| Project/Area Number |
24592809
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional basic dentistry
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| Research Institution | Nagasaki University |
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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) |
NEMOTO Yuko 長崎大学, 医歯薬学総合研究科(歯学系), 准教授 (10164667)
BABA Tomomi 長崎大学, 医歯薬学総合研究科(歯学系), 助教 (60189717)
KOBAYAKAWA Takeshi 長崎大学, 医歯薬学総合研究科(歯学系), 技術職員 (10153587)
ITO Kiyoshi 摂南大学, 薬学部, 教授 (50201926)
馬場 友巳 長崎大学, 医歯薬学総合研究科(歯学系), 助教 (60189727)
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| Co-Investigator(Renkei-kenkyūsha) |
KIMURA Shigenobu 岩手医大, 歯学部, 教授 (10177917)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | Porphyromonas gingivalis / 歯周病 / エキソペプチダーゼ / ジペプチジルペプチダーゼ / アシルオリゴペプチジルペプチダーゼ / アミノ酸代謝 / タンパク質分解 / 歯周病原性細菌 / オリゴペプチダーゼ / DPP11 / DPP5 / アシルアミノペプチダーゼ / ペプチダーゼ / 基質特異性 / ジペプチジルププチダーゼ / 口腔細菌 |
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| Outline of Final Research Achievements |
An asaccharolytic bacterium Porphyromonas gingivalis utilizes extracellular proteins as carbon sources. Since proteins are incorporated into bacterial cell mainly as di- and tri-peptides, exopeptidases including two dipeptidyl peptidases (DPPs) and one propyl tripeptidyl peptidase A (PtpA) are viewed as prerequisite for the metabolism. In 2011, we discovered novel DPP, designated DPP11, which indicated that this process is further mediated by yet-unkown exopeptidases. In this study, we identified that DPP5 and acylpeptidyl oligopeptidase (AOP) are expressed in P. gingivalis. DPP5 possessed hydrophobic P1 specificity similar to DPP7, but the two DPPs shared the substrates through the difference in the P2-position specificity. AOP is a novel and unique peptidase, because it is able to release N-terminally blocked oligopeptides unable to be managed by DPPs and PtpA. A line up of various exopeptidases shoulb be beneficial for the survival the nutritionally-limited subgingival environment.
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