| Project/Area Number |
11556017
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | HIROSHIMA UNIVERSITY |
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Principal Investigator |
MIYAKAWA Tokichi Hiroshima University, Graduate School of Advances Sciences of Matter., Professor, 大学院・先端物質科学研究科, 教授 (10116676)
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| Co-Investigator(Kenkyū-buntansha) |
TAKAHASHI Hidetoshi Research Institute of Life Science, Snow Brand Milk Products Co., Ltd., 生物科学研究所, 主任研究員
HIRATA Dai Hiroshima University, Graduate School of Advances Sciences of Matter., Associate Professor, 大学院・先端物質科学研究科, 助教授 (30243603)
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| Project Period (FY) |
1999 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥12,300,000 (Direct Cost: ¥12,300,000)
Fiscal Year 2002: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 2001: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 2000: ¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1999: ¥4,400,000 (Direct Cost: ¥4,400,000)
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| Keywords | Ca2+ signal / Calcineurin / Drug screening / MAP kinase / 生理活性物質 / 出芽酵母 / カルシニューリンニューリン / MAPキナーゼ / 細胞周期 / カルシウム / 免疫抑制剤 |
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| Research Abstract |
An inappropriate activation of a signaling pathway in yeast often has a deleterious physiological effect and causes various defects, including growth defects. In a certain genetic background (Δzdsl) of Saccharomyces cerevisiae, the cell-cycle progression in G2 is specifically blocked in the medium with CaCl_2 by the hyperactivation of the Ca^<2+>-signaling pathways. Here, we developed a novel drug screening procedure designed to detect the active compounds that specifically attenuate the Ca^<2+>-signaling activity on the basis of the ability to abrogate the growth defect of the cells suffering from the hyperactivated Ca^<2+> signal. Using known calcineurin inhibitors as model compounds, we have established the screening conditions for the drugs that suppress the Ca^<2+>-induced growth inhibition. An indicator strain with an increased drug sensitivity was constructed with a syr1/erg3 null mutation.
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