Molecular mechanism for activation of superoxide-producing NADPH oxidases

Ryu Takeya, Hideki Sumimoto

Research output: Contribution to journalShort surveypeer-review

78 Citations (Scopus)


The membrane-integrated protein gp91phox, existing as a heterodimer with p22phox, functions as the catalytic core of the phagocyte NADPH oxidase, which plays a crucial role in host defence. The oxidase, dormant in resting cells, becomes activated to produce superoxide, a precursor of microbicidal oxidants, by interacting with the adaptor proteins p47phox and p67phox as well as the small GTPase Rac. In the past few years, several proteins homologous to gp91phox were discovered as superoxide-producing NAD(P)H oxidases (Nox's) in non-phagocytic cells; however, regulatory mechanisms for the novel oxidases have been largely unknown. Current identification of proteins highly related to p47phox and p67phox, designated Noxo1 (Nox organizer 1) and Noxa1 (Nox activator 1), respectively, has shed lights on common and distinct mechanisms underlying activations of Nox family oxidases.

Original languageEnglish
Pages (from-to)271-277
Number of pages7
JournalMolecules and cells
Issue number3
Publication statusPublished - Dec 2003

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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