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Cited by 146Redox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative MechanismsNitric Oxide and Endothelin Effects

NOX5 is expressed at the plasma membrane and generates superoxide in response to protein kinase C activation

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SERRANDER, L, JAQUET, V, BEDARD, K, PLASTRE, O, HARTLEY, O, ARNAUDEAU, S, DEMAUREX, N, SCHLEGEL, W +1 more·2007·Biochimie
DOI 10.1016/j.biochi.2007.05.004
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Abstract

NOX5 is a ROS-generating NADPH oxidase which contains an N-terminal EF-hand region and can be activated by cytosolic Ca(2+) elevations. However the C-terminal region of NOX5 also contains putative phosphorylation sites. In this study we used HEK cells stably expressing NOX5 to analyze the size and subcellular localization of the NOX5 protein, its mechanisms of activation, and the characteristics of the ROS released. We demonstrate that NOX5 can be activated both by the protein kinase C activating phorbol esther PMA and by the Ca(2+) ionophore ionomycin. The PMA- but not the ionomycin-dependent activation can be inhibited by protein kinase C inhibitors. NOX5 activity is inhibited by submicromolar concentrations of diphenyl iodonium (DPI), but not by apocynin. Western blot analysis showed a lower ( approximately 70 kDa) than expected (82 kDa) molecular mass. Two arguments suggest that NOX5 is at least partially expressed on the plasma membrane: (i) the membrane-impermeant superoxide was readily detected by extracellular probes, and (ii) immunofluorescent labeling of NOX5 detected a fraction of the NOX5 protein at the plasma membrane. In summary, we demonstrate that NOX5 can be found intracellularly and at the cell surface. We also describe that it can be activated through protein kinase C, in addition to its Ca(2+) activation.

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  • NO, through its high affinity for heme groups or via S-nitrosation, can act as an important modulator of NOX or can modulate the insertion of heme in the receptor sGC.

    “In another example, NO, through its high affinity for heme groups or via S-nitrosation, can act as an important modulator of NOX (176, 315, 846) or can also modulate the insertion of heme in the receptor sGC.”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [846]

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Authors
SERRANDER, L., JAQUET, V, BEDARD, K., PLASTRE, O., HARTLEY, O., ARNAUDEAU, S., DEMAUREX, N., SCHLEGEL, W., & KRAUSE, K.
Affiliations
  • University of Geneva (CH)
  • University Hospital of Geneva (CH)
Corresponding author
KRAUSE, K
ORCID
Venue
Biochimie
Publisher
Elsevier BV
Published
2007-09
Volume
89
Issue
9
Pages
1159-1167
ISSN
  • 0037-9042 (ISSN-L)
  • 0300-9084
DOI
10.1016/j.biochi.2007.05.004
OpenAlex
W2093669649
Cited by
146
References
29
Citations by year
2026: 2 · 2025: 2 · 2024: 6 · 2023: 3 · 2022: 4 · 2021: 5 · 2020: 7 · 2019: 15 · 2018: 4 · 2017: 7 · 2016: 4 · 2015: 9 · 2014: 9 · 2013: 8 · 2012: 17
FWCI
4.10
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimie (publishedVersion)
  • PubMed (publishedVersion)
  • Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
  • Archive ouverte UNIGE (University of Geneva) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords
NADPH oxidase 5, NADPH oxidase, reactive oxygen species, superoxide, protein kinase C, phorbol ester, ionomycin, calcium signaling, plasma membrane localization, subcellular localization, apocynin, protein phosphorylation, EF-hand calcium binding
MeSH terms
NADPH Oxidase 5, Acetophenones, Amino Acid Sequence, Cell Line, Cell Membrane, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Fluorescent Antibody Technique, Humans, Membrane Proteins, Molecular Sequence Data, Phosphorylation, Protein Kinase C, Superoxides, Transfection, Blotting, Western, Ionomycin, Reactive Oxygen Species, Sequence Homology, Amino Acid, Microscopy, Confocal, NADPH Oxidases, Protein Kinase Inhibitors

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