Analysis of the mechanism of cytidine deaminase gene regulation using enChIP
Project/Area Number |
15K19005
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
General medical chemistry
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Research Institution | Gifu University |
Principal Investigator |
SATO Katsuya 岐阜大学, 大学院医学系研究科, 助教 (60733508)
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Project Period (FY) |
2015-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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Keywords | AID / 遺伝子発現制御 / 転写因子 / エンハンサー領域 / CRISPR/Cas9 / Aicda / 遺伝子転写調節 / 遺伝子発現調節 |
Outline of Final Research Achievements |
Activation-induced cytidine deaminase (AID) is expressed in activated B cells and essential for class switch recombination and somatic hypermutation. In addition, it is reported that AID can be involved in tumor progression and epigenetic regulation even in the non-B cells. To date, at least 11 transcription factors and 6 cis-regulatory elements have been identified as regulators of Aicda, the gene of AID. However, the detailed mechanisms to limited the AID expression in activated B cells are not fully understood. In this study, we investigated the mechanism of Aicda regulation. We revealed that Batf plays an essential role and the binding ability of BATF and IRF4 are important for AID expression. We established the cells that harboring deletion of each Aicda cis-regulatory element and found the Batf-IRF4 complex binds to a region different from the reported region on Aicda. Also, we examined the binding site of the complex and DNA structure-to-function relationship by ChIP and enChIP.
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Report
(4 results)
Research Products
(16 results)
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[Journal Article] M2-like macrophage polarization in high lactic acid-producing head and neck cancer.2017
Author(s)
Ohashi, T, Aoki, M, Tomita, H, Akazawa, T, Sato, K, Kuze, B, Mizuta, K, Hara, A, Nagaoka, H, Inoue, N, Ito, Y
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Journal Title
Cancer Sci
Volume: 印刷中
Issue: 6
Pages: 1128-1134
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Four-and-a-half LIM Domains 1 (FHL1) Protein Interacts with the Rho Guanine Nucleotide Exchange Factor PLEKHG2/FLJ00018 and Regulates Cell Morphogenesis.2016
Author(s)
Sato, K., Kimura, M., Sugiyama, K., Nishikawa, M., Okano, Y., Nagaoka, H., Nagase, T., Kitade, Y., and Ueda, H.
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Journal Title
J Biol Chem
Volume: 291
Issue: 48
Pages: 25227-25238
DOI
Related Report
Peer Reviewed / Open Access
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