2010 Fiscal Year Final Research Report
Mechanism for interaction between gp91phox and p22phox : two membrane-integrated proteins of the phagocyte NADPH oxidase
Project/Area Number |
21790283
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
General medical chemistry
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Research Institution | Kyushu University |
Principal Investigator |
MIYANO Kei Kyushu University, 医学研究院, 学術研究員 (60444783)
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Project Period (FY) |
2009 – 2010
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Keywords | NADPHオキシダーゼ / 活性酸素 / Nox2 / gp91^<phox> / 膜タンパク質 |
Research Abstract |
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/gp91^<phox>, a membrane-spaning protein that forms a stable heterodimer with p22^<phox>. In this study, I found that both N- and C-terminal regions play a crucial role in Nox binding to p22^<phox>. Furthermore, I showed that a short region between the TPR and activation domains in p67^<phox> is crucial for activation of Nox2.
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[Book] Front. Gastrointest.Res2011
Author(s)
Sumimoto H, Minakami R, Miyano K
Total Pages
23-346
Publisher
In free radical biology in digestive diseases(The Nox Family of NADPH oxidases that Deliberately Produce Reactive Oxygen Species)(S.Karger)