title: [Suppression of Aurora-A by RNA interference inhibits laryngeal cancer Hep-2 cell growth].
abstract: OBJECTIVE
  To investigate the effects of knockdown of Aurora-A by RNA interference on laryngeal cancer Hep-2 cell growth in vitro and in vivo.
  
  
  METHODS
  A plasmid containing siRNA against Aurora-A was constructed and transfected into human laryngeal cancer cell line Hep-2. Measurements included the CCK-8 assay for viability and proliferation, Transwell assay for invasion, colony formation assay for cell anchorage-independent growth. Western blot and immunohistochemistry assay for protein expression. Tumorigenicity was observed in vivo.
  
  
  RESULTS
  In Hep-2 cells transfected by Aurora-A siRNA (designated as siRNA-3), protein expression of Aurora-A was suppressed by 52%. In CCK-8 assay, absorbance value of siRNA-3 cells (3.268 ± 0.106, (x(-) ± s)) was lower than that of Hep-2 cells (3.722 ± 0.152, F = 17.634, P < 0.001). In Transwell assay, the average invasive cells per field in siRNA-3 cells (110.0 ± 18.0) was less than that in Hep-2 cells (236.0 ± 26.0, F = 26.462, P < 0.01). In colony formation assay, the average colony number of siRNA-3 cells (31.0 ± 6.6) was lower than that of Hep-2 cells (104.0 ± 14.0). The average tumor size in siRNA-3 group was (127.77 ± 174.83) mm(3), which was less than Hep-2 cell group (837.26 ± 101.80) mm(3), (F = 28.187, P < 0.001). Silencing of Aurora-A decreased the expression of focal adhesion kinase (FAK) and matrix metalloproteinase-2 (MMP-2), key regulators in cell adhesion and invasion.
  
  
  CONCLUSIONS
  The knockdown of Aurora-A inhibits the growth and invasiveness of Hep-2 cells in vitro and in vivo, which may be a promising therapeutic strategy for LSCC.
authors.affiliation: Department of Otorhinolaryngology, Ruijin Hospital, School of Medicine, Shanghai Jiaotong University, Shanghai 200025, China.
authors.forename: Hao
authors.initials: H
authors.lastname: Zhang
authors.forename: Xue-hua
authors.initials: XH
authors.lastname: Chen
authors.forename: Chang-ping
authors.initials: CP
authors.lastname: Cai
authors.forename: Shi-li
authors.initials: SL
authors.lastname: Wang
authors.forename: Bing-ya
authors.initials: BY
authors.lastname: Liu
authors.forename: Liang
authors.initials: L
authors.lastname: Zhou
mesh_terms: D000818:Animals; D064096:Aurora Kinase A; D064127:Aurora Kinases; D002294:Carcinoma, Squamous Cell / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D045744:Cell Line, Tumor; D002471:Cell Transformation, Neoplastic; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000378:metabolism; D020868:Gene Silencing; D006801:Humans; D007822:Laryngeal Neoplasms / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism; D051379:Mice; D008819:Mice, Nude; D017346:Protein Serine-Threonine Kinases / Q000235:genetics*; D034622:RNA Interference; D034741:RNA, Small Interfering / Q000235:genetics*; D014162:Transfection
chemical_list: D034741:RNA, Small Interfering; D051416:Focal Adhesion Protein-Tyrosine Kinases; C576918:Aurka protein, mouse; D064096:Aurora Kinase A; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases; D020778:Matrix Metalloproteinase 2