Development of fluorescence probe for visualization of in-cell methylation events
| Project/Area Number |
17K19492
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| Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Pharmaceutical Sciences and related fields
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| Research Institution | The University of Tokushima |
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Principal Investigator |
OTAKA Akira 徳島大学, 大学院医歯薬学研究部(薬学域), 教授 (20201973)
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| Project Period (FY) |
2017-06-30 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2018: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2017: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | 生体内メチル化 / 蛍光プローブ分子 / 生体反応可視化 / アデノシルホモシステイン / 蛍光プローブ / S-アデノシルホモシステイン / N-Sアシル転移 |
|---|
| Outline of Final Research Achievements |
Fluorescence-imaging of in-cell reactions using organic compounds has advanced physiological analyses of cell functions. Imaging of the methylation events involved in a wide variety of functional regulations of cell has remained to be achieved. Attempted researches allows for visualization of SAH hydrolase activity which is closely associated with the methylation events.
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| Academic Significance and Societal Importance of the Research Achievements |
細胞内のメチル化反応は生体機能の恒常性維持に重要な働きをしており、メチル化の変調は各種疾患の発症に関与する。しかし、その重要性にも拘らず、メチル化現象を制御する酵素反応の可視化は達成されていない。そこで本研究はメチル化現象を細胞外から直接可視化するために必要とされる蛍光プローブ分子の開発を行うもので、細胞機能発現におけるメチル化の重要性解明に繋がり、その学術的意義は高い。さらに、将来的には各種疾患治療薬開発への道を拓くものであり、その社会的意義にも大きいなものがある。
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Report
(3 results)
Research Products
(22 results)
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[Journal Article] Stapled BIG3 helical peptide ERAP potentiates anti-tumour activity for breast cancer therapeutics2017
Author(s)
Yoshimaru T, Aihara K, Komatsu M, Matsushita Y, Okazaki Y, Toyokuni S, Honda J, Sasa M, Miyoshi Y, Otaka A, Katagiri T
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Journal Title
Scientific Reports
Volume: 7
Issue: 1
Pages: 1821
DOI
NAID
URL
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Elucidation of inhibitor-binding pocket of D-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology2017
Author(s)
Kohiki, T.; Kato, Y.; Nishikawa, Y.;Yorita, K.; Sagawa, I.; Denda, M.; Inokuma, T.; Shigenaga, A.; Fukui, K.; Otaka, A.
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Journal Title
Organic & Biomolecular Chemistry
Volume: 15
Issue: 25
Pages: 5289-5297
DOI
Related Report
Peer Reviewed / Open Access
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[Presentation] Combined approach of computation and enzymology to investigate novel D-amino acid oxidase inhibitors.2018
Author(s)
Kato, Y.; Maita, N.; Kohiki, T.; Kurosawa, S.; Nishikawa, Y.; Sagawa, I.; Denda, M.; Inokuma, T.; Shishido, Y.; YORITA, K.; Shigenaga, A.; Otaka, A.; Fukui, K.
Organizer
The 13th International Symposium of the Institute Network for Biomedical Sciences joint with the 3rd Symposium of the Inter-University Research Network for Trans-Omics Medicine
Related Report
Int'l Joint Research
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[Presentation] Development and application of novel protein labeling reagent SEAL.2018
Author(s)
Kohiki, T.; Kato, Y.; Denda, M.; Nishikawa, Y.; YORITA, K.; Sagawa, I.; Inokuma, T.; Shigenaga, A.; Fukui, K.; Otaka, A.
Organizer
10th International Peptide Symposium
Related Report
Int'l Joint Research
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