[Comparative proteomics analysis of human adenomyosis].

OBJECTIVE: To set up the proteomic protein profiling of adenomyotic tissue and normal uterine muscle and identify the abnormally expressed proteins in adenomyotic tissue. METHODS: Samples of adenomyotic tissue (adenomyosis group) and age-matched healthy uterine muscle (control group) were collected from totally 10 patients undergoing transabdominal hysterectomy for adenomyosis and cervical diseases at Peking Union Medical College Hospital from January 2007 to October 2007. The proteomics profiling of adenomyotic tissue and normal uterine tissue were established using two dimensional gel electrophoresis (2-DE) and gel staining method. 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 (MALDI-TOF-MS). RESULTS: In Coomassie blue stained gels there were on average (512 +/- 36) spots and compared with the reference gel the matching rate was 83.7%. In silver stained gels there were (762 +/- 54) spots and compared with the reference gel the matching rate was 81.1%. Compared with normal uterine muscle, there were 15 protein spots disregulated in adenomyotic tissue. Among them 10 protein spots were successfully identified by mass spectrometry. The functions of these disregulated proteins included cell skeleton, oxidation, apoptosis and immune reaction. CONCLUSIONS: Comparative proteomics analysis is a useful approach for the study of adenomyosis. Compared with normal uterine muscle there are abnormalities in cell skeleton, oxidation, apoptosis and immune reaction. These life processes may participate in pathophysiology of adenomyosis.