title: [Proteomic analysis of proteins related to radiation-induced carcinogenesis].
abstract: 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.
authors.affiliation: Department of Radiomedicine,Second Military Medical University, Shanghai, 200433, PR China.
authors.forename: Jian-Guo
authors.initials: JG
authors.lastname: Cui
authors.forename: Jian-Ming
authors.initials: JM
authors.lastname: Cai
authors.forename: Fu
authors.initials: F
authors.lastname: Gao
authors.forename: Bai-Long
authors.initials: BL
authors.lastname: Li
mesh_terms: D000818:Animals; D014408:Biomarkers, Tumor / Q000378:metabolism; D015153:Blotting, Western; D001980:Bronchi / Q000166:cytology; D002460:Cell Line; D002471:Cell Transformation, Neoplastic / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism* / Q000528:radiation effects*; D005979:Glutathione Peroxidase / Q000378:metabolism; D018398:Homeodomain Proteins / Q000378:metabolism; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D008819:Mice, Nude; D009363:Neoplasm Proteins / Q000378:metabolism*; D009368:Neoplasm Transplantation; D009381:Neoplasms, Radiation-Induced / Q000209:etiology / Q000378:metabolism* / Q000473:pathology; D010751:Phosphopyruvate Hydratase / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D025521:Tumor Suppressor Proteins / Q000378:metabolism; D000094765:Glutathione Peroxidase GPX1; D000097603:Dyrk Kinases
chemical_list: D014408:Biomarkers, Tumor; D004268:DNA-Binding Proteins; D005979:Glutathione Peroxidase; D018398:Homeodomain Proteins; D009363:Neoplasm Proteins; D010751:Phosphopyruvate Hydratase; D017346:Protein Serine-Threonine Kinases; D011505:Protein-Tyrosine Kinases; D025521:Tumor Suppressor Proteins; D000094765:Glutathione Peroxidase GPX1; D000097603:Dyrk Kinases; C082157:PRRX1 protein, human; C095157:ENO1 protein, human