| Co-Investigator(Kenkyū-buntansha) |
YAMASAKI Soh KYUSHU UNIVERSITY, Factory of Medicine, Assistant, 大学院・医学研究院, 助手 (70315084)
MUTA Tatsushi KYUSHU UNIVERSITY, Factory of Medicine, Ass.Prof., 大学院・医学研究院, 助教授 (60222337)
SUMIMOTO Hideki KYUSHU UNIVERSITY, Factory of Medicine, Prof., 大学院・医学研究院, 教授 (30179303)
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| Research Abstract |
The neutrophil NADPH oxidase, dormant in resting state, is activated to produce superoxide, which is a precursor of other active oxygens which involved in killing of phagocytozed bacteria and in inflammation. The NADPH oxidase consists of a membrane-integrated flavocytochrome b_<558> comprising two subunits, gp91^<phox> and p22^<phox>. Activation of the oxidase occurs when two cytosolic SH3 domain-containing factors, p47^<phox> and p67^<phox>, the small GTP-binding protein Rac and another cytosolic factor, p40^<phox>, assemble and translocate to the plasma membrane. In addition, the cytosolic factors are phosphorylated during oxidase activation. The assembly process is regulated and involves multiple binding interactions between the oxidase factors, resulting in an active oxidase complex. It has been demonstrated in this study that the specific molecular interactions occuring between p47^<phox> and cytochrome b_<558>, p67^<phox> and Rac, and p40^<phox> and p67^<phox>, leading to activation of the oxidase.
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