1986 Fiscal Year Final Research Report Summary
Role of cytoskeletal proteins and heat shock proteins in regulation of cell growth
| Project/Area Number |
59480440
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | The Tokyo Metropolitan Institute of Medical Science, Department of Cell Biology |
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Principal Investigator |
YAHARA Ichiro Dept. Cell Biology, The Tokyo Metropolitan Institute of Medical Science, その他, 研究員 (60109957)
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| Co-Investigator(Kenkyū-buntansha) |
HARADA Fumiko Dept. Cell Biology, The Tokyo Metropolitan Institute of Medical Science, 細胞生物学研究部, 研究員 (70124485)
MATSUZAKI Fumio Dept. Cell Biology, The Tokyo Metropolitan Institute of Medical Science, 細胞生物学研究部, 研究員 (10173824)
IIDA Hidetoshi Dept. Cell Biology, The Tokyo Metropolitan Institute of Medical Science, 細胞生物学研究部, 研究員 (70124435)
KOYASU Shigeo Dept. Cell Biology, The Tokyo Metropolitan Institute of Medical Science, 細胞生物学研究部, 研究員 (90153684)
IIDA Kazuko Dept. Cell Biology, The Tokyo Metropolitan Institute of Medical Science, 細胞生物学研究部, 研究員 (40151229)
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| Project Period (FY) |
1984 – 1986
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| Keywords | Cell Growth / Tubulin / Microtubule / Actin / Cell Volume / Heat Shock Protein / Mutant / エノラーゼ |
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| Research Abstract |
On mouse beta-tubulin isoforms: We have examined whether isoform composition of beta-tubulin is a majour factor which determines structures and functions of microtubules. The results indicated that the expression of an acidic <beta> tubulin ( <beta> 2) caused a low degree of polymerization of total tubulin in L5178Y cells. <beta> tubulin cDNA clones were isolated and the origin of acidic <beta> 2 tubulin was investigated.
On induction of actin rods: Environmental factors which affect supuramolecular structures of actin filaments in cells were investigated. We have found that ionic (both cationic and anionic) compositions of media, osmolarity, temperature are such factors. Actin rods were induced in NaCl-buffer, in hyperosmotic media, or at high temperatures. Decrease in cell volume preceded formation of actin rods. Phalloidin did not bind actin rods although the rods consist of actin filaments. This intriguing property of the actin rods was found to be accounted for binding of cofilin, an actinbinding protein, to actin filaments that compose the rods.
Function of heat shock proteins: Yeast heat shock protein of Mr 48,000 (HSP48) appeared to be one of the key molecules that determine heat resistance of this organism. We have identified yeast HSP48 as an isozyme of enolase. Next, we have isolated a heat shock-resistant variant from CHO cells. Only HSP90 was observed to be increased in both amount and synthrsizing rate in the variant. HSP90 was purified and the intracellular location of the HSP was investigated by immuno-fluorescence microscopy. The specific properties of the vairant and the loclization of HSP90 suggested an interaction of HSP90 to actin. This was found to be the case.
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Research Products
(13 results)
