Exopeptidases from periodontopathic bacteria as risk factors of type-2 diabetes mellitus
Project/Area Number |
15K11047
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Functional basic dentistry
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Research Institution | Nagasaki University |
Principal Investigator |
NEMOTO Takayuki 長崎大学, 医歯薬学総合研究科(歯学系), 教授 (90164665)
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Co-Investigator(Kenkyū-buntansha) |
小早川 健 長崎大学, 医歯薬学総合研究科(歯学系), 技術職員 (10153587)
根本 優子 長崎大学, 医歯薬学総合研究科(歯学系), 准教授 (10164667)
木村 重信 関西女子短期大学, 歯科衛生学科, 教授 (10177917)
馬場 友巳 長崎大学, 医歯薬学総合研究科(歯学系), 助教 (60189727)
下山 佑 岩手医科大学, 歯学部, 講師 (90453331)
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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 |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2017: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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Keywords | 歯周病 / 歯周病細菌 / ジペプチジルペプチダーゼ / プロテアーゼ / Porphyromonas gingivalis / 歯周病菌 / エキソペプチダーゼ / インクレチン / インスリン / 耐糖試験 / DPP7 / DPP11 / 糖尿病 / DPP / Prevotera intermedia / Trepanema forsythia / ペプチド代謝 / ジペプチド / アミノ酸トランスポーター / ペプチダーゼ |
Outline of Final Research Achievements |
We previously identified novel exopeptidases expressed in periodontopathic bacteria, such as Porphyromonas gingivalis. In this project, we synthesized a substrate truly specific for dipeptidyl-peptidase (DPP) 7. Moreover, based on the hypothesis that these exopeptidases are involved to the exacerbation of type-2 diabetes melitus, we investiagetd the role of bacterial DPPs. Mice with pre-injected with DPP4 showed increased blood glucose concentrations and retarded decline during the glucose tolerance test. In consistent to these changes, blood insulin and incretin (GLP-1) concentrations were decresed in DPP4-injected mice. To our knowledge, this is the first study that periodontopathic bactria can exacerbate type-2 diabetes via bacterial DPP4. Separately, we identified an oligopeptidase in P. gingivalis that preferentially degrades N-terminally acylated peptides, which are unable to be degraded by DPPs.
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Report
(4 results)
Research Products
(27 results)
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[Journal Article] Degradation of Incretins and Modulation of Blood Glucose Levels by Periodontopathic Bacterial Dipeptidyl Peptidase 4.2017
Author(s)
Ohara-Nemoto, Y., Nakasato, M., Shimoyama, Y., Baba, T., Kobayakawa, T., Ono, T., Yaegashi, T., Kimura, S., Nemoto, T.K.
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Journal Title
Infection and Immunity
Volume: 85
Issue: 9
DOI
NAID
Related Report
Peer Reviewed / Open Access
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[Journal Article] Bacterial protease uses distinct thermodynamic signatures for substrate recognition.2017
Author(s)
Bezerra, G. A., Ohara-Nemoto, Y., Fedosyuk, S., Cornaciu, I., Hoffmann, G., Round, A., Marquez, J. A., Nemoto, T.K., Djinovic-Carugo, K.
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Journal Title
Scientific Reports
Volume: 7
Issue: 1
Pages: 2848-2848
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] A Porphyromonas gingivalis periplasmic novel exopeptidase, acylpeptidyl oligopeptidase, releases N-acylated di- and tri-peptides from oligopeptides.2016
Author(s)
Nemoto, T.K., Ohara-Nemoto, Y., Bezerra, G. A., Shimoyama, Y. and Kimura, S.
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Journal Title
J. Biol. Chem.
Volume: 291
Issue: 11
Pages: 5913-5925
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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