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A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential
Open accessAbstract
The redox potential of the plasma cysteine/cystine couple (E(h)CySS) is oxidized in association with risk factors for cardiovascular disease (CVD), including age, smoking, type 2 diabetes, obesity, and alcohol abuse. Previous in vitro findings support a cause-effect relationship for extracellular E(h)CySS in cell signaling pathways associated with CVD, including those controlling monocyte adhesion to endothelial cells. In this study, we provide evidence that mitochondria are a major source of reactive oxygen species (ROS) in the signaling response to a more oxidized extracellular E(h)CySS. This increase in ROS was blocked by overexpression of mitochondrial thioredoxin-2 (Trx2) in endothelial cells from Trx2-transgenic mice, suggesting that mitochondrial thiol antioxidant status plays a key role in this redox signaling mechanism. Mass spectrometry-based redox proteomics showed that several classes of plasma membrane and cytoskeletal proteins involved in inflammation responded to this redox switch, including vascular cell adhesion molecule, integrins, actin, and several Ras family GTPases. Together, the data show that the proinflammatory effects of oxidized plasma E(h)CySS are due to a mitochondrial signaling pathway that is mediated through redox control of downstream effector proteins.
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“Redox-active thiols accessible at the plasma membrane were found to mediate these effects through mechanisms that may involve receptor proteins and subsequent signaling-dependent oxidation of actin and other intracellular protein targets (157).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [157]
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van der Flier, A., & Sonnenberg, A. (2001) · Cell and Tissue Research · doi:10.1007/s004410100417 · Cited by 1,068
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Doughan, A. K., Harrison, D. G., & Dikalov, S. I. (2008) · Circulation Research · doi:10.1161/circresaha.107.162800 · Cited by 710
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Self-citationSamiec, P. S., Drews‐Botsch, C., Flagg, E. W., Kurtz, J. C., Sternberg, P., Reed, R. L., & Jones, D. P. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00286-4 · Cited by 497
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Jones, D. P., Mody, V. C., Carlson, J. L., Lynn, M. J., & Sternberg, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01040-7 · Cited by 392
Self-citationLiu, Y., Zhao, H., Li, H., Kalyanaraman, B., Nicolosi, A. C., & Gutterman, D. D. (2003) · Circulation Research · doi:10.1161/01.res.0000091261.19387.ae · Cited by 323
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Self-citationFree radical biology and medicine
(2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00485-4
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Environmental Toxicology: Oxidative Stress
Jones, D. P. (2012) · Springer eBooks · doi:10.1007/978-1-4419-0851-3_45
Self-citation
Metadata
- Authors
- Go, Y.-M., Park, H., Koval, M., Orr, M., Reed, M., Liang, Y., Smith, D., Pohl, J., & Jones, D. P.
- Affiliations
- Emory University (US)
- Dankook University (KR)
- Centers for Disease Control and Prevention (US)
- Corresponding author
- Go, Young-Mi
- Jones, Dean P.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 48
- Issue
- 2
- Pages
- 275-283
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC3057402
- OpenAlex
- W1964139246
- Cited by
- 103
- References
- 36
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 7 · 2021: 3 · 2020: 5 · 2019: 4 · 2018: 7 · 2017: 8 · 2016: 5 · 2015: 9 · 2014: 7 · 2013: 7 · 2012: 10
- FWCI
- 4.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL083120, R01HL083120)
- National Institute of Environmental Health Sciences (ES 009047, ES011195, R01ES009047, R01ES011195)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- endothelial signaling, mitochondria, reactive oxygen species, thioredoxin 2, cardiovascular risk factors, monocyte adhesion, inflammation, redox proteomics, VCAM-1, integrins, actin, Ras GTPase
- MeSH terms
- Animals, Cardiovascular Diseases, Cell Adhesion, Cysteine, Cystine, Cytoskeletal Proteins, Endothelium, Vascular, Humans, Membrane Proteins, Mice, Transgenic, Mitochondria, Oxidation-Reduction, Mass Spectrometry, Thioredoxins, Signal Transduction, Reactive Oxygen Species, Oxidative Stress, Proteomics, NIH 3T3 Cells, Mice
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