title: Overexpression of myosin is associated with the development of uterine myoma.
abstract: OBJECTIVE
  Myosin is involved in cell contraction and motility, but it is unclear whether it is involved in cell proliferation in uterine myoma. In this study therefore we aimed to explore the role of myosin in uterine myoma.
  
  
  METHODS
  Immunohistochemistry and real-time polymerase chain reaction were used to determine the expression of myosin light chain (MLC), myosin heavy chain (MHC) and myosin light chain kinase (MLCK) in patient uterine myoma and adjacent smooth muscle tissue. Human uterine fibroid cells were isolated and cultured in vitro, myosin heavy chain 11 (MHC subtype expressed in uterine fibroid cells) was knocked down by RNA interference to reduce the expression of myosin, then cell proliferation was determined by the methyl thiazol tetrazolium bromide method. To explore the possible mechanism of reduced cell proliferation after myosin heavy chain 11 knockdown, the downstream proteins collagen I, insulin-like growth factor-1, fibronectin and proteoglycans were analyzed.
  
  
  RESULTS
  Expression of MLC, MHC, MLCK and p-MLCK in uterine myoma cells was significantly higher than in adjacent smooth muscle cells. After knockdown of MHC, smooth muscle cell proliferation decreased, and the production of collagen I, insulin-like growth factor-1 and fibronectin was also reduced, but proteoglycans did not show any significant change.
  
  
  CONCLUSIONS
  Myosin is overexpressed in uterine myoma, and the overexpression of myosin is associated with both uterine contraction and tumor development of uterine myoma.
authors.affiliation: Center for Reproductive Medicine, Provincial Hospital Affiliated to Shandong University, Jinan, China; Department of Obstetrics and Gynecology, Yangpu District Central Hospital, Shanghai, China.
authors.forename: Wenchao
authors.initials: W
authors.lastname: Zhang
authors.forename: Zhongping
authors.initials: Z
authors.lastname: Cheng
authors.forename: Xiaoyan
authors.initials: X
authors.lastname: Qu
authors.forename: Hong
authors.initials: H
authors.lastname: Dai
authors.forename: Xiaoping
authors.initials: X
authors.lastname: Ke
authors.forename: Zijiang
authors.initials: Z
authors.lastname: Chen
mesh_terms: D000328:Adult; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D049109:Cell Proliferation; D002478:Cells, Cultured; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D007889:Leiomyoma / Q000378:metabolism / Q000473:pathology / Q000601:surgery; D018231:Leiomyomatosis / Q000378:metabolism* / Q000473:pathology / Q000601:surgery; D008875:Middle Aged; D018995:Myosin Heavy Chains / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D018994:Myosin Light Chains / Q000235:genetics / Q000378:metabolism*; D009219:Myosin-Light-Chain Kinase / Q000235:genetics / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D034622:RNA Interference; D014407:Tumor Cells, Cultured; D015854:Up-Regulation; D014594:Uterine Neoplasms / Q000378:metabolism* / Q000473:pathology; D014599:Uterus / Q000378:metabolism* / Q000473:pathology / Q000601:surgery
chemical_list: D002135:Calcium-Binding Proteins; C509903:MYH11 protein, human; D018994:Myosin Light Chains; D009363:Neoplasm Proteins; C499378:MYLK protein, human; D009219:Myosin-Light-Chain Kinase; D018995:Myosin Heavy Chains
keywords: contraction; myosin heavy chain; myosin light chain; myosin light chain kinase; uterine myoma