| Project/Area Number |
08680750
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Molecular biology
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| Research Institution | Kanazawa Medical University |
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Principal Investigator |
IWABUCHI Kuniyoshi Kanazawa Medical University Department of Biochemistry, Associate Professor, 医学部, 助教授 (10232696)
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| Co-Investigator(Kenkyū-buntansha) |
FUKUTOKU Masaaki Kanazawa Medical University Department of Internal Medicine, Assistant Professor, 医学部, 助手 (20218944)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1997: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1996: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | Tumor Suppressor Gene / p53 / 53BP1 / 53BP2 / Transcription Factor / BRCT Domain / p53結合蛋白質 |
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| Research Abstract |
p53 is a tumor suppressor protein that controls cell proliferation by regulating the expression of growth control genes. In a previous study, we identified two proteins, 53BP1 and 53BP2, that are able to bind to wild type but not to mutant p53 via the DNA-binding domain of p53. We isolated cDNAs expressing a full-length human 53BP1 clone, which predicts a protein of 1972 residues which is detected in the H358 human lung carcinoma cell line. The 53BP1 and 53BP2 genes were mapped to chromosomes 15q15-21 and 1q41-42, respectively. Immunofluorescence studies showed three types of staining pattern for 53BP1 : both cytoplasmic and nuclear ; homogeneous nuclear ; and nuclear dot patterns. In contrast, 53BP2 localized exclusively to the cytoplasm, and this pattern did not change upon coexpression of wild type p53. Although our previous study revealed that p53 is not able to bind simultaneously to either 53BP1 or 53BP2 and to DNA carrying a consensus binding site, both 53BP1 and 53BP2 enhanced p53-mediated transcriptional activation, suggesting that these proteins might function in signal transduction pathways to promote p53 activity.
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