Mechanism for interaction between Nox2 and p22phox: two membrane integrated proteins of the phagocytic oxidase
| Project/Area Number |
25460372
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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 |
General medical chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
Miyano Kei 九州大学, 医学(系)研究科(研究院), 助教 (60444783)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | NADPHオキシダーゼ / 活性酸素 / Nox2 / 膜タンパク質 / レドックスシグナル / 殺菌 / Nox |
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| Outline of Final Research Achievements |
The phagocyte NADPH oxidase, dormant in resting cells, is activated during phagocytosis to produce superoxide, a precursor of microbicidal oxidants. The catalytic core of the phagocyte oxidase is Nox2, a membrane-spaning protein that forms a stable heterodimer with p22phox. In this study, I found that both N- and C-terminal regions play a crucial role in Nox binding to p22phox. Furthermore, I showed that the C-terminal part of Nox1, Nox2 and Nox4 play a role in activation of activator proteins-dependent or -independent activation of Nox family. I also found that the posttranslational modification plays a crucial role for the protein maturation of Nox.
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Report
(4 results)
Research Products
(13 results)
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[Journal Article] DOCK2 and DOCK5 Act Additively in Neutrophils To Regulate Chemotaxis, Superoxide Production, and Extracellular Trap Formation.2014
Author(s)
Mayuki Watanabe, Masao Terasawa, Kei Miyano, Toyoshi Yanagihara, Takehito Uruno, Fumiyuki Sanematsu, Akihiko Nishikimi, Jean-Francois Cote, Hideki Sumimoto, Yoshinori Fukui
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Journal Title
The Journal of Immunology
Volume: 193
Pages: 5660-5667
Related Report
Peer Reviewed
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