| Project/Area Number |
06404019
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General pharmacology
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| Research Institution | NAGOYA UNIVERSITY |
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Principal Investigator |
HIDAKA Hiroyoshi NAGOYA UNIVERSITY SCHOOL OF MEDICINE,PHATMACOLOGY,PROFESSOR, 医学部, 教授 (80100171)
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| Co-Investigator(Kenkyū-buntansha) |
YOKOKURA Hisayuki NAGOYA UNIVERSITY SCHOOL OF MEDICINE,PHARMACOLOGY, ASSISTANT PROFESSOR, 医学部, 助手 (90273242)
WATANABE Yasuo NAGOYA UNIVERSITY SCHOOL OF MEDICINE,PHARMACOLOGY, ASSISTANT PROFESSOR, 医学部, 助手 (10273228)
NIKI Ichiro NAGOYA UNIVERSITY SCHOOL OF MEDICINE,PHARMACOLOGY, ASSOCIATE PROFESSOR, 医学部, 助教授 (10262908)
水谷 顕洋 名古屋大学, 医学部, 助手 (30242861)
岡崎 勝男 名古屋大学, 医学部, 助手 (20252231)
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| Project Period (FY) |
1994 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥34,700,000 (Direct Cost: ¥34,700,000)
Fiscal Year 1996: ¥4,700,000 (Direct Cost: ¥4,700,000)
Fiscal Year 1995: ¥7,600,000 (Direct Cost: ¥7,600,000)
Fiscal Year 1994: ¥22,400,000 (Direct Cost: ¥22,400,000)
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| Keywords | CALCIUM SIGNAL TRANSDUCTION / CALMODULIN / CALMODULIN-DEPENDENT PROTEIN KINASE / PROTEIN KINASE CASCADES / カルモデュリン依存性キナーゼ / カルモデュリンキナーゼV / カルモデュリンキナーゼV活性化因子 / 活性化メカニズム |
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| Research Abstract |
Research on cellular signals, which depend heavily on physiological, biochemical and enzymatic studies, has made a rapid progress in the last 10 years with the break through introduction of such molecular biotogical approach as cDNA cloning. We studied molecular basis of the intracellular calcium signal transduction system by protein chemical, molecular biological, and molecular pharmacological approach. We have examined the mechanisms by which a novel Ca2+/calmodulin-dependent protein kinase V(CaM kinase V) was activated by phosphorylation. Physicochemical or biochemical properties of CaM kinase V were also analyzed Furthermore, polyclonal antibody against CaM kinase V was prepared and tissue distribution and immunohistochemical localization of CaM kinase V were studied. We have then discovered the CaM kinase V-activator which was necessary for CaM kinase V catalytic activity. Interestingly, the CaM kinase V-activator did phosphorylate Ca2+/calmodulin-dependent protein kinase IV(CaM kinase IV)associated with its activation. Finally, we suggested that there were new CaM kinase cascades such as those of MAP kinase. We have been studying to analyze biological function using synthesized molecule to activate or inhibit the activities of the target molecule. Based on these studies in creating designed molecular probes acting in the intracellular signal transduction, we have clarified the physiological functions of the CaM kinase which are closely linked to the intracellular signal transduction. Recently, we have cloned two new Ca2+/calmodulin-dependent protein kinase I(CaM kinase I) isoforms from rat brain and CaM kinase V has been thought to be an isoform of CaM kinase I.
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