The DOI matches its Crossref record.
Physiological role of AMP-activated protein kinase (AMPK): insights from knockout mouse models
Abstract
AMP-activated protein kinase (AMPK) is viewed as a fuel sensor for glucose and lipid metabolism. To understand better the physiological role of the catalytic AMPK subunit isoforms, we generated two knockout mouse models with the α1 (AMPKα1−/−) and α2 (AMPKα2−/−) catalytic subunit genes deleted. No defect in glucose homoeostasis was observed in AMPKα1−/− mice. On the other hand, AMPKα2−/− mice presented high plasma glucose levels and low plasma insulin concentrations in the fed period and during the glucose tolerance test. Nevertheless, in isolated AMPKα2−/− pancreatic islets, glucose-stimulated insulin secretion was not affected. Surprisingly, AMPKα2−/− mice were insulin-resistant and had reduced muscle glycogen synthesis as assessed in vivo by the hyperinsulinaemic euglycaemic clamp procedure. Reduction of insulin sensitivity and glycogen synthesis were not dependent on the lack of AMPK in skeletal muscle, since mice expressing a dominant inhibitory mutant of AMPK in skeletal muscle were not affected and since insulin-stimulated glucose transport in incubated muscles in vitro was normal in AMPKα2−/− muscles. Furthermore, AMPKα2−/− mice have a higher sympathetic tone, as shown by increased catecholamine urinary excretion. Increased adrenergic tone could explain both decreased insulin secretion and insulin resistance observed in vivo in AMPKα2−/− mice. We suggest that the α2 catalytic subunit of AMPK plays a major role as a fuel sensor by modulating the activity of the autonomous nervous system in vivo.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“In contrast, AMPK α1 KO mice have normal AMPK T172 phosphorylation in skeletal muscle despite reduced α1 activity, showing that α2 AMPK is the predominant isoform contributing to AMPK activity in skeletal muscle [35].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [35]
Citations
Cited by
Sorted by citations
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
AMP-Activated Protein Kinase (AMPK) Controls the Aging Process via an Integrated Signaling Network
Salminen, A., & Kaarniranta, K. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2011.12.005 · Cited by 860
Management of cellular energy by the AMP‐activated protein kinase system
Hardie, D. G., Scott, J. W., Pan, D. A., & Hudson, E. R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00560-x · Cited by 868
Activation of the AMP-activated Protein Kinase by the Anti-diabetic Drug Metformin in Vivo
Zou, M., Kirkpatrick, S. S., Davis, B. J., Nelson, J. S., Wiles, W. G., Schlattner, U., Neumann, D., Brownlee, M., Freeman, M. B., & Goldman, M. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404421200 · Cited by 480
RetractedDavis, B. J., Xie, Z., Viollet, B., & Zou, M. (2006) · Diabetes · doi:10.2337/diabetes.55.02.06.db05-1064 · Cited by 465
“RESEARCH DESIGN AND METHODS Male AMPK-knockout (AMPK / ) mice (27), which had been cross-bred with C57BL6 mice, were bred from the animal house of the University of Tennessee Medical Center.”
MethodSelf-citationAMPK dysregulation promotes diabetes-related reduction of superoxide and mitochondrial function
Dugan, L. L., You, Y.-H., Ali, S. S., Diamond-Stanic, M. K., Miyamoto, S., Declèves, A., Andreyev, A. Y., Quach, T., Ly, S., Shekhtman, G., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66218 · Cited by 457
“…validate that AMPK is the critical enzyme responsible for regulating mitochondrial function in diabetic kidney disease, additional studies were performed with a model of progressive diabetic kidney disease (the F1 cross of DBA2J and C57BL/6J with Akita) (27, 28) and with the Ampka2 –/– mice (29).”
Self-citationMairet-Coello, G., Courchet, J., Pieraut, S., Courchet, V., Maximov, A., & Polleux, F. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.003 · Cited by 351
“Constitutive AMPKa1 KO mice (Prkaa1) (Viollet et al., 2003) were a kind gift from Dr.”
Obesity-related derangements in metabolic regulation
Muoio, D. M., & Newgard, C. B. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142512 · Cited by 345
Mackenzie, R., & Elliott, B. (2014) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s48260 · Cited by 322
Wang, S., Zhang, M., Liang, B., Xu, J., Xie, Z., Liu, C., Viollet, B., Yan, D., & Zou, M.-H. (2010) · Circulation Research · doi:10.1161/circresaha.109.212530 · Cited by 296
AMPK and Exercise: Glucose Uptake and Insulin Sensitivity
O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295
“In contrast, AMPK α1 KO mice have normal AMPK T172 phosphorylation in skeletal muscle despite reduced α1 activity, showing that α2 AMPK is the predominant isoform contributing to AMPK activity in skeletal muscle [35].”
BackgroundA role for AMP-activated protein kinase in diabetes-induced renal hypertrophy
Lee, M.-J., Féliers, D., Mariappan, M. M., Sataranatarajan, K., Mahimainathan, L., Musi, N., Foretz, M., Viollet, B., Weinberg, J. M., Choudhury, G. G., et al. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00278.2006 · Cited by 287
“On activation, AMPK inhibits energy-consuming reactions, such as synthesis of fatty acids and sterols (55), and activates ATP-generating processes, such as fatty acid oxidation (39).”
BackgroundSelf-citationMechanisms of animal diapause: recent developments from nematodes, crustaceans, insects, and fish
Hand, S. C., Denlinger, D. L., Podrabsky, J. E., & Roy, R. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00250.2015 · Cited by 287
“In most organisms AMPK signaling is essential (24, 108, 187); however, in C.”
BackgroundStatins Activate AMP-Activated Protein Kinase In Vitro and In Vivo
Sun, W., Lee, T., Zhu, M., Gu, C., Wang, Y., Zhu, Y., & Shyy, J. Y.-J. (2006) · Circulation · doi:10.1161/circulationaha.106.630194 · Cited by 264
Li, J., Zeng, Z., Viollet, B., Ronnett, G. V., & McCullough, L. D. (2007) · Stroke · doi:10.1161/strokeaha.107.490904 · Cited by 216
Self-citationMa, T., Chen, Y., Vingtdeux, V., Zhao, H., Viollet, B., Marambaud, P., & Klann, E. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1694-14.2014 · Cited by 191
“Therefore, we examined A -induced impairments in LTP in mice that lack the 2- subunit of AMPK (Viollet et al., 2003a,b).”
MethodSelf-citationRegulation of erythrocyte survival by AMP‐activated protein kinase
Föller, M., Sopjani, M., Koka, S., Gu, S., Mahmud, H., Wang, K., Floride, E., Schleicher, E. D., Schulz, E., Münzel, T. F., et al. (2008) · The FASEB Journal · doi:10.1096/fj.08-121772 · Cited by 203
“The ampk / mice have been described previously (27).”
AMP-activated protein kinase (AMPK) activation regulates in vitro bone formation and bone mass
Shah, M., Kola, B., Bataveljic, A., Arnett, T. R., Viollet, B., Saxon, L., Korbonits, M., & Chenu, C. (2010) · Bone · doi:10.1016/j.bone.2010.04.596 · Cited by 196
“No known metabolic changes were detected in AMPK α1-deficient mice that could explain our skeletal defects[50,71].”
BackgroundSelf-citationCancer Drug Discovery and Development
Humphrey, J. S., Price, K., Gupta, E., Baxter, A. R. W., Bird, J., Sonnichsen, D. S., & Naglich, J. G. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-325-5_21 · Cited by 195
Keerthana, C. K., Rayginia, T. P., Shifana, S. C., Anto, N. P., Kalishwaralal, K., Isakov, N., & Anto, R. J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1114582 · Cited by 206
Zhu, Y. P., Brown, J. R., Sağ, D., Zhang, L., & Suttles, J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401024 · Cited by 197
The Role of AMPK and mTOR in Nutrient Sensing in Pancreatic β-Cells
Gleason, C. E., Lu, D., Witters, L. A., Newgard, C. B., & Birnbaum, M. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610631200 · Cited by 182
Self-citationMetabolic alterations and targeted therapies in prostate cancer
Flavin, R., Zadra, G., & Loda, M. F. (2010) · The Journal of Pathology · doi:10.1002/path.2809 · Cited by 178
“Moreover, a recent study revealed an association between polymorphisms in the PRKAA2 gene (encoding the α2 subunit of AMPK, which is responsible for the MS phenotype) [58] and susceptibility to insulin resistance and diabetes in the Japanese population [59].”
Jørgensen, S. B., Treebak, J. T., Viollet, B., Schjerling, P., Vaulont, S., Wojtaszewski, J. F. P., & Richter, E. A. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00243.2006 · Cited by 181
“The 2-KO mice have been described previously (18, 19, 45, 46).”
MethodSelf-citationViollet, 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
“This is in part due to the development of transgenic and knockout (KO) mouse models that have made it possible to study distinct physiological functions for AMPK isoforms [4].”
BackgroundSelf-citationEffects of AMP-Activated Protein Kinase in Cerebral Ischemia
Li, J., & McCullough, L. D. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.255 · Cited by 165
Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1
Amodeo, G. A., Rudolph, M. J., & Tong, L. (2007) · Nature · doi:10.1038/nature06127 · Cited by 164
Wu, S., Wu, Y., Wu, T.-P., & Wei, Y. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.034 · Cited by 164
Zhu, M. J., Han, B., Tong, J., Ma, C., Kimzey, J. M., Underwood, K. R., Xiao, Y., Hess, B. W., Ford, S. P., Nathanielsz, P. W., et al. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.149633 · Cited by 158
“Knockout of the AMPKα2 catalytic subunit in mice leads to insulin resistance (Viollet et al. 2003).”
BackgroundSchulz, E., Dopheide, J. F., Schuhmacher, S., Thomas, S. R., