Masa‐Aki Okubo

Hiroshima University, Hirosima, Hiroshima, Japan

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Publications (2)5.64 Total impact

  • Tadao Takahashi · Masa‐Aki Okubo · Hiroshi Hosoya
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    ABSTRACT: We observed the cell surface of Paramecium trichium using three different methods. A non-dividing paramecium's cell surface consisted of three major regions outside of the oral apparatus: a) an oral groove region, with 2-cilia-2-basal-body (2C-2BB) units; b) a posterior region, occupying 1/4 to 1/5 of the cell surface, with 1-cilium-l-basal-body (1C-1BB) units; c) the remainder, with l-cilium-2-basal-body (1C-2BB) units. Five kinds of region-specific cortical reorganization occurred prior to cytokinesis: the 2C-2BB and 1C-1BB units were not duplicated, while the 1C-2BB units were reorganized to 2C-2BB, 1C-2BB or 1C-1BB units. These reorganizations of the cell surface progressed from the fission line to the anterior in the prospective anterior daughter cell, and to the posterior in the prospective posterior daughter cell, and bilaterally from the old and also newly developing oral apparatus in both daughter cells. In contrast, the development of cilia and their associated structures in each of the cortical units always progressed from posterior to anterior. The present work also showed that two fission lines began to develop bilaterally from the oral primordium, and then they joined to become a single fission line at the dorsal surface.
    No preview · Article · May 2007 · Journal of Eukaryotic Microbiology
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    ABSTRACT: Hybridoma cell lines were prepared from spleen cells of mouse immunized with mitotic HeLa cells. A monoclonal antibody (mH1), which intensively reacted with cleavage furrows of dividing HeLa cells in immunofluorescence, was obtained. In interphase, this antibody diffusely stained whole HeLa cells. Immunoelectron microscopy showed that mH1 antigens were localized at microvillus projections at the surface of dividing HeLa cells, but definite localization of that antigen was not observed in interphasic cells. Immunoblot analysis showed that mH1 is reactive to 42-kDa and 130-kDa components. Further, the 42-kDa component was identified as a gamma-actin homolog by N-terminal amino acid sequence analysis.
    Full-text · Article · Sep 1999 · Development Growth and Regeneration