial cell line BEAS-2B was irradiated by gamma-ray to prepare malignant BR22P50 cells. Protein profiles of BR22P50 cells and normal cell line BNP50 were detected by two-dimensional (2D) electrophoresis. The differentially expressed proteins were identified by mass spectrometry. The protein levels of ENO1, Prx I, Dyrk2, and GPX1 in different phases of radiation-induced carcinogenesis were detected by Western blot.
Results:
A total of 59 proteins were differentially expressed between BR22 P50 and BNP50 cells. Of the 59 proteins, 14 were only expressed in BR22P50 cells, 15 were only expressed in BNP50, 7 were overexpressed and 23 were lowly expressed in BR22P50 cells. Using MALDI-TOF MS technology, 26 proteins were identified, including enzymes, structure proteins, cell signal proteins, binding proteins, metabolism-related proteins, some unknown functional proteins, and poly-peptides. The expression of ENO1 and Prx I was up-regulated and that of Dyrk2 and GPX1 was down-regulated with the advancement of radiation-induced carcinogenesis.
Conclusions:
The proteins related to radiation-induced carcinogenesis are identified by 2D electrophoresis. This study may provide a novel clue to probe the mechanism of radiation-induced carcinogenesis.

