Reactive oxygen species enhance insulin sensitivity
Open accessAbstract
Chronic reactive oxygen species (ROS) production by mitochondria may contribute to the development of insulin resistance, a primary feature of type 2 diabetes. In recent years it has become apparent that ROS generation in response to physiological stimuli such as insulin may also facilitate signaling by reversibly oxidizing and inhibiting protein tyrosine phosphatases (PTPs). Here we report that mice lacking one of the key enzymes involved in the elimination of physiological ROS, glutathione peroxidase 1 (Gpx1), were protected from high-fat-diet-induced insulin resistance. The increased insulin sensitivity in Gpx1(-/-) mice was attributed to insulin-induced phosphatidylinositol-3-kinase/Akt signaling and glucose uptake in muscle and could be reversed by the antioxidant N-acetylcysteine. Increased insulin signaling correlated with enhanced oxidation of the PTP family member PTEN, which terminates signals generated by phosphatidylinositol-3-kinase. These studies provide causal evidence for the enhancement of insulin signaling by ROS in vivo.
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Mice lacking glutathione peroxidase are protected from insulin resistance induced by high-fat diets.
“Additionally, mice lacking glutathione peroxidase are protected from insulin resistance induced by high-fat diets (39).”
Increasing H2O2 in skeletal muscle or the deletion of KEAP1 enhances insulin sensitivity or improves glucose tolerance.
“Similarly, previous studies have shown that increasing H2O2 in skeletal muscle (8) or the deletion of KEAP1 (9) enhances insulin sensitivity or improves glucose tolerance.”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [8]
Lack of mitochondrial oxidant production leads to diminished cell signaling in response to growth factors such as insulin and decreases the formation of necessary protein disulfides.
“lack of mitochondrial oxidant production leads to diminished cell signaling in response to growth factors, such as insulin, and decreases the formation of necessary protein disulfides (169, 264, 284, 450, 464).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [264]
In mouse in vivo models, lack of GPx-1 augments insulin-mediated Akt activation in skeletal muscle, whereas overexpression of GPx-1 attenuates these responses in transgenic mice.
“Furthermore, in mouse in vivo models, lack of GPx-1 was found to augment insulin-mediated Akt activation in skeletal muscle (264), whereas overexpression of GPx-1 attenuated these responses in transgenic mice (284).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [264]
ROS enhance insulin sensitivity in high-fat-diet mice.
“It has also been reported that ROS enhance insulin sensitivity in HFD mice ([100](#B100)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [100]
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Griffin, T. M., Humphries, K. M., Kinter, M., Lim, H.-Y., & Szweda, L. I. (2016) · Biochimie · doi:10.1016/j.biochi.2015.10.013 · Cited by 36 · see citing works
Zinc homeostasis and redox alterations in obesity
Franco, C., & Canzoniero, L. M. T. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1273177 · Cited by 31 · see citing works
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- Authors
- Loh, K., Deng, H., Fukushima, A., Cai, X., Boivin, B., Galic, S., Bruce, C., Shields, B. J., Skiba, B., Ooms, L. M., Stepto, N., Wu, B., Mitchell, C. A., Tonks, N. K., Watt, M. J., Febbraio, M. A., Crack, P. J., Andrikopoulos, S., & Tiganis, T.
- Affiliations
- Monash University (AU)
- Baker Heart and Diabetes Institute (AU)
- Cold Spring Harbor Laboratory (US)
- The University of Melbourne (AU)
- Corresponding author
- Tiganis, Tony
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 10
- Issue
- 4
- Pages
- 260-272
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC2892288
- OpenAlex
- W2032172473
- Cited by
- 581
- References
- 48
- Citations by year
- 2026: 12 · 2025: 17 · 2024: 27 · 2023: 22 · 2022: 28 · 2021: 36 · 2020: 24 · 2019: 24 · 2018: 42 · 2017: 36 · 2016: 51 · 2015: 34 · 2014: 50 · 2013: 56 · 2012: 43
- FWCI
- 16.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Victoria University Research Repository (Victoria University) (submittedVersion)
- Funders
- National Cancer Institute (R37CA053840, R01CA053840, CA53840)
- National Institute of General Medical Sciences (GM55989, R01GM055989)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- reactive oxygen species, insulin sensitivity, insulin resistance, type 2 diabetes, glutathione peroxidase 1, protein tyrosine phosphatase, phosphatidylinositol 3-kinase/Akt signaling, muscle glucose uptake, high-fat diet, N-acetylcysteine, mitochondrial reactive oxygen species
- MeSH terms
- Glutathione Peroxidase GPX1, Acetylcysteine, Animals, Antioxidants, Cells, Cultured, Energy Metabolism, Female, Glutathione Peroxidase, Humans, Insulin, Insulin Resistance, Male, Motor Activity, Obesity, Oxidation-Reduction, Signal Transduction, Reactive Oxygen Species, Mice, Knockout, Phosphatidylinositol 3-Kinases, Proto-Oncogene Proteins c-akt, PTEN Phosphohydrolase, Mice
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