Comparative proteomic analysis of human adenomyosis using two-dimensional gel electrophoresis and mass spectrometry

ObjectiveTo identify the differently expressed proteins in adenomyotic tissue compared with normal uterine muscle.DesignRetrospective, case-controlled study.SettingUniversity-based Department of Obstetrics and Gynecology and Proteomic Research Center.Patient(s)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.Intervention(s)Postoperative adenomyotic tissue and normal uterine muscle samples were collected.Main Outcome Measure(s)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.Result(s)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.Conclusion(s)Comparative proteomic analysis is a useful approach for the discovery of protein biomarkers for adenomyosis and understanding the pathophysiology of the disease.