Nox4, a novel homologue of the phagocyte NADPH oxidase catalytic subunit gp91phox

Akira Shiose, Futoshi Kuribayashi, Ryu Takeya, Hideki Sumimoto

Research output: Contribution to journalArticle

Abstract

During phagocytosis, the NADPH oxidase in neutrophils produces superoxide, a precursor of microbicidal oxidants, thereby playing a crucial role in host defense. The phagocyte oxidase contains the two subunits p22phox and gp91phox, the latter of which contains binding sites for the heme, FAD, and NADPH, forming the complete electron-transporting apparatus. Recent studies have revealed that four nonphagocytic homologues of gp91phox exist, including Nox4, whose cDNA we have currently cloned. Here we describe the molecular nature of Nox4, in comparison with those of other members of the NAD(P)H oxidase family.

Original languageEnglish
Pages (from-to)63-68
Number of pages6
JournalInternational Congress Series
Volume1233
Issue numberC
DOIs
Publication statusPublished - Nov 1 2002

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NADPH Oxidase
Phagocytes
Catalytic Domain
Flavin-Adenine Dinucleotide
Heme
NADP
Phagocytosis
Oxidants
Superoxides
Oxidoreductases
Neutrophils
Complementary DNA
Binding Sites
Electrons

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

Nox4, a novel homologue of the phagocyte NADPH oxidase catalytic subunit gp91phox. / Shiose, Akira; Kuribayashi, Futoshi; Takeya, Ryu; Sumimoto, Hideki.

In: International Congress Series, Vol. 1233, No. C, 01.11.2002, p. 63-68.

Research output: Contribution to journalArticle

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