| Project/Area Number |
11460044
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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 |
応用微生物学・応用生物化学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
AMACHI Teruo graduate school of Agriculture, Kyoto University, Professor, 農学研究科, 教授 (30301245)
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| Co-Investigator(Kenkyū-buntansha) |
KIOKA Noriyuki graduate school of Agriculture, Kyoto University, Assistant, 農学研究科, 助手 (90234179)
UEDA Kazumitsu graduate school of Agriculture, Kyoto University, Associate Professor, 農学研究科, 助教授 (10151789)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥10,700,000 (Direct Cost: ¥10,700,000)
Fiscal Year 2001: ¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 2000: ¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 1999: ¥4,000,000 (Direct Cost: ¥4,000,000)
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| Keywords | fatty acids / cholesterol / phospholipids / ABC proteins / transporter / peroxisome / ABCA1 / atherosclerosis / ATP / 遺伝子 / クローニング / ベーター酸化 |
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| Research Abstract |
This study was done to understand the regulation of metabolism of lipids including long-chain fatty acids, very-long-chain fatty acids, phospholipids, and cholesterol from a comprehensive standpoint. The rate-determining step of catabolic pathway of long-chain fatty acids and very-long-chain fatty acids is the ATP- show high-affinity ATP binding and are co-precipitated together. The are also phosphorylated. Dimer formation could be regulated by ATP binding and/or phosphorylation.
ABCA1 has been suggested to play a key role in cellular lipid release from peripheral cells. In orderto study structure-function relationship of this protein, the protein product of a full-length human ABCA1 cDNA was examined for its functions and topological oreintation. We suggested that the signal peptide in he amino-terminal region is cleaved off in its mature form and that the following large hydrophilic region is exposed to outside of cells unlike previously proposed models.We found that this amino-termibnal extracellular domain contains a segment homologous to he autoantigen SS-N, an epitope of Sjogren's syndrome, and further identified that ABCA7codes for the autoantigen SS-N.
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