| Project/Area Number |
04044100
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research |
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| Research Institution | Kyoto University |
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Principal Investigator |
NAGATA Kazuhiro Kyoto University, Chest Disease Research Institute, professor, 胸部疾患研究所, 教授 (50127114)
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| Co-Investigator(Kenkyū-buntansha) |
BENSAUDE O.C. Ecole Normale Superieure, 主任研究員
WELCH W.J. University of California, San Francisco, サンフランシスコ校, 教授
MORIMOTO R.I. Northwestern University, 教授
HIRAYOSHI Kazunori Kyoto University, Chest Disease Research Institute, 胸部疾患研究所, 助手 (80199108)
O C Bensaude エコールノルマール高等研究所, 主任研究員
W J Welch カリフォルニア大学, サンフランシスコ校, 助教授
R I Morimoto ノースウエスタン大学, 助教授
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥4,500,000 (Direct Cost: ¥4,500,000)
Fiscal Year 1993: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1992: ¥2,500,000 (Direct Cost: ¥2,500,000)
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| Keywords | Stress protein / Heat shock transcription factor / Molecular Chaperone / コラーゲン / 小胞体 |
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| Research Abstract |
1. Nagata and Morimoto collaborated to investigate the regulatory mechanism of the expression of stress proteins through heat shock transcription factor (HSF). Previously, HSF1 and HSF2 were identified and cloned. We have cloned a cDNA encoding a novel heat shock factor, HSF3, from the cDNA library of chick cells in addition to the chick homologues of human HSF1 and HSF2. HSF3 was activated by heat shock in chick erythrocytic cell line, but not in other chick cells. However, it has been revealed that HSF3 can synergistically cooperate with HSF1 in the activation of stress-induced transcription of stress proteins.
2. Nagata and Hirayoshi investigated the interaction of collagen-specific stress protein, HSP47, with newly synthesized procollagens in the cells. The purpose of the study this year was focused to where the procollagen associates with and dissociates from HSP47 during its biosynthesis. It has been revealed that procollagen binds to HSP47 in the endplasmic reticulum (ER) immediately after the procollagen co-translationally enters the ER, and dissociates from HSP47 in the cis-golgi network after the procollagen is transported into the golgi area.
3. Welch, Bensaude and Morimoto investigated the interaction of HSP70 with newly synthesized proteins as well as with HSFs. During the period of this project, it was figured out that HSP70 associates with activated DNA-binding HSF and renders the dissociation of HSF from the DNA resulting in the attenuation of the HSF activation after the completion of the induction of stress proteins including HSP70.
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