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Tissue-specific control of mitochondrial respiration in obesity-related insulin resistance and diabetes
Abstract
The tissue-specific role of mitochondrial respiratory capacity in the development of insulin resistance and type 2 diabetes is unclear. We determined mitochondrial function in glycolytic and oxidative skeletal muscle and liver from lean (+/?) and obese diabetic (db/db) mice. In lean mice, the mitochondrial respiration pattern differed between tissues. Tissue-specific mitochondrial profiles were then compared between lean and db/db mice. In liver, mitochondrial respiratory capacity and protein expression, including peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α), was decreased in db/db mice, consistent with increased mitochondrial fission. In glycolytic muscle, mitochondrial respiration, as well as protein and mRNA expression of mitochondrial markers, was increased in db/db mice, suggesting increased mitochondrial content and fatty acid oxidation capacity. In oxidative muscle, mitochondrial complex I function and PGC-1α and mitochondrial transcription factor A (TFAM) protein levels were decreased in db/db mice, along with increased level of proteins related to mitochondrial dynamics. In conclusion, mitochondrial respiratory performance is under the control of tissue-specific mechanisms and is not uniformly altered in response to obesity. Furthermore, insulin resistance in glycolytic skeletal muscle can be maintained by a mechanism independent of mitochondrial dysfunction. Conversely, insulin resistance in liver and oxidative skeletal muscle from db/db mice is coincident with mitochondrial dysfunction.
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“and with insulin resistance in the same mice model (Holmstrom et al., 2012).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Holmstrom et al., 2012
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Cites
Dysfunction of Mitochondria in Human Skeletal Muscle in Type 2 Diabetes
Kelley, D. E., He, J., Menshikova, E. V., & Ritov, V. B. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2944 · Cited by 2,321
Chen, H., Charlat, O., Tartaglia, L. A., Woolf, E. A., Weng, X., Ellis, S. J., Lakey, N. D., Culpepper, J., More, K. J., Breitbart, R. E., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81294-5 · Cited by 2,214
Impaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
Petersen, K. F., Dufour, S., Befroy, D., Garcia, R., & Shulman, G. I. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031314 · Cited by 2,193
Mitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070
Patti, M. E., Butte, A. J., Crunkhorn, S., Cusi, K., Berria, R., Kashyap, S., Miyazaki, Y., Kohane, I., Costello, M., Saccone, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1032913100 · Cited by 1,952
CORRELATED MORPHOMETRIC AND BIOCHEMICAL STUDIES ON THE LIVER CELL
Weibel, E. R., Stäubli, W., Gnägi, H. R., & Hess, F. A. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.42.1.68 · Cited by 1,142
Wang, Y., Rimm, E. B., Stampfer, M. J., Willett, W. C., & Hu, F. B. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/81.3.555 · Cited by 1,127
Kelley, D. E., Goodpaster, B., Wing, R. R., & Simoneau, J.-A. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.6.e1130 · Cited by 1,096
Mootha, V. K., Bunkenborg, J., Olsen, J. V., Hjerrild, M., Wisniewski, J. R., Stahl, E., Bolouri, M. S., Ray, H. N., Sihag, S., Kamal, M., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00926-7 · Cited by 889
High-fat diets cause insulin resistance despite an increase in muscle mitochondria
Hancock, C. R., Han, D.-H., Chen, M., Terada, S., Yasuda, T., Wright, D. C., & Holloszy, J. O. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802057105 · Cited by 538 · cited 1×
“Several lines of evidence suggest that mitochondrial function in liver or skeletal muscle is associated with insulin sensitivity and T2DM in animal models (2, 10, 12, 20, 40, 48) and humans (25, 27, 36–39).”
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Cantó, C. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811752-1.00017-1 · Cited by 1
Martins, A. R. (2014) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.87.2014.tde-05012015-152951
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Tadic, M. V., & Cuspidi, C. (2014) · Gene Cell and Tissue · doi:10.17795/gct-20664
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Cedrone, M. (2019) · Scholarship@Western (Western University)
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Metadata
- Authors
- Holmström, M. H., Iglesias-Gutierrez, E., Zierath, J. R., & Garcia-Roves, P. M.
- Affiliations
- Departments of 1Molecular Medicine and Surgery and
- Physiology and Pharmacology, Section for Integrative Physiology, Karolinska Institutet, Stockholm, Sweden
- Karolinska Institutet (SE)
- Corresponding author
- Zierath, Juleen R.
- ORCID
- Zierath, Juleen R.
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2012-03-15
- Volume
- 302
- Issue
- 6
- Pages
- E731-E739
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2112563343
- Cited by
- 137
- References
- 53
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 10 · 2023: 7 · 2022: 6 · 2021: 10 · 2020: 11 · 2019: 7 · 2018: 13 · 2017: 13 · 2016: 7 · 2015: 11 · 2014: 15 · 2013: 15 · 2012: 6
- FWCI
- 6.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mitochondrial respiration, insulin resistance, type 2 diabetes, obesity, db/db mice, skeletal muscle, liver, PGC-1α, TFAM, mitochondrial dynamics, mitochondrial fission, mitochondrial biogenesis, fatty acid oxidation, mitochondrial complex I
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Animal Nutritional Physiological Phenomena, Blood Glucose, Diabetes Mellitus, Experimental, Diabetes Mellitus, Type 2, DNA-Binding Proteins, Glycogen, Glycolysis, High Mobility Group Proteins, Insulin Resistance, Mice, Inbred C57BL, Mice, Obese, Mitochondria, Mitochondria, Liver, Mitochondria, Muscle, Obesity, Oxygen Consumption, Transcription Factors, Triglycerides, Blotting, Western, Trans-Activators, Mice, Inbred NOD, Cell Lineage, Mice, Real-Time Polymerase Chain Reaction
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