p40 phox , a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains

Wientjes, F B; Hsuan, J J; Totty, N F; Segal, A W

doi:10.1042/bj2960557

Cited by 301Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

p40 phox , a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains

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Wientjes, F B, Hsuan, J J, Totty, N F, Segal, A W·1993·Biochemical Journal

DOI 10.1042/bj2960557PMC PMC1137734

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Abstract

The NADPH oxidase generates superoxide in phagocytic cells. It is important for immunity and its deficiency leads to chronic granulomatous disease (CGD). It consists of a membrane-bound flavocytochrome b that lies dormant until activated by the translocation to the plasma membrane of cytosolic proteins, p47phox (phox for phagocyte oxidase), p67phox and p21rac, a small GTP-binding protein. We show here that a novel component, p40phox, forms an activation complex with p47phox and p67phox with which it translocates to the membrane to associate with the flavocytochrome b. cDNA cloning and amino acid analysis revealed that p40phox has an src homology 3 (SH3) domain and a large region of sequence similarity with the N-terminus of p47phox. The primary association of p40phox appears to be with p67phox, and it is present in reduced amounts in patients with CGD lacking p67phox.

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H2O2 can modulate gene expression by epigenetic modification and activate transcription factors such as AP-1, NRF2, CREB, HSF1, HIF-1, TP53, NF-κβ, NOTCH, SP1, SCREB-1 and FOXO family.
“For example, H2O2 can also modulate genes expression by epigenetic modification and activate transcription factors such as AP-1, NRF2, CREB, HSF1, HIF-1, TP53, NF-κβ, NOTCH, SP1, SCREB-1 and FOXO family [14,15,16,17,18,19,20,21,22].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [20]

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P40(PHOX), A 3RD CYTOSOLIC COMPONENT OF THE ACTIVATION COMPLEX OF THE NADPH OXIDASE TO CONTAIN SRC HOMOLOGY 3 DOMAINS
WIENTJES, F., HSUAN, J., Totty, N., & SEGAL, A. (1993) · UCL Discovery (University College London)
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Involvement of p40phox in activation of phagocyte NADPH oxidase through association of its carboxyl-terminal, but not its amino-terminal, with p67phox.
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Involvement of p4 ~ h ~ in Activation of Phagocyte NADPH Oxidase through Association of Its Carboxyl-terminal, but not Its Amino-terminal, with p67ph0~
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Authors: Wientjes, F. B., Hsuan, J. J., Totty, N. F., & Segal, A. W.
Affiliations: University College London (GB)
Ludwig Cancer Research (GB)
ORCID: Hsuan, J J
Segal, A W
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1993-12-15
Volume: 296
Issue: 3
Pages: 557-561
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj2960557
PMC: PMC1137734
OpenAlex: W1727958888
Cited by: 301
References: 27
Citations by year: 2026: 3 · 2025: 3 · 2024: 3 · 2023: 9 · 2022: 4 · 2021: 7 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 11 · 2013: 11 · 2012: 2
FWCI: 6.94
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
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 › Nitric Oxide and Endothelin Effects
Keywords: p40phox, NADPH oxidase, superoxide production, chronic granulomatous disease, p47phox, p67phox, Src homology 3 domain, membrane translocation, phagocytes, G proteins
MeSH terms: Amino Acid Sequence, Base Sequence, Biological Transport, Cell Membrane, Cloning, Molecular, Enzyme Activation, Granulomatous Disease, Chronic, Humans, Molecular Sequence Data, NADH, NADPH Oxidoreductases, Neutrophils, Phosphoproteins, Genes, src, Sequence Homology, Amino Acid, DNA, Complementary, NADPH Oxidases

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p40 phox , a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains

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