Cited by 154Mitochondrial Function and PathologyMetabolism, Diabetes, and CancerAdipose Tissue and Metabolism

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The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance

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Pagel-Langenickel, Ines, Bao, Jianjun, Pang, Liyan, Sack, Michael N.·2010·Endocrine Reviews

DOI 10.1210/er.2009-0003PMC PMC2852205

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Abstract

Multiple organs contribute to the development of peripheral insulin resistance, with the major contributors being skeletal muscle, liver, and adipose tissue. Because insulin resistance usually precedes the development of type 2 diabetes mellitus (T2DM) by many years, understanding the pathophysiology of insulin resistance should enable development of therapeutic strategies to prevent disease progression. Some subjects with mitochondrial genomic variants/defects and a subset of lean individuals with hereditary predisposition to T2DM exhibit skeletal muscle mitochondrial dysfunction early in the course of insulin resistance. In contrast, in the majority of subjects with T2DM the plurality of evidence implicates skeletal muscle mitochondrial dysfunction as a consequence of perturbations associated with T2DM, and these mitochondrial deficits then contribute to subsequent disease progression. We review the affirmative and contrarian data regarding skeletal muscle mitochondrial biology in the pathogenesis of insulin resistance and explore potential therapeutic options to intrinsically modulate mitochondria as a strategy to combat insulin resistance. Furthermore, an overview of restricted molecular manipulations of skeletal muscle metabolic and mitochondrial biology offers insight into the mitochondrial role in metabolic substrate partitioning and in promoting innate adaptive and maladaptive responses that collectively regulate peripheral insulin sensitivity. We conclude that skeletal muscle mitochondrial dysfunction is not generally a major initiator of the pathophysiology of insulin resistance, although its dysfunction is integral to this pathophysiology and it remains an intriguing target to reverse/delay the progressive perturbations synonymous with T2DM.

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Gene Ontology: tool for the unification of biology
Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D., Butler, H., Cherry, J. M., Davis, A. P., Dolinski, K., Dwight, S. S., Eppig, J. T., et al. (2000) · Nature Genetics · doi:10.1038/75556 · Cited by 43,206
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Ihaka, R., & Gentleman, R. (1996) · Journal of Computational and Graphical Statistics · doi:10.1080/10618600.1996.10474713 · Cited by 11,747
PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
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(2008) · New England Journal of Medicine · doi:10.1056/nejmoa0802987 · Cited by 7,397
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Brownlee, M. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1615 · Cited by 5,339
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Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290

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Retracted
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DNA damage in normal-weight obese syndrome measured by Comet assay
Tomasello, B., Malfa, G. A., Galvano, F., & Renis, M. (2010) · Mediterranean Journal of Nutrition and Metabolism · doi:10.1007/s12349-010-0035-6 · Cited by 26
Benfotiamine increases glucose oxidation and downregulates NADPH oxidase 4 expression in cultured human myotubes exposed to both normal and high glucose concentrations
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Measuring the acute effect of insulin infusion on ATP turnover rate in human skeletal muscle using phosphorus‐31 magnetic resonance saturation transfer spectroscopy
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FGF19 alleviates palmitate-induced atrophy in C2C12 cells by inhibiting mitochondrial overload and insulin resistance
Sun, Y., Yang, Z.-X., Ren, F., & Fang, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.04.186 · Cited by 22
Chronic Renal Failure, Cachexia, and Ghrelin
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RETRACTED: Mitochondrial pathophysiology and type 2 diabetes mellitus
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Retracted
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Ohlendieck, K. (2012) · Journal of Nutrition and Metabolism · doi:10.1155/2012/893876 · Cited by 20
Raspberry supplementation reduces lipid accumulation and improves insulin sensitivity in skeletal muscle of mice fed a high-fat diet
Zou, T., Kang, Y., Wang, B., de Avila, J. M., You, J., Zhu, M. J., & Du, ‬. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103572 · Cited by 20
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Memon, A. A., Vats, S., Sundquist, J., Li, Y., & Sundquist, K. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0100 · Cited by 19
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Liao, B., & Xu, Y. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-011-1892-5 · Cited by 19
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Wang, H., Arias, E. B., Yu, C. S., Verkerke, A. R. P., & Cartee, G. D. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glx099 · Cited by 18
Profiling of human myotubes reveals an intrinsic proteomic signature associated with type 2 diabetes
Al‐Khalili, L., Barbosa, T. D. C., Östling, J., Massart, J., Katayama, M., Nyström, A., Oscarsson, J., & Zierath, J. R. (2013) · Translational Proteomics · doi:10.1016/j.trprot.2013.12.002 · Cited by 18
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Yang, X., Ding, W., Chen, Z., Lai, K., & Liu, Y. (2024) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.3762 · Cited by 18
Differences in the Triglyceride to HDL-Cholesterol Ratio between Palestinian and Israeli Adults
Weiss, R., Nassar, H., Sinnreich, R., & Kark, J. D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116617 · Cited by 17
Relationships between plasma lactate, plasma alanine, genetic variations in lactate transporters and type 2 diabetes in the Japanese population
Higuchi, I., Kimura, Y., Kobayashi, M., Narumi, K., Furugen, A., Miyoshi, H., Nakamura, A., Yamada, T., Atsumi, T., & Iseki, K. (2019) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2019.10.001 · Cited by 17
The Mitochondrial Proteomic Signatures of Human Skeletal Muscle Linked to Insulin Resistance
Kruse, R., Sahebekhtiari, N., & Højlund, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155374 · Cited by 19
Impact of dyslipidemia in the development of cardiovascular complications: Delineating the potential therapeutic role of coenzyme Q10
Mthembu, S. X. H., Orlando, P., Silvestri, S., Ziqubu, K., Mazibuko-Mbeje, S. E., Mabhida, S. E., Nyambuya, T. M., Nkambule, B. B., Muller, C. J. F., Basson, A. K., et al. (2022) · Biochimie · doi:10.1016/j.biochi.2022.08.018 · Cited by 18
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Yeon, M., Seo, E., Lee, J., & Jun, H. (2023) · Antioxidants · doi:10.3390/antiox12010137 · Cited by 17
Tissue-Specific Effects of Bariatric Surgery Including Mitochondrial Function
Dankel, S. N., Staalesen, V., Bjørndal, B., Berge, R. K., Mellgren, G., & Burri, L. (2011) · Journal of Obesity · doi:10.1155/2011/435245 · Cited by 16
Effects of raising muscle glycogen synthesis rate on skeletal muscle ATP turnover rate in type 2 diabetes
Lim, E. L., Hollingsworth, K. G., Smith, F. E., Thelwall, P. E., & Taylor, R. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00278.2011 · Cited by 16

Authors: Pagel-Langenickel, I., Bao, J., Pang, L., & Sack, M. N.
Affiliations: Translational Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-1454
National Institutes of Health (US)
ORCID: Sack, Michael N.
Venue: Endocrine Reviews
Publisher: The Endocrine Society
Published: 2009-10-27
Volume: 31
Issue: 1
Pages: 25-51
ISSN: 0163-769X (ISSN-L)
1945-7189
DOI: 10.1210/er.2009-0003
PMC: PMC2852205
OpenAlex: W2161339546
Cited by: 154
References: 333
Citations by year: 2026: 6 · 2025: 5 · 2024: 6 · 2023: 6 · 2022: 5 · 2021: 3 · 2020: 13 · 2019: 7 · 2018: 8 · 2017: 8 · 2016: 11 · 2015: 7 · 2014: 15 · 2013: 17 · 2012: 11
FWCI: 0.94
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Endocrine Reviews (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Keywords: skeletal muscle insulin resistance, mitochondrial dysfunction, type 2 diabetes, peripheral insulin resistance, mitochondrial DNA variants, mitochondrial-targeted therapy, insulin sensitivity, skeletal muscle metabolism
MeSH terms: Animals, Diabetes Mellitus, Type 2, Humans, Insulin Resistance, Mitochondria, Muscle, Organ Specificity, Prediabetic State, Muscle, Skeletal, Metabolic Syndrome, Mitochondrial Diseases

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The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance

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