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1998 Fiscal Year Final Research Report Summary

Membrane associated clathrin sheets as a possible adhesion structure in cultured osteoclasts

Research Project

Project/Area Number 09671878
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Morphological basic dentistry
Research InstitutionAsahi 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
Keywordscultured 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.

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Published: 2001-10-23  

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