1995 Fiscal Year Final Research Report Summary
The behavior of the trans-Golgi networks in plant cells.
Project/Area Number |
06640864
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Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
生物形態・構造
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Research Institution | NARA WOMEN'S UNIVERSITY |
Principal Investigator |
NOGUCHI Tetsuko NARA WOMEN'S UNIV., DEPT.OF SCIENCE,PROFESSOR, 理学部, 教授 (00135823)
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Project Period (FY) |
1994 – 1995
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Keywords | Trans-Golgi network / Golgi body / Protein transport / Freeze substitution / Immuno-electron microscopy / Botryococcus |
Research Abstract |
The behavior of the trans-Golgi networks (TGNs) in plant cells which are the sorting site of vesicle transport were examined by freeze substitution method and immuno-electron microscopy. The existence and the structure of TGNs in Cyanidium (Rhodophyceae) , Brachiomonas, Trebouxia, Ankistrodesmus, Pediastrum, Scenedesmus and Botryo-coccus (Chlorophyceae) , Bryum (Moss) , pollens and pollen tubes of Tradescantia (higher plant) were studied to get information about the TGNs which have little known in the tissue cells of higher plants. In all cells except for the pollen tubes of Tradescantia, TGNs could be observed. Accordingly, it can be suggested that the universal occurrence of the TGNs in cells from Rodophyceae to higher plants. The TGNs in Botryococcus was the biggest in structure among the cells listed above, so that the structure and the behavior of the TGN in Botryococcus were studied in ditail throughout the cell cycle. Clathrin-coated vesicles were always attached to the TGNs. The TGNs formed the vesicles which participated in the septum formation during cell division and produced multi-vesicular bodies which participated in the vacuole formation after cell division. Vesicles derived from Golgi bodies seemed to be transported to their distination sites via TGNs. The antibodies against to the Golgi-TGN and to the endoplasmic reticulum were successively produced by us. We are applying these antibodies to the immuno-electron microscopy to examine the movement of protein molecules associated TGNs.
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