Cited by 380Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

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Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

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Takeya, Ryu, Ueno, Noriko, Kami, Keiichiro, Taura, Masahiko, Kohjima, Motoyuki, Izaki, Tomoko, Nunoi, Hiroyuki, Sumimoto, Hideki·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.m212856200PMC PMC4358237

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Abstract

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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pEF-BOS, a powerful mammalian expression vector
Mizushima, S., & Nagata, S. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.17.5322 · Cited by 1,594
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840
Novel gp91 phox Homologues in Vascular Smooth Muscle Cells: nox1 Mediates Angiotensin II–Induced Superoxide Formation and Redox-Sensitive Signaling Pathways
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839
Homologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820
A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103034200 · Cited by 622
Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins
DeLeo, F. R., & Quinn, M. T. (1996) · Journal of Leukocyte Biology · doi:10.1002/jlb.60.6.677 · Cited by 526
A Novel Superoxide-producing NAD(P)H Oxidase in Kidney
Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki, Y., & Sumimoto, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007597200 · Cited by 517
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Bánfi, B., Clark, R. A., Steger, K., & Krause, K.-H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200613200 · Cited by 491

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Bechor, E., Zahavi, A., Amichay, M., Fradin, T., Federman, A., Berdichevsky, Y., & Pick, E. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.4a1219-607r · Cited by 11
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Kim, J.-S., & Bokoch, G. (2008) · Journal of Innate Immunity · doi:10.1159/000151481 · Cited by 12
The NOXO1β PX Domain Preferentially Targets PtdIns(4,5)P2 and PtdIns(3,4,5)P3
Davis, N. Y., McPhail, L. C., & Horita, D. A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.058 · Cited by 10
Role of gp91phoxHomolog Nox1 in Induction of Premalignant Spindle Phenotypes of HPV 16 E6/E7—Immortalized Human Keratinocytes
Chamulitrat, W. (2010) · The Scientific World JOURNAL · doi:10.1100/tsw.2010.131 · Cited by 9
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Miyano, K., Okamoto, S., 山内, 明., Kajikawa, M., Kiyohara, T., Taura, M., Kawai, C., & Kuribayashi, F. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1823383 · Cited by 9
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Shrestha, P., Yun, J.-H., Ko, Y., Kim, M., Bae, Y. S., & Lee, W. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.083 · Cited by 7
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Liu, Y., Liang, S., Shi, D., Zhang, Y., Bai, C., & Ye, R. D. (2023) · PLoS ONE · doi:10.1371/journal.pone.0285206 · Cited by 9
Superoxide Generation by Nox1 in Guinea Pig Gastric Mucosal Cells Involves a Component with p67phox-Ability
Yoshida, L. S., Nishida, S., Shimoyama, T., Kawahara, T., Kondo-Teshima, S., Rokutan, K., Kobayashi, T., & Tsunawaki, S. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.147 · Cited by 7
NOXA1-dependent NADPH oxidase 1 signaling mediates angiotensin II activation of the epithelial sodium channel
Mironova, E., Archer, C. R., Vendrov, A. E., Runge, M. S., Madamanchi, N. R., Arendshorst, W. J., Stockand, J. D., & El‐Aziz, T. M. A. (2022) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00107.2022 · Cited by 7
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Nunoi, H. (2007) · Japanese Journal of Clinical Immunology · doi:10.2177/jsci.30.1 · Cited by 5
Self-citation
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Dinauer, M. C. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9424-3_9 · Cited by 5
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Spina, A., Guidarelli, A., Buffi, G., Fiorani, M., & Cantoni, O. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107554 · Cited by 4
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Weaver, J. R., & Taylor, D. (2014) · Springer eBooks · doi:10.1007/978-94-007-6686-0_46 · Cited by 2
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Davis, N. Y., McPhail, L. C., & Horita, D. A. (2010) · Biomolecular NMR Assignments · doi:10.1007/s12104-010-9286-x · Cited by 1
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Sharma, M., & Afolayan, A. J. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_16 · Cited by 1
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Ushio‐Fukai, M. (2009) · Wiley eBooks · doi:10.1002/9783527627585.ch14 · Cited by 1
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Fletcher, E. V. M. (2012) · doi:10.17077/etd.t0bey3zr · Cited by 1
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Yin, W. (2012) · SMARTech Repository (Georgia Institute of Technology) · Cited by 1
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Bokoch, G., Gianni, D., Kim, J., & Kao, Y.-Y. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00216-3
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Stanley, A. (2014) · Arrow@dit (Dublin Institute of Technology) · doi:10.13025/16338
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Sha, S. (2012)
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Identification of oxLDL-induced oxidative stress sources in cardiovascular disease.
Cross, S. (2016) · UC Research Repository (University of Canterbury) · doi:10.26021/9030
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Ringwood, L. A. (2011) · VTechWorks (Virginia Tech)
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Nakano, Y., & Bánfi, B. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_11
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Dang, P. M., & Benna, J. E. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_15 · Cited by 2
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Luo, J., & Li, Y. (2008) · World Chinese Journal of Digestology · doi:10.11569/wcjd.v16.i16.1768
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Henri, P. (2010) · theses.fr (ABES) · doi:10.70675/3d9b68e3z3ff2z4f0czae15z1e7b3d7b9f58
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Leclerc, J. (2013) · theses.fr (ABES) · doi:10.70675/5743e778zd4fdz4faazbccfz81db73478c61
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Chocry, M. (2017) · theses.fr (ABES) · doi:10.70675/effec4c5z947az4947z8f4az0a74067f7f5e
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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
ORCID: Takeya, Ryu
Kohjima, Motoyuki
Nunoi, Hiroyuki
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)
DOI: 10.1074/jbc.m212856200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6305 d)
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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

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Cited by

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Metadata

Record

About these checks