| Project/Area Number |
07044233
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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 | Tokyo Medical and Dental University |
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Principal Investigator |
HIRAOKA Masayasu Medical Research Institute, Tokyo Medical and Dental University, Professor, 難治疾患研究所, 教授 (80014281)
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| Co-Investigator(Kenkyū-buntansha) |
HIRANO Yuji Medical Research Institute, Tokyo Medical and Dental University, Assistant Profe, 難治疾患研究所, 助手 (00181181)
KAWANO Seiko Medical Research Institute, Tokyo Medical and Dental University, Associate Profe, 難治疾患研究所, 助教授 (00177718)
HARTZELL Criss School of Medicine, Emory University, Professor, 医学部, 教授
FOZZARD Harry A School of Medicine, University of Chicago, Professor, 医学部, 教授
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥8,400,000 (Direct Cost: ¥8,400,000)
Fiscal Year 1996: ¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 1995: ¥4,400,000 (Direct Cost: ¥4,400,000)
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| Keywords | protein phosphorylation / L-type Ca^<2+> channel / ATP-sensitive / K^+ channel / HERG K^+ channel / Ca^<2+> -activated Cl^- -channel / Ryanodine receptor channel / α受容体 / cGMP / Ca活性化Clチャネル |
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| Research Abstract |
The collaboration with Professor H.A.Fozzard has made a great advance in the technical achievements of the expressed channels functions and structural confirmation. We also acquired the clones of ATP-sensitive K^+ channel. Now, we are ready to express these K^+ channels and functional modulation of HERG K channel by tyrosin phosphorylation is under investigation. Furthermore, mutation of HERG K^+ channels is one of etiological factors for long QT syndrome. Therefore, we started to examine functional abnormality of the mutated channels. The joint research with Professor H.C.Hartzell has made a great advance for the purification of ryanodine receptor channel proteins, which enables us to study their function with much higher success rate. Modulation of Ca^<2+> -activated Cl^- -channel and L-type Ca^<2+> channel by protein phosphorylation and phosphatases is now studied with refined technique and new information owing to the fruits of this joint research.
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