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Redox Signaling Across Cell Membranes
Open accessAbstract
Generation of reactive oxygen species (ROS) by plasma membrane-localized NADPH oxidase (Nox 2) is a major mechanism of cell signaling associated with activation of the enzyme by a variety of agonists. With activation, the integral membrane flavocytochrome of Nox 2 transfers an electron from intracellular NADPH to extracellular O(2), generating superoxide anion (O(2)(*-)). The latter dismutes to H(2)O(2) which can diffuse through aquaporin channels in the plasma membrane to elicit an intracellular signaling response. O(2)(*-) also can initiate intracellular signaling by penetration of the cell membrane through anion channels (Cl(-) channel-3, ClC-3). Endosomes containing Nox2 and ClC-3 (called signaling endosomes) are composed of internalized plasma membrane and generate O(2)(*-) in the endosomal lumen to initiate signaling at intracellular sites. Thus, cellular signaling by Nox2 is dependent on the transmembrane flux of ROS. The role of this pathway has only recently been described and will require additional investigation to appreciate its physiological significance fully.
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“ROS are generated on the membranes of the endosome of the phagocytosing cells, with the involvement of NOx [9].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [9]
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McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Griendling, K. K., Sorescu, D., & Ushio-Fukai, M. (2000) · Circulation Research · doi:10.1161/01.res.86.5.494 · Cited by 2,886
Flow-mediated endothelial mechanotransduction
Davies, P. F. (1995) · Physiological Reviews · doi:10.1152/physrev.1995.75.3.519 · Cited by 2,802
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393
Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes
Bienert, G. P., Møller, A. L. B., Kristiansen, K. A., Schulz, A., Møller, I. M., Schjoerring, J. K., & Jahn, T. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603761200 · Cited by 1,311
Hydrogen Peroxide: A Signaling Messenger
Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,194
Oxygen poisoning and x-irradiation: a mechanism in common
Gerschman, R., Gilbert, D. L., Nye, S. W., Dwyer, P., & Fenn, W. O. (1954) · Science · doi:10.1126/science.119.3097.623 · Cited by 961 · cited 1×
“T he generation of reactive oxygen species (ROS) in tissues was first proposed > 50 years ago by Gerschman, Gilbert, and co-workers (20, 21) as a possible mechanism for the toxic effects of oxygen at increased partial pressure.”
BABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911
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Graciano, M. F. R. (2011) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2011.tde-22072011-134957
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Nishio, R., Morioka, H., Takeuchi, A., Saeki, N., Furuhata, R., Chinenn, T., Tamura, H., Tamano, H., & Takeda, A. (2021) · Research Square · doi:10.21203/rs.3.rs-512285/v1
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Mishra, K. P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95545-4.00021-9
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Li, R., Li, M., Wang, X., & Zhou, Z. (2025) · Clínica e Investigación en Arteriosclerosis (English Edition) · doi:10.1016/j.artere.2026.500844
Salunkhe, S. S., Shelar, D. S., Dhavan, P. P., Butcher, R. J., & Manjare, S. T. (2026) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2026.117033
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Clère-Jehl, R. (2020) · theses.fr (ABES) · doi:10.70675/a65a57a6ze1d1z47baz8fa5zabef17722df4
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Corder, N. L. B. (2014) · eScholarship (California Digital Library)
Metadata
- Authors
- Fisher, A. B.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Fisher, Aron B.
- ORCID
- Fisher, Aron B.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2009-06
- Volume
- 11
- Issue
- 6
- Pages
- 1349-1356
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC2842114
- OpenAlex
- W2049637089
- Cited by
- 269
- References
- 62
- Citations by year
- 2026: 14 · 2025: 12 · 2024: 12 · 2023: 15 · 2022: 15 · 2021: 16 · 2020: 23 · 2019: 22 · 2018: 23 · 2017: 17 · 2016: 20 · 2015: 17 · 2014: 15 · 2013: 13 · 2012: 5
- FWCI
- 4.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute
- 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 (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase 2, reactive oxygen species, superoxide, hydrogen peroxide, aquaporins, ClC-3 chloride channel, signaling endosomes, redox signaling, plasma membrane, flavocytochrome
- MeSH terms
- Animals, Cell Membrane, Humans, Models, Biological, Oxidation-Reduction, Superoxides, Signal Transduction, Reactive Oxygen Species
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