title: Aurora-B dysfunction of multinucleated giant cells in glioma detected by site-specific phosphorylated antibodies.
abstract: OBJECTIVE
  The origin of multinucleated giant cells in glioma has not been made clear. In a previous paper the authors studied multinucleated giant tumor cells by using mitosis-specific phosphorylated antibodies to determine the phosphorylation of intermediate filaments and demonstrated that these cells stay in the early mitotic stage, undergoing neither fusion nor degeneration. In the current study the authors investigated the possible genetic causes of multinucleated giant tumor cells.
  
  
  METHODS
  Cultured mono- or multinucleated human glioma cells were immunostained with monoclonal antibodies (mAbs) 4A4, YT33, TM71, HTA28, YG72, and alphaAIM-1. The three former antibodies revealed a particular mitotic cell cycle through site-specific phosphorylation of vimentin; that is, the early phase, mid phase, and late phase, respectively. The three later antibodies demonstrated phosphorylation of H3 at Ser28, phosphorylation of vimentin at Ser72, and aurora-B, respectively, making it possible to identify aurora-B distribution and function during mitosis. In addition, paraffin-embedded tissue sections obtained in three patients with giant cell glioblastoma were also examined. Multinucleated giant tumor cells immunoreacted with the mAb 4A4 and alphaAIM-1 but not with YT33, TM71, HTA28, and YG72 in vitro and in vivo.
  
  
  CONCLUSIONS
  Findings in this study indicated that multinucleated giant tumor cells remain in the early mitotic phase because of aurora-B dysfunction, effecting aberrations in cytoplasmic cleavage without affecting nuclear division.
authors.affiliation: Department of Neurosurgery, Nagoya University Graduate School of Medicine, Japan.
authors.forename: Mitsugu
authors.initials: M
authors.lastname: Fujita
authors.forename: Masaaki
authors.initials: M
authors.lastname: Mizuno
authors.forename: Tetsuro
authors.initials: T
authors.lastname: Nagasaka
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Wakabayashi
authors.forename: Kenkou
authors.initials: K
authors.lastname: Maeda
authors.forename: Dai
authors.initials: D
authors.lastname: Ishii
authors.forename: Toru
authors.initials: T
authors.lastname: Arima
authors.forename: Aie
authors.initials: A
authors.lastname: Kawajiri
authors.forename: Masaki
authors.initials: M
authors.lastname: Inagaki
authors.forename: Jun
authors.initials: J
authors.lastname: Yoshida
mesh_terms: D000911:Antibodies, Monoclonal / Q000378:metabolism; D064107:Aurora Kinase B; D064127:Aurora Kinases; D001932:Brain Neoplasms / Q000378:metabolism* / Q000473:pathology; D045744:Cell Line, Tumor; D005455:Fluorescent Antibody Technique; D015726:Giant Cells / Q000201:enzymology* / Q000473:pathology; D005909:Glioblastoma / Q000378:metabolism* / Q000473:pathology; D006657:Histones / Q000378:metabolism; D006801:Humans; D008938:Mitosis; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000276:immunology / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D014746:Vimentin / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D006657:Histones; D014746:Vimentin; D012694:Serine; C576921:AURKB protein, human; D064107:Aurora Kinase B; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases