Cited by 524Metabolism, Diabetes, and CancerMitochondrial Function and PathologyDiabetes Treatment and Management

The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.

Thiazolidinediones, Like Metformin, Inhibit Respiratory Complex I

Open access

Brunmair, Barbara, Staniek, Katrin, Gras, Florian, Scharf, Nicole, Althaym, Aleksandra, Clara, Renate, Roden, Michael, Gnaiger, Erich, Nohl, Hans, Waldhäusl, Werner, Fürnsinn, Clemens·2004·Diabetes

DOI 10.2337/diabetes.53.4.1052

Open this paper in CoChat — free account Open PDF

Abstract

Metformin and thiazolidinediones (TZDs) are believed to exert their antidiabetic effects via different mechanisms. As evidence suggests that both impair cell respiration in vitro, this study compared their effects on mitochondrial functions. The activity of complex I of the respiratory chain, which is known to be affected by metformin, was measured in tissue homogenates that contained disrupted mitochondria. In homogenates of skeletal muscle, metformin and TZDs reduced the activity of complex I (30 mmol/l metformin, −15 ± 2%; 100 μmol/l rosiglitazone, −54 ± 7; and 100 μmol/l pioglitazone, −12 ± 4; P < 0.05 each). Inhibition of complex I was confirmed by reduced state 3 respiration of isolated mitochondria consuming glutamate + malate as substrates for complex I (30 mmol/l metformin, −77 ± 1%; 100 μmol/l rosiglitazone, −24 ± 4; and 100 μmol/l pioglitazone, −18 ± 5; P < 0.05 each), whereas respiration with succinate feeding into complex II was unaffected. In line with inhibition of complex I, 24-h exposure of isolated rat soleus muscle to metformin or TZDs reduced cell respiration and increased anaerobic glycolysis (glucose oxidation: 270 μmol/l metformin, −30 ± 9%; 9 μmol/l rosiglitazone, −25 ± 8; and 9 μmol/l pioglitazone, −45 ± 3; lactate release: 270 μmol/l metformin, +84 ± 12; 9 μmol/l rosiglitazone, +38 ± 6; and 9 μmol/l pioglitazone, +64 ± 11; P < 0.05 each). As both metformin and TZDs inhibit complex I activity and cell respiration in vitro, similar mitochondrial actions could contribute to their antidiabetic effects.

Integrity signals

Registry

Crossref · 10.2337/diabetes.53.4.1052

Cites

39 of 39 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity
Yamauchi, T., Kamon, J., Waki, H., Terauchi, Y., Kubota, N., Hara, K., Mori, Y., Ide, T., Murakami, K., Tsuboyama-Kasaoka, N., et al. (2001) · Nature Medicine · doi:10.1038/90984 · Cited by 4,915
Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain
OWEN, M. R., DORAN, E., & HALESTRAP, A. P. (2000) · Biochemical Journal · doi:10.1042/bj3480607 · Cited by 2,157
Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I
El-Mir, M.-Y., Nogueira, V., Fontaine, E., Avéret, N., Rigoulet, M., & Leverve, X. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.223 · Cited by 1,399
PPARγ: a Nuclear Regulator of Metabolism, Differentiation, and Cell Growth
Rosen, E. D., & Spiegelman, B. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100034200 · Cited by 1,178
The Anti-diabetic Drugs Rosiglitazone and Metformin Stimulate AMP-activated Protein Kinase through Distinct Signaling Pathways
Fryer, L. G. D., Patel, A. P., & Carling, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202489200 · Cited by 1,035
Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation
Tomas, E., Tsao, T.-S., Saha, A. K., Murrey, H. E., Zhang, C. C., Itani, S. I., Lodish, H. F., & Ruderman, N. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222657499 · Cited by 973
A Role for AMP-Activated Protein Kinase in Contraction- and Hypoxia-Regulated Glucose Transport in Skeletal Muscle
Mu, J., Brozinick, J. T., Valladares, O., Bucan, M., & Birnbaum, M. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00251-9 · Cited by 924
Metformin Increases AMP-Activated Protein Kinase Activity in Skeletal Muscle of Subjects With Type 2 Diabetes
Musi, N., Hirshman, M. F., Nygren, J., Svanfeldt, M., Bavenholm, P., Rooyackers, O., Zhou, G., Williamson, J. M., Ljunqvist, O., Efendic, S., et al. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2074 · Cited by 806

Show all 39 references

Sorted by citations

AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism
Kahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799
Cellular and molecular mechanisms of metformin: an overview
Viollet, B., Guigas, B., Garcia, N. S., Leclerc, J., Foretz, M., & Andreelli, F. (2012) · Clinical Science · doi:10.1042/cs20110386 · Cited by 1,720
Metformin: from mechanisms of action to therapies
Foretz, M., Guigas, B., Bertrand, L., Pollak, M., & Viollet, B. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.09.018 · Cited by 1,501
Metformin improves healthspan and lifespan in mice
Martin-Montalvo, A., Mercken, E. M., Mitchell, S. J., Palacios, H. H., Mote, P. L., Scheibye-Knudsen, M., Gomes, A. P., Ward, T. M., Minor, R. K., Blouin, M.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3192 · Cited by 1,445
The AMP-activated protein kinase pathway – new players upstream and downstream
Hardie, D. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01540 · Cited by 1,163
AMPK activators: mechanisms of action and physiological activities
Kim, J., Yang, G., Kim, Y., Kim, J., & Ha, J. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.16 · Cited by 817
AMP-Activated Protein Kinase – Development of the Energy Sensor Concept
Hardie, D. G., Hawley, S. A., & Scott, J. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108944 · Cited by 813
Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation
Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773
Mitochondrial dysfunction in Nash: causes, consequences and possible means to prevent it
Begriche, K., Igoudjil, A., Pessayre, D., & Fromenty, B. (2006) · Mitochondrion · doi:10.1016/j.mito.2005.10.004 · Cited by 753
AMPK: a key regulator of energy balance in the single cell and the whole organism
Hardie, D. G. (2008) · International Journal of Obesity · doi:10.1038/ijo.2008.116 · Cited by 727
Mechanisms of insulin resistance in obesity
Ye, J. (2013) · Frontiers of Medicine · doi:10.1007/s11684-013-0262-6 · Cited by 699
Metformin-associated lactic acidosis: current perspectives on causes and risk
DeFronzo, R., Fleming, G. A., Chen, K., & Bicsak, T. A. (2016) · Metabolism · doi:10.1016/j.metabol.2015.10.014 · Cited by 658
Circumventing the Crabtree Effect: Replacing Media Glucose with Galactose Increases Susceptibility of HepG2 Cells to Mitochondrial Toxicants
Marroquin, L. D., Hynes, J., Dykens, J. A., Jamieson, J. D., & Will, Y. (2007) · Toxicological Sciences · doi:10.1093/toxsci/kfm052 · Cited by 632
PI3K/AKT, MAPK and AMPK signalling: protein kinases in glucose homeostasis
Schultze, S. M., Hemmings, B. A., Nießen, M., & Tschopp, O. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002109 · Cited by 553
Berberine and Its More Biologically Available Derivative, Dihydroberberine, Inhibit Mitochondrial Respiratory Complex I
Turner, N., Li, J.-Y., Gosby, A., To, S. W. C., Cheng, Z., Miyoshi, H., Taketo, M. M., Cooney, G. J., Kraegen, E. W., James, D. E., et al. (2008) · Diabetes · doi:10.2337/db07-1552 · Cited by 535
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534
Mitochondrial dysfunction and insulin resistance: an update
Montgomery, M. K., & Turner, N. A. (2014) · Endocrine Connections · doi:10.1530/ec-14-0092 · Cited by 549
AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle
Hardie, D. G., & Sakamoto, K. (2006) · Physiology · doi:10.1152/physiol.00044.2005 · Cited by 536
Role of Skeletal Muscle in Insulin Resistance and Glucose Uptake
Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive Physiology · doi:10.1002/cphy.c190029 · Cited by 494
AMP‐activated protein kinase in the regulation of hepatic energy metabolism: from physiology to therapeutic perspectives
Viollet, B., Guigas, B., Leclerc, J., Hébrard, S., Lantier, L., Mounier, R., Andréelli, F., & Foretz, M. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01970.x · Cited by 498
Molecular mechanism of action of metformin: old or new insights?
Rena, G., Pearson, E. R., & Sakamoto, K. (2013) · Diabetologia · doi:10.1007/s00125-013-2991-0 · Cited by 479
AMPK activation: a therapeutic target for type 2 diabetes?
Saha, A. K., Coughlan, K. A., Valentine, R. J., & Ruderman, N. B. (2014) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s43731 · Cited by 458
Mitochondrial dysfunction in type 2 diabetes mellitus: an organ-based analysis
Pinti, M. V., Fink, G. K., Hathaway, Q. A., Durr, A. J., Kunovac, A., & Hollander, J. M. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00314.2018 · Cited by 447
The significance of mitochondrial toxicity testing in drug development
Dykens, J. A., & Will, Y. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.07.013 · Cited by 419
AMP-Activated Protein Kinase as a Drug Target
Hardie, D. G. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105304 · Cited by 411
Antidiabetic Activities of Triterpenoids Isolated from Bitter Melon Associated with Activation of the AMPK Pathway
Tan, M.-J., Ye, J.-M., Turner, N. A., Hohnen-Behrens, C., Ke, C., Tang, C., Chen, T., Weiß, H., Gesing, E.-R., Rowland, A., et al. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.01.013 · Cited by 410
AMP-Activated Protein Kinase: A Target for Drugs both Ancient and Modern
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.08.019 · Cited by 385
Hydroxycinnamic acid derivatives: a potential class of natural compounds for the management of lipid metabolism and obesity
Alam, M. A., Subhan, N., Hossain, H., Hossain, M., Reza, H. M., Rahman, M., & Ullah, M. O. (2016) · Nutrition & Metabolism · doi:10.1186/s12986-016-0080-3 · Cited by 389
Metformin in cancer: translational challenges
Dowling, R. J. O., Niraula, S., Stambolic, V., & Goodwin, P. J. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0007 · Cited by 371
Development of protein kinase activators: AMPK as a target in metabolic disorders and cancer
Fogarty, S., & Hardie, D. G. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.012 · Cited by 357
Mitochondrial Adaptation in Nonalcoholic Fatty Liver Disease: Novel Mechanisms and Treatment Strategies
Sunny, N. E., Bril, F., & Cusi, K. J. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.11.006 · Cited by 327
Thiazolidinediones are acute, specific inhibitors of the mitochondrial pyruvate carrier
Divakaruni, A. S., Wiley, S. E., Rogers, G. W., Andreyev, A. Y., Petrosyan, S., Loviscach, M., Wall, E. A., Yadava, N., Heuck, A. P., Ferrick, D. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303360110 · Cited by 308
The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress
Kim, K. H., Son, J. M., Benayoun, B. A., & Lee, C. D. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.06.008 · Cited by 318
Modulation of the oxidative stress and inflammatory response by PPAR-γ agonists in the hippocampus of rats exposed to cerebral ischemia/reperfusion
Collino, M., Aragno, M., Mastrocola, R., Gallicchio, M., Rosa, A. C., Dianzani, C., Danni, O., Thiemermann, C., & Fantozzi, R. (2005) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.11.049 · Cited by 300
Activation of AMPK attenuates neutrophil proinflammatory activity and decreases the severity of acute lung injury
Zhao, X., Zmijewski, J. W., Lorne, E., Liu, G., Park, Y.-J., Tsuruta, Y., & Abraham, E. H. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90210.2008 · Cited by 303
AMPK as a mediator of hormonal signalling
Lim, C. T., Kola, B., & Korbonits, M. (2009) · Journal of Molecular Endocrinology · doi:10.1677/jme-09-0063 · Cited by 304
AMP-activated protein kinase: an emerging drug target to regulate imbalances in lipid and carbohydrate metabolism to treat cardio-metabolic diseases
Srivastava, R. A. K., Pinkosky, S. L., Filippov, S. I., Hanselman, J. C., Cramer, C. T., & Newton, R. S. (2012) · Journal of Lipid Research · doi:10.1194/jlr.r025882 · Cited by 308
Hyperactivation of oxidative mitochondrial metabolism in epithelial cancer cells in situ
Whitaker‐Menezes, D., Martinez‐Outschoorn, U., Flomenberg, N., Birbe, R., Witkiewicz, A. K., Howell, A., Pavlides, S., Tsirigos, A., Ertel, A., Pestell, R. G., et al. (2011) · Cell Cycle · doi:10.4161/cc.10.23.18151 · Cited by 295
Metformin Activates AMP-Activated Protein Kinase in Primary Human Hepatocytes by Decreasing Cellular Energy Status
Stephenne, X., Foretz, M., Taleux, N., van der Zon, G. C., Sokal, E., Hue, L., Viollet, B., & Guigas, B. (2011) · Diabetologia · doi:10.1007/s00125-011-2311-5 · Cited by 287
AMP-activated protein kinase: maintaining energy homeostasis at the cellular and whole-body levels
Hardie, D. G. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161148 · Cited by 281
Thiazolidinediones can rapidly activate AMP-activated protein kinase in mammalian tissues
LeBrasseur, N. K., Kelly, M., Tsao, T.-S., Farmer, S. R., Saha, A. K., Ruderman, N. B., & Tomas, E. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00453.2005 · Cited by 276
Receptor-independent actions of PPAR thiazolidinedione agonists: Is mitochondrial function the key?
Feinstein, D. L., Spagnolo, A., Akar, C., Weinberg, G., Murphy, P., Gavrilyuk, V., & Russo, C. D. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.03.033 · Cited by 275
Mitochondrial Quality Control as a Therapeutic Target
Suliman, H. B., & Piantadosi, C. A. (2015) · Pharmacological Reviews · doi:10.1124/pr.115.011502 · Cited by 267
Metformin Prevents High-Glucose–Induced Endothelial Cell Death Through a Mitochondrial Permeability Transition-Dependent Process
Detaille, D., Guigas, B., Chauvin, C., Batandier, C., Fontaine, E., Wiernsperger, N., & Leverve, X. (2005) · Diabetes · doi:10.2337/diabetes.54.7.2179 · Cited by 263
Induction of mitochondrial dysfunction as a strategy for targeting tumour cells in metabolically compromised microenvironments
Zhang, X., Fryknäs, M., Hernlund, E., Fayad, W., Milito, A. D., Olofsson, M. H., Gogvadze, V. G., Dang, L. H., Påhlman, S., Kunz‐Schughart, L. A., et al. (2014) · Nature Communications · doi:10.1038/ncomms4295 · Cited by 263
The diabetes medication Canagliflozin reduces cancer cell proliferation by inhibiting mitochondrial complex-I supported respiration
Villani, L. A., Smith, B. K., Marcinko, K., Ford, R. J., Broadfield, L. A., Green, A. E., Houde, V. P., Muti, P. C., Tsakiridis, T. K., & Steinberg, G. R. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.08.014 · Cited by 247
Molecular Mechanisms of Adipogenesis: The Anti-adipogenic Role of AMP-Activated Protein Kinase
Ahmad, B., Serpell, C. J., Fong, I. L., & Wong, E. H. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00076 · Cited by 260
Adipose-specific deletion of TFAM increases mitochondrial oxidation and protects mice against obesity and insulin resistance
Vernochet, C., Mourier, A., Bezy, O., Macotela, Y., Boucher, J., Rardin, M. J., An, D., Lee, K. Y., Ilkayeva, O. R., Zingaretti, C. M., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.016 · Cited by 245
Metformin Activates AMP Kinase through Inhibition of AMP Deaminase
Ouyang, J., Parakhia, R. A., & Ochs, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121806 · Cited by 251
Neuroprotective Role of Antidiabetic Drug Metformin Against Apoptotic Cell Death in Primary Cortical Neurons
El‐Mir, M., Détaille, D., R-Villanueva, G., Delgado‐Esteban, M., Guigas, B., Attia, S., Fontaine, E. M., Almeida, Á., & Leverve, X. M. (2007) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-9002-1 · Cited by 243
Skeletal muscle mitochondria as a target to prevent or treat type 2 diabetes mellitus
Hesselink, M. K. C., Schrauwen-Hinderling, V., & Schrauwen, P. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.104 · Cited by 242
Mitochondrial Biogenesis: A Therapeutic Target for Neurodevelopmental Disorders and Neurodegenerative Diseases
Uittenbogaard, M. N., & Chiaramello, A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305224906 · Cited by 246
Metformin inhibits mitochondrial adaptations to aerobic exercise training in older adults
Konopka, A. R., Laurin, J. L., Schoenberg, H. M., Reid, J. J., Castor, W. M., Wolff, C. A., Musci, R. V., Safairad, O. D., Linden, M. A., Biela, L. M., et al. (2019) · Aging Cell · doi:10.1111/acel.12880 · Cited by 238
The Mammalian Target of Rapamycin Pathway Regulates Nutrient-Sensitive Glucose Uptake in Man
Krebs, M., Brunmair, B., Brehm, A., Artwohl, M., Szendroedi, J., Nowotny, P., Roth, E., Fürnsinn, C., Promintzer, M., Anderwald, C., et al. (2007) · Diabetes · doi:10.2337/db06-1016 · Cited by 230
Self-citation
Salidroside ameliorates insulin resistance through activation of a mitochondria‐associated AMPK / PI3K / A kt/ GSK 3β pathway
Zheng, T., Yang, X., Wu, D., Xing, S., Bian, F., Li, W., Chi, J., Bai, X., Wu, G., Chen, X., et al. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13120 · Cited by 230
Biguanide-induced mitochondrial dysfunction yields increased lactate production and cytotoxicity of aerobically-poised HepG2 cells and human hepatocytes in vitro
Dykens, J. A., Jamieson, J., Marroquin, L., Nadanaciva, S., Billis, P. A., & Will, Y. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.08.013 · Cited by 220
The key role of growth hormone-insulin-IGF-1 signaling in aging and cancer
Anisimov, V. N., & Bartke, A. (2013) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2013.01.005 · Cited by 192
Pioglitazone treatment activates AMP-activated protein kinase in rat liver and adipose tissue in vivo
Saha, A. K., Avilucea, P. R., Ye, J.-M., Assifi, M. M., Kraegen, E. W., & Ruderman, N. B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.120 · Cited by 220
Role of AMP‐activated protein kinase in the metabolic syndrome and in heart disease
Hardie, D. G. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.018 · Cited by 221
Aging networks in Caenorhabditis elegans : AMP‐activated protein kinase ( aak‐2 ) links multiple aging and metabolism pathways
Curtis, R., O'Connor, G., & DiStefano, P. S. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00205.x · Cited by 220
AMPK and autophagy in glucose/glycogen metabolism
Ha, J., Guan, K., & Kim, J. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2015.08.002 · Cited by 219
Metformin protects the ischemic heart by the Akt-mediated inhibition of mitochondrial permeability transition pore opening
Bhamra, G. S., Hausenloy, D. J., Davidson, S. M., Carr, R. D., Paiva, M. S. A., Wynne, A. M., Mocanu, M. M., & Yellon, D. M. (2007) · Basic Research in Cardiology · doi:10.1007/s00395-007-0691-y · Cited by 211
Mitochondrial disease and endocrine dysfunction
Chow, J. C. K., Rahman, J., Achermann, J. C., Dattani, M., & Rahman, S. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.151 · Cited by 217
Structure–function analysis of NEET proteins uncovers their role as key regulators of iron and ROS homeostasis in health and disease
Tamir, S., Paddock, M. L., Darash-Yahana-Baram, M., Holt, S. H., Sohn, Y. S., Agranat-Tamir, L., Michaeli, D., Stofleth, J. T., Lipper, C. H., Morcos, F., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.014 · Cited by 198
Flavonoids and type 2 diabetes: Evidence of efficacy in clinical and animal studies and delivery strategies to enhance their therapeutic efficacy
Hussain, T., Tan, B., Murtaza, G., Liu, G., Rahu, N., Kalhoro, M. S., Kalhoro, D. H., Adebowale, T. O., Mazhar, M. U., Rehman, Z. U., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104629 · Cited by 208
Potential Therapeutic Benefits of Strategies Directed to Mitochondria
Camara, A. K. S., Lesnefsky, E. J., & Stowe, D. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2788 · Cited by 199
Metabolism and mitochondria in polycystic kidney disease research and therapy
Padovano, V., Podrini, C., Boletta, A., & Caplan, M. J. (2018) · Nature Reviews Nephrology · doi:10.1038/s41581-018-0051-1 · Cited by 182
The Role of AMPK Activation for Cardioprotection in Doxorubicin-Induced Cardiotoxicity
Timm, K. N., & Tyler, D. J. (2020) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-020-06941-x · Cited by 192
Role of AMP Kinase and PPARδ in the Regulation of Lipid and Glucose Metabolism in Human Skeletal Muscle
Krämer, D. K., Al-Khalili, L., Guigas, B., Leng, Y., Garcia-Roves, P. M., & Krook, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702329200 · Cited by 180
AMP-activated protein kinase: a cellular energy sensor with a key role in metabolic disorders and in cancer
Hardie, D. G. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390001 · Cited by 180
Drug-induced mitochondrial toxicity
Chan, K., Truong, D., Shangari, N., & O'Brien, P. J. (2005) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.1.4.655 · Cited by 176
Mitochondrial Respiratory Complex I Regulates Neutrophil Activation and Severity of Lung Injury
Żmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., Siegal, G. P., & Abraham, E. H. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200710-1602oc · Cited by 167
Mitochondrial impairment by PPAR agonists and statins identified via immunocaptured OXPHOS complex activities and respiration
Nadanaciva, S., Dykens, J. A., Bernal, A. J., Capaldi, R., & Will, Y. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.06.003 · Cited by 166
AMP-activated protein kinase pathway: a potential therapeutic target in cardiometabolic disease
Wong, A., Howie, J., Petrie, J. R., & Lang, C. C. (2009) · Clinical Science · doi:10.1042/cs20080066 · Cited by 170
Targeting AMP-activated protein kinase as a novel therapeutic approach for the treatment of metabolic disorders
Viollet, B., Mounier, R., Leclerc, J., Yazigi, A., Foretz, M., & Andréelli, F. (2007) · Diabetes & Metabolism · doi:10.1016/j.diabet.2007.10.004 · Cited by 168
The role of mitochondria in pharmacotoxicology: A reevaluation of an old, newly emerging topic
Scatena, R., Bottoni, P., Botta, G., Martorana, G. E., & Giardina, B. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00314.2006 · Cited by 163
Mitochondrial coupling defect in Charcot–Marie–Tooth type 2A disease
Loiseau, D., Chevrollier, A., Verny, C., Guillet, V., Guéguen, N., de Crescenzo, M. P., Ferré, M., Malinge, M., Guichet, A., Nicolas, G., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21086 · Cited by 156
Insulin Resistance and Mitochondrial Dysfunction
González-Franquesa, A., & Patti, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_25 · Cited by 160
Metformin inhibits mitochondrial permeability transition and cell death: a pharmacological in vitro study
Guigas, B., Détaille, D., Chauvin, C., Batandier, C., Oliveira, F. D., Fontaine, E. M., & Leverve, X. M. (2004) · Biochemical Journal · doi:10.1042/bj20040885 · Cited by 153
Mitochondrial Approaches to Protect Against Cardiac Ischemia and Reperfusion Injury
Camara, A. K. S., Bienengraeber, M., & Stowe, D. F. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00013 · Cited by 155
Metformin potentiates the effects of paclitaxel in endometrial cancer cells through inhibition of cell proliferation and modulation of the mTOR pathway
Hanna, R. K., Zhou, C., Malloy, K., Sun, L., Zhong, Y., Gehrig, P. A., & Bae-Jump, V. L. (2012) · Gynecologic Oncology · doi:10.1016/j.ygyno.2012.01.009 · Cited by 150
Neuronal ROS signaling rather than AMPK/sirtuin-mediated energy sensing links dietary restriction to lifespan extension
Schmeisser, S., Priebe, S., Groth, M., Monajembashi, S., Hemmerich, P. H., Guthke, R., Platzer, M., & Ristow, M. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.02.002 · Cited by 147
Cardioprotection by metabolic shut-down and gradual wake-up
Burwell, L. S., Nadtochiy, S. M., & Brookes, P. S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.026 · Cited by 146
Exercise-induced AMPK activity in skeletal muscle: Role in glucose uptake and insulin sensitivity
Friedrichsen, M., Mortensen, B., Pehmøller, C., Birk, J. B., & Wojtaszewski, J. F. P. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.013 · Cited by 143
Metformin for aging and cancer prevention
Anisimov, V. N. (2010) · Aging · doi:10.18632/aging.100230 · Cited by 142
Exercise and metformin counteract altered mitochondrial function in the insulin-resistant brain
Ruegsegger, G. N., Vanderboom, P. M., Dasari, S., Klaus, K. A., Kabiraj, P., McCarthy, C. B., Lucchinetti, C. F., & Nair, K. S. (2019) · JCI Insight · doi:10.1172/jci.insight.130681 · Cited by 141
AMP-activated protein kinase: A remarkable contributor to preserve a healthy heart against ROS injury
Marino, A., Hausenloy, D. J., Andreadou, I., Horman, S., Bertrand, L., & Beauloye, C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.047 · Cited by 140
Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity
Luo, X., Wu, J., Jing, S., & Yan, L. (2016) · Aging and Disease · doi:10.14336/ad.2015.0702 · Cited by 145
Metformin Beyond Diabetes: Pleiotropic Benefits of Metformin in Attenuation of Atherosclerosis
Forouzandeh, F., Salazar, G., Patrushev, N. A., Xiong, S., Hilenski, L. L., Fei, B., & Alexander, R. W. (2014) · Journal of the American Heart Association · doi:10.1161/jaha.114.001202 · Cited by 129
The Role of Metformin in Controlling Oxidative Stress in Muscle of Diabetic Rats
Vilela, D. D., Peixoto, L. G., Teixeira, R. R., Baptista, N. B., Caixeta, D. C., de Souza, A. V., Machado, H. L., Pereira, M. N., Silva, R. S., & Espíndola, F. S. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/6978625 · Cited by 134
Oxidative Reactive Species in Cell Injury: Mechanisms in Diabetes Mellitus and Therapeutic Approaches
Fridlyand, L. E., & Philipson, L. H. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1363.019 · Cited by 122
Nanoparticle Effects on Stress Response Pathways and Nanoparticle–Protein Interactions
Cameron, S. J., Sheng, J., Hosseinian, F. S., & Willmore, W. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147962 · Cited by 126
AMPK in cardiac fibrosis and repair: Actions beyond metabolic regulation
Daskalopoulos, E. P., Dufeys, C., Bertrand, L., Beauloye, C., & Horman, S. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.01.001 · Cited by 121
Mitochondrial dysfunction in non-alcoholic fatty liver disease and insulin resistance: Cause or consequence?
García‐Ruiz, C., Baulies, A., Marí, M., García-Rovés, P. M., & Fernández-Checa, J. C. (2013) · Free Radical Research · doi:10.3109/10715762.2013.830717 · Cited by 119
Effects of rosiglitazone on the liver histology and mitochondrial function in ob/ob mice†
García‐Ruíz, I., Rodríguez‐Juan, C., Díaz-Sanjuán, T., Martínez, M. Á., Muñoz‐Yagüe, T., & Solis-Herruzo, J. A. (2007) · Hepatology · doi:10.1002/hep.21687 · Cited by 124
The Thiazolidinedione Pioglitazone Alters Mitochondrial Function in Human Neuron-Like Cells
Ghosh, S., Patel, N., Rahn, D. A., McAllister, J., Sadeghi, S., Horwitz, G., Berry, D., Wang, K. X., & Swerdlow, R. H. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.033845 · Cited by 119
Fenofibrate Impairs Rat Mitochondrial Function by Inhibition of Respiratory Complex I
Brunmair, B., Lest, A., Staniek, K., Gras, F., Scharf, N., Roden, M., Nohl, H., Waldhäusl, W. K., & Fürnsinn, C. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.068312 · Cited by 114
Self-citation
The role of mitochondria in the aetiology of insulin resistance and type 2 diabetes
Martin, S. D., & McGee, S. L. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.019 · Cited by 117
Troglitazone causes acute mitochondrial membrane depolarisation and an AMPK-mediated increase in glucose phosphorylation in muscle cells
Konrad, D., Rudich, A., Bilan, P. J., Patel, N., Richardson, C., Witters, L. A., & Klip, A. (2005) · Diabetologia · doi:10.1007/s00125-005-1713-7 · Cited by 114
Emerging roles of cardiolipin remodeling in mitochondrial dysfunction associated with diabetes, obesity, and cardiovascular diseases
Shi, Y. (2010) · Journal of Biomedical Research · doi:10.1016/s1674-8301(10)60003-6 · Cited by 119

