Cited by 187Redox biology and oxidative stressSelenium in Biological SystemsOrganoselenium and organotellurium chemistry

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Glutathione Peroxidase-1 Regulates Mitochondrial Function to Modulate Redox-dependent Cellular Responses

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Handy, Diane E., Lubos, Edith, Yang, Yi, Galbraith, John D., Kelly, Neil, Zhang, Ying-Yi, Leopold, Jane A., Loscalzo, Joseph·2009·Journal of Biological Chemistry

DOI 10.1074/jbc.m900392200PMC PMC2673260

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Abstract

Glutathione peroxidase-1 (GPx-1) is a selenocysteine-containing enzyme that plays a major role in the reductive detoxification of peroxides in cells. In permanently transfected cells with approximate 2-fold overexpression of GPx-1, we found that intracellular accumulation of oxidants in response to exogenous hydrogen peroxide was diminished, as was epidermal growth factor receptor (EGFR)-mediated Akt activation in response to hydrogen peroxide or EGF stimulation. Knockdown of GPx-1 augmented EGFR-mediated Akt activation, whereas overexpression of catalase decreased Akt activation, suggesting that EGFR signaling is regulated by redox mechanisms. To determine whether mitochondrial oxidants played a role in these processes, cells were pretreated with a mitochondrial uncoupler prior to EGF stimulation. Inhibition of mitochondrial function attenuated EGF-mediated activation of Akt in control cells but had no additional effect in GPx-1-overexpressing cells, suggesting that GPx-1 overexpression decreased EGFR signaling by decreasing mitochondrial oxidants. Consistent with this finding, GPx-1 overexpression decreased global protein disulfide bond formation, which is dependent on mitochondrially produced oxidants. GPx-1 overexpression, in permanently transfected or adenovirus-treated cells, also caused overall mitochondrial dysfunction with a decrease in mitochondrial potential and a decrease in ATP production. GPx-1 overexpression also decreased EGF- and serum-mediated [(3)H]thymidine incorporation, indicating that alterations in GPx-1 can attenuate cell proliferation. Taken together, these data suggest that GPx-1 can modulate redox-dependent cellular responses by regulating mitochondrial function.

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Authors: Handy, D. E., Lubos, E., Yang, Y., Galbraith, J. D., Kelly, N., Zhang, Y.-Y., Leopold, J. A., & Loscalzo, J.
Affiliations: Brigham and Women's Hospital (US)
Corresponding author: Handy, Diane E.
ORCID: Handy, Diane E.
Yang, Yi
Kelly, Neil
Leopold, Jane A.
Loscalzo, Joseph
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2009-05
Volume: 284
Issue: 18
Pages: 11913-11921
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m900392200
PMC: PMC2673260
OpenAlex: W2020272282
Cited by: 187
References: 64
Citations by year: 2026: 12 · 2025: 10 · 2024: 5 · 2023: 6 · 2022: 18 · 2021: 8 · 2020: 17 · 2019: 11 · 2018: 14 · 2017: 16 · 2016: 9 · 2015: 11 · 2014: 7 · 2013: 13 · 2012: 8
FWCI: 4.02
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4179 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
Funders: National Heart, Lung, and Blood Institute (HL81587, HL61795, HL58976, R01HL058976, P01HL081587, R01HL061795)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Physical Sciences › Chemistry › Organic Chemistry › Organoselenium and organotellurium chemistry
Keywords: glutathione peroxidase 1, redox signaling, EGFR signaling, Akt activation, hydrogen peroxide, protein disulfide bond formation, mitochondrial dysfunction, mitochondrial membrane potential, ATP production, cell proliferation, catalase, oxidative stress
MeSH terms: Glutathione Peroxidase GPX1, Adenosine Triphosphate, Adenoviridae, Catalase, Cell Line, Disulfides, Enzyme Activation, Epidermal Growth Factor, Glutathione Peroxidase, Humans, Hydrogen Peroxide, Mitochondria, Liver, Oxidation-Reduction, Transduction, Genetic, Uncoupling Agents, Signal Transduction, Oxidants, Selenocysteine, Cell Proliferation, Proto-Oncogene Proteins c-akt, Selenoproteins, Gene Knockdown Techniques, ErbB Receptors

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Glutathione Peroxidase-1 Regulates Mitochondrial Function to Modulate Redox-dependent Cellular Responses

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