| Project/Area Number |
62570123
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | National Institute of Neuroscience, NCNP |
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Principal Investigator |
ISHIURA Shoichi National Institute of Neuroscience, NCNP. Section Chief., 神経研究所, 室長 (10158743)
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| Co-Investigator(Kenkyū-buntansha) |
安楽 治美 国立精神, 神経センター・神経研究所, 研究補助
KOIZUMI Hirotaka National Institute of Neuroscience, NCNP. Research fellow., 神経センター・神経研究所, 研究生 (10215155)
TSUKAHARA Toshifumi National Institute of Neuroscience, NCNP. Researcher., 神経センター・神経研究所, 研究員 (60207339)
ARAHATA Kiichi National Institute of Neuroscience, NCNP. Section Chief., 神経センター・神経研究所, 室長 (30053325)
SUGITA Hideo National Institute of Neuroscience, NCNP. Head., 神経センター・神経研究所, 部長 (80009951)
ANRAKU Harumi National Institute of Neuroscience, NCNP. Research fellow.
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1988: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1987: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | T-lymphocyte / Cytotoxicity / Myopathy / Perforin / Protease / Killer lymphocyte / CTL |
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| Research Abstract |
The mechanism by Which structural proteins in myopathic muscle are degraded is not fully understood. This work focused on the killing molecules in T-lymphocytes from the viewpoint of their functions. During 2 years of research project, we found the following:
1) Cytotoxic granules in cytotoxic T-lymphocytes (CTL) contain two distinct lytic molecules, perforin and serine esterase (SE). Perforin, which is released after signalling by a receptor on the CTL membrane, first binds to the target cell membrane and subsequently forms functional pore on the same membrane. These processes require Ca^<2+>ions. Heparin and other acid mucopolysaccharides only enhanced the pore-forming lytic process.
2) We found that localization of SE is different from that of perforin in CTL cells. SE did not digest myosin, whereas other cytoplasmic protease digested it. Suggesting that SE is not directly involved in CTL-mddiated protein degradation.
3) We isolated and purified two novel proteolytic enzymes, one is a high-molecular-mass multicatalytic proteinase, ingensin, and the other cystine aminopeptidase. Ingensin was shown to be involved in ATP-dependent proteolysis.
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