title: Comparative proteomic analysis of human adenomyosis using two-dimensional gel electrophoresis and mass spectrometry.
abstract: OBJECTIVE
  To identify the differently expressed proteins in adenomyotic tissue compared with normal uterine muscle.
  
  
  METHODS
  Retrospective, case-controlled study.
  
  
  METHODS
  University-based Department of Obstetrics and Gynecology and Proteomic Research Center.
  
  
  METHODS
  Ten patients who underwent transabdominal hysterectomy were included in this study. Five of them were histologically diagnosed with adenomyosis and the other five age-matched patients had cervical carcinoma in situ.
  
  
  METHODS
  Postoperative adenomyotic tissue and normal uterine muscle samples were collected.
  
  
  METHODS
  The protein extracts from paired sample tissue were separated using two-dimensional gel electrophoresis. The differently expressed protein spots were detected by gel comparison using image analysis software and identified using matrix-assisted laser desorption/ionization time of flight mass spectrometry.
  
  
  RESULTS
  Compared with protein profiling of normal uterine muscle, there were 12 protein spots dysregulated in adenomyotic tissue. Among them, 10 protein spots were successfully identified by mass spectrometry.
  
  
  CONCLUSIONS
  Comparative proteomic analysis is a useful approach for the discovery of protein biomarkers for adenomyosis and understanding the pathophysiology of the disease.
authors: Department of Obstetrics and Gynecology, Peking Union Medical College Hospital, Chinese Academy of Medical Science, Beijing, China.
authors: Haiyuan
authors: H
authors: Liu
authors: Jinghe
authors: J
authors: Lang
authors: Xiaorong
authors: X
authors: Wang
authors: Shuzhen
authors: S
authors: Wu
mesh_terms: D000328:Adult; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D004715:Endometriosis / Q000235:genetics*; D005260:Female; D020869:Gene Expression Profiling; D006801:Humans; D008597:Menstrual Cycle; D008875:Middle Aged; D010298:Parity; D010446:Peptide Fragments / Q000302:isolation & purification; D011247:Pregnancy; D011506:Proteins / Q000235:genetics* / Q000302:isolation & purification; D020543:Proteome; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D011506:Proteins; D020543:Proteome; D014357:Trypsin