1998 Fiscal Year Final Research Report Summary
Membrane associated clathrin sheets as a possible adhesion structure in cultured osteoclasts
Project/Area Number |
09671878
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Morphological basic dentistry
|
Research Institution | Asahi University |
Principal Investigator |
AKISAKA Toshitaka Asahi University, School of Dentistry, Professor, 歯学部, 教授 (70116523)
|
Co-Investigator(Kenkyū-buntansha) |
YOSHIDA Hisao Asahi University, School of Dentistry, Assistant Professor, 歯学部, 助手 (80102119)
|
Project Period (FY) |
1997 – 1998
|
Keywords | cultured osteoclast / clathrin sheet / podosome / cytoskeleton / cell shearing / immunostaining / quick-freezing / freeze-dried replica |
Research Abstract |
The purpose of the present study is to investigate the cell-substratum adhesion structures in cultured osteoclasts using immunofluorescent microscopy and electron microscopy after cell shearing or detergent extraction. Two different adhesion structures were identified ; one was typical podosomes and the other clathrin sheets. In quick-freezing and freeze-substituted or freeze-dried replicas the clathrins showed a typical honey-comb substructure which were composed of polygons with hexagonal or pentagonal in shape (each polygon was 20〜30nm in diameter). These clathrin sheets were often encountered the peripheral or central region of the ventral membrane. Almost clathrin sheets were devoid of the cytoskeletons, while podosomes were composed of the bundles of microfilaments and related structures. In some case, the ventral membrane of pseudo-podium in moving osteoclasts contained several clathrin sheets. In addition clathrin sheets were left behind the cell surface even after almost cellular structures had removed away by using mechanical cell shearing and chemical detergent extraction. In conclusion, these results, therefore, support the idea that the clathrin sheets plays a possible role in osteoclastic adhesion via receptor-ligand interaction.
|