2012 Fiscal Year Final Research Report
Mechanism for interaction between Nox2/gp91^<phox>and p22^<phox>: two membrane proteins of the phagocyte NADPH oxidase
Project/Area Number |
23790338
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
General medical chemistry
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Research Institution | Kyushu University |
Principal Investigator |
MIYANO Kei 九州大学, 医学研究院, 特任助教 (60444783)
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Project Period (FY) |
2011 – 2012
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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 thatboth N-and C-terminal regions play a crucial role in Nox binding to p22^<phox>.Furthermore, I found that the addition of a specific region of nonphagocytic Nox (Nox5) to Nox2 leads to a large amount of Nox2 protein expression.
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Research Products
(12 results)
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[Journal Article] Blockade of Inflammatory Responses by a Small-Molecule Inhibitor of the Rac Activator DOCK22012
Author(s)
Nishikimi A., Uruno T., Duan X., Cao Q., Okamura Y., Saitoh T., Saito N., Sakaoka S., Du Y., Suenaga A., Kukimoto-Niino M., Miyano K., Gotoh K., Okabe T., Sanematsu F., Tanaka Y., Sumimoto H., Honma T., Yokoyama S., Nagano T., Koh
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Journal Title
Chem. Biol
Volume: 19
Pages: 488-497
DOI
Peer Reviewed
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[Journal Article] Selectively induced apoptosis in human neutrophils in the presence of oxidative phenoxazines, 2-amino-4, 4α-dihydryo-4α-7H-phenoxazine-3-one and 2-aminophenoxazine-3-one preceded by decrease of intracellular pH, depolarization of the mitocho2011
Author(s)
Tabuchi T., Che X.-F.,Hiraishi K., Adachi M., Miyano K., Sumimoto H., Tabuchi T., Miyazawa K., and Tomoda A
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Journal Title
J. Pharmacol. Sci
Volume: 117
Pages: 139-48
URL
Peer Reviewed
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