Oxidative stress impairs nuclear proteins binding to the insulin responsive element in the GLUT4 promoter
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Aims/hypothesis Substantial evidence suggests an important role for the expression of GLUT4 in adipocytes, in the pathogenesis of insulin resistance and Type II (non-insulin-dependent) diabetes mellitus. We investigated whether oxidative stress decreases GLUT4 expression by impairing DNA binding of nuclear proteins to the insulin responsive element in the GLUT4 promoter. Methods 3T3-L1 adipocytes were exposed to micromolar H2O2 concentrations and GLUT4 expression and binding of nuclear proteins to defined DNA sequences were assessed. Results GLUT4 mRNA was decreased after at least 4 h exposure to H2O2, without a major change in the stability of GLUT4 transcripts. Nuclear protein extracts prepared from oxidized cells showed decreased binding to the insulin responsive element of the GLUT4 promoter but not to other DNA sequences. The direct effect of oxidation on the binding to the insulin response element was shown by the observation that in vitro oxidation of nuclear extracts with H2O2, n-ethylmaleimide or diamide decreased protein-DNA complex formation. This, and decreased binding capacity observed in nuclear extracts from oxidized cells, were partly reversible by subsequent treatment with a reducing agent. Protein binding to a consensus DNA sequence for nuclear factor 1 transcription factors was decreased 16 % by oxidation, whereas no change was observed in the protein content of several isoforms of these proteins. Conclusion/interpretation Oxidative stress causes decreased GLUT4 expression, associated with impaired binding of nuclear proteins to the insulin responsive element in the GLUT4 promoter.
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ROS inhibit insulin-stimulated glucose uptake by interfering with both IRS-1 and GLUT4.
“ROS inhibit insulin-stimulated glucose uptake by interfering with both IRS-1 and GLUT4 [140].”
From The Pathophysiology of Gestational Diabetes Mellitus (2018) · cites this paper as [140]
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Gestational diabetes mellitus management: diet and lifestyle
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From Pregnancy to Postpartum: The Cardiovascular Risks Associated with Gestational Diabetes
Sharma, R., Singh, U., Kamal, R., & Kumar, R. (2025) · Current Cardiology Reviews · doi:10.2174/011573403x354645250329171327 · Cited by 3 · see citing works
“GLUT4 and IRS-1 interference by ROS prevents insulin-stimulated glucose uptake [89].”
Study of Oxidative Stress Marker Serum Paraoxonase in Metabolic Syndrome
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- Authors
- Pessler, D., Rudich, A., & Bashan, N.
- Affiliations
- Ben-Gurion University of the Negev (IL)
- ORCID
- Rudich, A.
- Venue
- Diabetologia
- Published
- 2001-12-01
- Volume
- 44
- Issue
- 12
- Pages
- 2156-2164
- ISSN
- 0012-186X (ISSN-L)
- 1432-0428
- OpenAlex
- W2016385506
- Cited by
- 82
- References
- 30
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 3 · 2023: 12 · 2022: 3 · 2021: 5 · 2020: 5 · 2018: 2 · 2017: 4 · 2016: 1 · 2015: 3 · 2014: 5 · 2013: 2 · 2012: 7
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Diabetologia (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Israel Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- oxidative stress, GLUT4, promoter binding, nuclear proteins, adipocytes, insulin resistance, type 2 diabetes, hydrogen peroxide, protein oxidation, gene expression regulation
- MeSH terms
- Animals, Diamide, DNA, Ethylmaleimide, Hydrogen Peroxide, Insulin, Monosaccharide Transport Proteins, Muscle Proteins, Nuclear Proteins, Promoter Regions, Genetic, RNA, Messenger, Consensus Sequence, 3T3 Cells, Oxidants, Oxidative Stress, Response Elements, Glucose Transporter Type 4, Mice
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