ROS-induced ROS release orchestrated by Nox4, Nox2, and mitochondria in VEGF signaling and angiogenesis
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Reactive oxygen species (ROS) derived from NADPH oxidase (NOX) and mitochondria play a critical role in growth factor-induced switch from a quiescent to an angiogenic phenotype in endothelial cells (ECs). However, how highly diffusible ROS produced from different sources can coordinate to stimulate VEGF signaling and drive the angiogenic process remains unknown. Using the cytosol- and mitochondria-targeted redox-sensitive RoGFP biosensors with real-time imaging, here we show that VEGF stimulation in human ECs rapidly increases cytosolic RoGFP oxidation within 1 min, followed by mitochondrial RoGFP oxidation within 5 min, which continues at least for 60 min. Silencing of Nox4 or Nox2 or overexpression of mitochondria-targeted catalase significantly inhibits VEGF-induced tyrosine phosphorylation of VEGF receptor type 2 (VEGFR2-pY), EC migration and proliferation at the similar extent. Exogenous hydrogen peroxide (H 2 O 2 ) or overexpression of Nox4, which produces H 2 O 2 , increases mitochondrial ROS (mtROS), which is prevented by Nox2 siRNA, suggesting that Nox2 senses Nox4-derived H 2 O 2 to promote mtROS production. Mechanistically, H 2 O 2 increases S36 phosphorylation of p66Shc, a key mtROS regulator, which is inhibited by siNox2, but not by siNox4. Moreover, Nox2 or Nox4 knockdown or overexpression of S36 phosphorylation-defective mutant p66Shc(S36A) inhibits VEGF-induced mtROS, VEGFR2-pY, EC migration, and proliferation. In summary, Nox4-derived H 2 O 2 in part activates Nox2 to increase mtROS via pSer36-p66Shc, thereby enhancing VEGFR2 signaling and angiogenesis in ECs. This may represent a novel feed-forward mechanism of ROS-induced ROS release orchestrated by the Nox4/Nox2/pSer36-p66Shc/mtROS axis, which drives sustained activation of angiogenesis signaling program.
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STAT3 can directly regulate mitochondrial function, and Nox2 can modulate mitochondrial activity.
“STAT3 can directly regulate mitochondrial function [97,98], and Nox2 can modulate mitochondrial activity [99][100][101]”
From Parvalbumin interneuron vulnerability and brain disorders (2021) · cites this paper as [99]
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- Authors
- Kim, Y.-M., Kim, S.-J., Tatsunami, R., Yamamura, H., Fukai, T., & Ushio-Fukai, M.
- Affiliations
- Augusta University (US)
- Northwestern University (US)
- Hokkaido Pharmaceutical University (JP)
- Nagoya City University (JP)
- Vascular Biology Center, Medical College of Georgia at Augusta University, Augusta, Georgia;
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2017-06-01
- Volume
- 312
- Issue
- 6
- Pages
- C749-C764
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- PMC
- PMC5494593
- OpenAlex
- W2605678467
- Cited by
- 251
- References
- 69
- Citations by year
- 2026: 22 · 2025: 25 · 2024: 24 · 2023: 32 · 2022: 38 · 2021: 32 · 2020: 31 · 2019: 24 · 2018: 16 · 2017: 7
- FWCI
- 8.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Heart, Lung, and Blood Institute (NHBLI) (NIHR01HL116976, NIHR01HL077524, NIHR01HL070187, NIHR21HL112293)
- American Heart Association (AHA) (#16GRNT31390032)
- Department of Veterans Affairs, Australian Government (DVA) (2I01BX001232)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- reactive oxygen species, NADPH oxidase, NOX4, NOX2, mitochondrial reactive oxygen species, VEGF signaling, angiogenesis, endothelial cells, hydrogen peroxide, feed-forward signaling, endothelial cell migration, endothelial cell proliferation, catalase
- MeSH terms
- Src Homology 2 Domain-Containing, Transforming Protein 1, NADPH Oxidase 2, NADPH Oxidase 4, Catalase, Cell Movement, Gene Expression Regulation, Humans, Hydrogen Peroxide, Membrane Glycoproteins, Microscopy, Fluorescence, Mitochondria, Oxidation-Reduction, Phosphorylation, Biosensing Techniques, Signal Transduction, Neovascularization, Physiologic, NADPH Oxidases, Feedback, Physiological, RNA, Small Interfering, Vascular Endothelial Growth Factor Receptor-2, Vascular Endothelial Growth Factor A, Cell Proliferation, Time-Lapse Imaging, Human Umbilical Vein Endothelial Cells
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