A new role of Pro-73 of p47phox in the activation of neutrophil NADPH oxidase

Teruaki Nagasawa, Kentaro Ebisu, Yasuyuki Inoue, Kei Miyano, Minoru Tamura

研究成果: Contribution to journalArticle査読

7 被引用数 (Scopus)


The PX domain of p47phox is thought to be involved in autoinhibition. However, when the domain was deleted, the ability to activate the phagocyte NADPH oxidase was markedly diminished. We have mutated the proline-rich region of the PX domain and examined the mutants for the ability to activate. Substitution of Gln for Pro-73 of p47phox(1-286) (P73Q) resulted in a considerably lower activity than the wild type and P73Q had a much lower affinity for the oxidase complex. Whereas, Gln substitution for Pro-76 (P76Q) showed a slightly enhanced activation and the mutant had a slightly higher affinity for the complex than the wild type. Affinity for p67phox(1-210) was slightly decreased either by P73Q or P76Q. Optimal SDS concentration for the activation was lowered by these mutations. Binding of PX domain with phosphatidylinositol-3,4-bisphosphate was diminished by P73Q mutation. The results in this study suggest that Pro-73 has a role in interaction with the catalytic component cytochrome b558.

ジャーナルArchives of Biochemistry and Biophysics
出版ステータス出版済み - 8 1 2003

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学


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