Authors: Brunmair, B., Staniek, K., Gras, F., Scharf, N., Althaym, A., Clara, R., Roden, M., Gnaiger, E., Nohl, H., Waldhäusl, W., & Fürnsinn, C.
Affiliations: University of Vienna (AT)
University of Veterinary Medicine Vienna (AT)
Universität Innsbruck (AT)
Department of Medicine III, Division of Endocrinology & Metabolism, University of Vienna, Vienna, Austria
ORCID: Brunmair, Barbara
Roden, Michael
Gnaiger, Erich
Venue: Diabetes
Publisher: American Diabetes Association
Published: 2004-04-01
Volume: 53
Issue: 4
Pages: 1052-1059
ISSN: 0012-1797 (ISSN-L)
1939-327X
DOI: 10.2337/diabetes.53.4.1052
OpenAlex: W2403578638
Cited by: 521
References: 39
Citations by year: 2026: 6 · 2025: 9 · 2024: 15 · 2023: 10 · 2022: 14 · 2021: 15 · 2020: 33 · 2019: 25 · 2018: 16 · 2017: 27 · 2016: 37 · 2015: 30 · 2014: 40 · 2013: 33 · 2012: 29
FWCI: 7.64
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Diabetes (publishedVersion)
PubMed (publishedVersion)
Funders: Pfizer
Austrian Science Fund
Universität Wien
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Keywords: thiazolidinediones, metformin, mitochondrial complex I, mitochondrial respiration, rosiglitazone, pioglitazone, skeletal muscle, anaerobic glycolysis, glucose oxidation, lactate release, antidiabetic mechanism, type 2 diabetes
MeSH terms: Rosiglitazone, Pioglitazone, Animals, Energy Metabolism, Hypoglycemic Agents, Male, Metformin, Mitochondria, Oxygen Consumption, Potassium Chloride, Rotenone, Rats, Sprague-Dawley, Muscle, Skeletal, Electron Transport Complex I, Thiazolidinediones, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Thiazolidinediones, Like Metformin, Inhibit Respiratory Complex I

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks