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Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases
Open accessAbstract
The catalytic core of a superoxide-producing NADPH oxidase (Nox) in phagocytes is gp91phox/Nox2, a membrane-integrated protein that forms a heterodimer with p22phox to constitute flavocytochrome b558. The cytochrome becomes activated by interacting with the adaptor proteins p47phox and p67phox as well as the small GTPase Rac. Here we describe the cloning of human cDNAs for novel proteins homologous to p47phox and p67phox, designated p41nox and p51nox, respectively; the former is encoded by NOXO1 (Nox organizer 1), and the latter is encoded by NOXA1 (Nox activator 1). The novel homologue p41nox interacts with p22phox via the two tandem SH3 domains, as does p47phox. The protein p51nox as well as p67phox can form a complex with p47phox and with p41nox via the C-terminal SH3 domain and binds to GTP-bound Rac via the N-terminal domain containing four tetratricopeptide repeat motifs. These bindings seem to play important roles, since p47phox and p67phox activate the phagocyte oxidase via the same interactions. Indeed, p41nox and p51nox are capable of replacing the corresponding classical homologue in activation of gp91phox. Nox1, a homologue of gp91phox, also can be activated in cells, when it is coexpressed with p41nox and p51nox, with p41nox and p67phox, or with p47phox and p51nox; in the former two cases, Nox1 is partially activated without any stimulants added, suggesting that p41nox is normally in an active state. Thus, the novel homologues p41nox and p51nox likely function together or in combination with a classical one, thereby activating the two Nox family oxidases.
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“This loop in NOX4 seems to provide steric hindrance to slow down superoxide release, forcing two superoxide molecules to react with each other in a reaction that appears to be catalyzed, in part, by a histidine residue (925).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [925]
In the citing paper
“The mechanism of NOX4 is still controversial, but elegant work by Takac et al. indicates that the E-loop (sequence between helices V and VI) of NOX4 shows notable differences with the other NOX isoforms (925).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [925]
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Metadata
- Authors
- Takeya, R., Ueno, N., Kami, K., Taura, M., Kohjima, M., Izaki, T., Nunoi, H., & Sumimoto, H.
- Affiliations
- Kyushu University (JP)
- University of Miyazaki (JP)
- Corresponding author
- Sumimoto, Hideki
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 278
- Issue
- 27
- Pages
- 25234-25246
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4358237
- OpenAlex
- W2003241255
- Cited by
- 380
- References
- 58
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 3 · 2023: 10 · 2022: 5 · 2021: 8 · 2020: 9 · 2019: 11 · 2018: 7 · 2017: 14 · 2016: 9 · 2015: 9 · 2014: 13 · 2013: 20 · 2012: 15
- FWCI
- 12.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase, p47phox, p67phox, NOXO1, NOXA1, gp91phox, p22phox, flavocytochrome b558, Rac GTPase, SH3 domain, NOX1, superoxide production, phagocytes, oxidase activation, adaptor proteins
- MeSH terms
- Amino Acid Sequence, Cloning, Molecular, Enzyme Activation, Humans, Molecular Sequence Data, Phosphoproteins, Genome, Human, Sequence Alignment, Sequence Homology, DNA, Complementary, NADPH Oxidases, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing
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