2013 Fiscal Year Final Research Report
Elucidation of a novel lipid signaling in Pseudomonas aeruginosa
| Project/Area Number |
23570142
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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 |
Structural biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
OKINO NOZOMU 九州大学, (連合)農学研究科(研究院), 准教授 (90363324)
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| Project Period (FY) |
2011 – 2013
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| Keywords | セラミダーゼ / セラミド / 転写制御因子 / 緑膿菌 |
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| Research Abstract |
Ceramidase (EC3.5.1.23) is an enzyme that catalyses the hydrolysis of the N-acyl linkage of ceramide to generate fatty acid and sphingosine. We previously reported the purification, molecular cloning and characterization of a neutral ceramidase from Pseudomonas aeruginosa, which is a famous opportunistic pathogen that causes serious infectious diseases. Recently, we found that the simultaneous production of hemolytic phospholipase C (PlcH) and ceramidase was induced by plasma membrane lipids, and PlcH-induced hemolysis was significantly enhanced by the action of ceramidase. In the present study, we identified a novel transcriptional regulator, which is involved in the expression of Pseudomonas ceramidase and PlcH. We also revealed the mechanism of the ceramidase expression through the transcriptional regulator, which is activated by host-derived sphingolipid.
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Research Products
(9 results)
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[Journal Article] Pseudomonas-derived ceramidase induces production of inflammatory mediators from human keratinocytes via sphingosine-1-phosphate2014
Author(s)
Oizumi A, Nakayama H, Okino N, Iwahara C, Kina K, Matsumoto R, Ogawa H, Takamori K, Ito M, Suga Y, Iwabuchi K.
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Journal Title
PLoS One.
Volume: 9(2)
Pages: 89402
DOI
Peer Reviewed
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[Remarks] データベース (ozomu Okino, Makoto Ito,日本糖鎖科学統合 データベースJCGGDB GlycoPOD (GlycoScience Protocol Online Database), 2012.03 Hydrolysis of ceramide by ceramidase (CDase) and measurement of CDase activity)
