Molecular characterization of the construction and function of the membrane microdomain(raft)
| Project/Area Number |
16370062
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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 | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Kobe University |
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Principal Investigator |
MAEKAWA Shohei Kobe-University, Graduate School of Science and Technology, Professor, 自然科学研究科, 教授 (40173695)
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| Project Period (FY) |
2004 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥13,800,000 (Direct Cost: ¥13,800,000)
Fiscal Year 2006: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 2005: ¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2004: ¥8,500,000 (Direct Cost: ¥8,500,000)
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| Keywords | raft / NAP-22 / cholesterol / neuron / bioinformation / ミエリン / PIP2 / 細胞膜 / v-ATPase / Cl-ATPase |
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| Research Abstract |
1. Molecular characterization of brain-derived membrane microdomain was performed. The raft-localization of Na/K-ARPase, one of the main ATPase in the cell membrane, was found. The isoform-specific localization change of this ATPase through ouabain-treatment was discovered.
2. NAP-22 binding proteins were detected through immunoprecipitation, and these proteins were identified as protein N-myristoyl transferase-1, and-2. This result suggests the possibility of protein modification on raft.
3. Oligomer-formation of NAP-22 through the maturation of neurons was found. Since cholesterol depletion abolished this formation, membrane cholesterol is found to have an important role in this oligomerization.
4. Neurocalcin a is a raft-localized protein. Alsin, one of the proteins related to ALS(amyotrophic lateral screlosis), was identified as a neurocalcin a binding protein. The molecular interaction of these proteins are under investigation.
5. Raft-localization of phospholipaseC β1, β2, and β3 were found. Purification and molecular characterization of PLC β1 from raft was performed and an inhibitory effect of NAP-22 on the enzymatic activity was found. This result suggests the participation of NAP-22 on the lipid dynamics on the membrane.
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Report
(4 results)
Research Products
(14 results)
