| Project/Area Number |
60440033
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Kobe University School of Medicine |
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Principal Investigator |
NISHIZUKA Yasutomi Kobe University School of Medicine, Professor, 医学部, 教授 (10025546)
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| Co-Investigator(Kenkyū-buntansha) |
OGITA Kouji Kobe University School of Medicine, Research Associate, 医学部, 助手 (60204103)
KIKKAWA Ushio Kobe University School of Medicine, Lectuer, 医学部, 講師 (40150354)
KISHIMOTO Akira Kobe University School of Medicine, Lecturer, 医学部, 講師 (60127363)
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| Project Period (FY) |
1985 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥30,200,000 (Direct Cost: ¥30,200,000)
Fiscal Year 1988: ¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 1987: ¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 1986: ¥4,300,000 (Direct Cost: ¥4,300,000)
Fiscal Year 1985: ¥18,000,000 (Direct Cost: ¥18,000,000)
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| Keywords | hormone / neurotransmitter / tumorpromotor / Ca^<2+> / phosphatidylinositol / protein kinase / receptor / 受容体 / プロテインキナーゼC / 外界シグナル / 情報受容伝達 / ジアシルグリセロール / プロティンキナーゼC / 生体膜 / 生理活性物質 |
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| Research Abstract |
The physiological importance of protein kinase C (PKC) activation is widely appreciated and well documented. Namely, this enzyme plays a specific role in the mechanisms by which external signals are transmitted to the interior of cells and in tumorignesis. In this study it has been clarified that there is more than one species of PKC molecule, and that several discrete subspecies have been defined. These proteins are derived both from multiple genes and from alternative splicing of a single RNA transcript, yet possess a primary structure containing conserved structural motifs with a high degree of sequence homology. The enzyme subspecies furified form tissues show subtle differences in their mode of activation, sensitivity of Ca^<2+>, and catalytic activity toward endogenous substrates. In the brain tissues, for example, at least seven subspecies can be distinguished, one of which is expressed only in the central nervous tissue. Biochemical and immunocytochemical studies with subspecies-specific antibodies suggest that the PKC subspecies may be differently located in pariticular cell types and at limited intracellular locations. Many cell types so far examined express more than one subspecies in variable ratios, and their intracellular distribution may depend on the state of activation of the cells. Interestingly, in response to extracellular signals, these subspecies are frequently down-regulated at different rates. The results obtained for the last three years have shown that the members of the enzyme family may have distinct roles in the processing and modulation of a variety of physiological and pathological cellular responses. The specific functions of each PKC subspecies in cellular processes remain to be explored.
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