| Project/Area Number |
11470388
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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 basic dentistry
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| Research Institution | NIIGATA UNIVERSITY |
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Principal Investigator |
ODA Kimimitsu NIIGATA UNIVERSITY, GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES , Professor, 大学院・医歯学総合研究科, 教授 (10122681)
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| Co-Investigator(Kenkyū-buntansha) |
ITO Masahiro NIIGATA UNIVERSITY, GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES, Assistant, 大学院・医歯学総合研究科, 助手 (40313522)
MIZUNO Takashi NIIGATA UNIVERSITY, GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES Assitant, 大学院・医歯学総合研究科, 助手 (10018426)
AMAYA Yoshinori NIIGATA UNIVERSITY, GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES, Associate Professor, 大学院・医歯学総合研究科, 助教授 (50193032)
OHSUYE Kazuhiro SUNTORY LIMITED Director, 主席研究員
KOBAYASHI Jun MIE UNIVERSITY Faculty of technology, Assistant, 工学部, 助手 (70242930)
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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 |
¥14,500,000 (Direct Cost: ¥14,500,000)
Fiscal Year 2001: ¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 2000: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1999: ¥10,800,000 (Direct Cost: ¥10,800,000)
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| Keywords | Hvpophosphatasia / Mineralization / Alkaline phosphaiase / cis-Golgi / Proteasome / ER quality control system / 組織非特異型アルカリホスファターゼ / 細胞内輸送 / プロテアゾーム / グリコシルホスファチジルイノシトール / バキュロウイルス |
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| Research Abstract |
As a first step to understand the molecular mechanism by. which mutations in the tissue-nonspecific alkaline phosphatase gene (TNSALP) cause hypophosphatasia, we have analyzed the effects of severafmissense mutations on.the properties of TNSALP Analyzed mutants are as follows: TNSALP (R54C), TNSALP (D277A) and TNSALP [N153D] reported in the patients diagnosed with sever form of hypophsophatasia. When being expressed in COS- 1 cells, these mutated form of TNSALP were found to fail to assume proper folding and correct assembly, resulting in the formation of a high-molecular mass aggregate. These aberrant proteins tend to accumulate in the endoplasmic reticulum (TNSALP [R54C]) and cis-Golgi (TNSALP [N153D] en route to the cell surface, followed by degradation in proteasome.
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