ArticleProceedings of the National Academy of Sciences of the United States of America1998
Gp91(phox) is the heme binding subunit of the superoxide-generating NADPH oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.
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Who cites it
79 citing papers in PubMed, 1 synthesis or guideline pooled it, 196 citations in OpenAlex.
- NADPH oxidases in Parkinson's disease: a systematic review.Molecular neurodegeneration · 2017Pooled it
- Increased CD14(+)HLA-DR (-/low) myeloid-derived suppressor cells correlate with extrathoracic metastasis and poor response to chemotherapy in non-small cell lung cancer patients.Cancer immunology, immunotherapy : CII · 2013Trial
- Molecular Views into the Synthesis and Activation of FlavocytochromeAntioxidants (Basel, Switzerland) · 2026Review
- Article
- Heme and immunity: The heme oxygenase dichotomy.Journal of inorganic biochemistry · 2025Review
- NADPH Oxidase 3: Beyond the Inner Ear.Antioxidants (Basel, Switzerland) · 2024Review
- NADPH Oxidases in Aortic Aneurysms.Antioxidants (Basel, Switzerland) · 2022Review
- Genotoxic stress signalling as a driver of macrophage diversity.Cell stress · 2022Review
- Are sex disparities in COVID-19 a predictable outcome of failing men's health provision?Nature reviews. Urology · 2022Review
- The impact of metal availability on immune function during infection.Trends in endocrinology and metabolism: TEM · 2021Review
- Single cell analysis of M. tuberculosis phenotype and macrophage lineages in the infected lung.The Journal of experimental medicine · 2021Article
- NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology.Antioxidants (Basel, Switzerland) · 2021Review
- A Novel Interaction of Translocator Protein 18 kDa (TSPO) with NADPH Oxidase in Microglia.Molecular neurobiology · 2020Article
- Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance.PLoS pathogens · 2020Review
- Hydrogen Sulfide Protects Against High Glucose-Induced Human Umbilical Vein Endothelial Cell Injury Through Activating PI3K/Akt/eNOS Pathway.Drug design, development and therapy · 2020Article
- The New Era of Cancer Immunotherapy: Targeting Myeloid-Derived Suppressor Cells to Overcome Immune Evasion.Frontiers in immunology · 2020Review
- Wenxin Granule Ameliorates Hypoxia/Reoxygenation-Induced Oxidative Stress in Mitochondria via the PKC-Oxidative medicine and cellular longevity · 2020Article
- Glutathione Reductase Promotes Fungal Clearance and Suppresses Inflammation during SystemicJournal of immunology (Baltimore, Md. : 1950) · 2019Article
- Nicotinamide adenine dinucleotide phosphate oxidase activation and neuronal death after ischemic stroke.Neural regeneration research · 2019Review
- Reactive Oxygen Species (ROS), Intimal Thickening, and Subclinical Atherosclerotic Disease.Frontiers in cardiovascular medicine · 2019Review
19 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The phagocyte NADPH oxidase flavocytochrome b558 is a membrane-bound heterodimer comprised of a glycosylated subunit, gp91(phox), and a nonglycosylated subunit, p22(phox). It contains two nonidentical heme groups that mediate the final steps of electron transfer to molecular oxygen (O2), resulting in the generation of superoxide ion (O2-). However, the location of the hemes within the flavocytochrome heterodimer remains controversial. In this study, we have used transgenic COS7 cell lines expressing gp91(phox), p22(phox), or both polypeptides to examine the relative role of each flavocytochrome b558 subunit in heme binding and O2- formation. A similar membrane localization was observed when gp91(phox) and p22(phox) were either expressed individually or coexpressed, as analyzed by confocal microscopy and immunoblotting of subcellular fractions. Spectral analysis of membranes prepared from COS7 cell lines expressing either gp91(phox) or both gp91(phox) and p22(phox) showed a b-type cytochrome with spectral characteristics identical to those of human neutrophil flavocytochrome b558. In contrast, no heme spectrum was detected in wild-type COS7 membranes or those containing only p22(phox). Furthermore, redox titration studies suggested that two heme groups were contained in gp91(phox) expressed in COS7 membranes, with midpoint potentials of -264 and -233 mV that were very similar to those obtained for neutrophil flavocytochrome b558. These results provide strong support for the hypothesis that gp91(phox) is the sole heme binding subunit of flavocytochrome b558. However, coexpression of gp91(phox) and p22(phox) in COS7 membranes was required to support O2- production in combination with neutrophil cytosol, indicating that the functional assembly of the active NADPH oxidase complex requires both subunits of flavocytochrome b558.
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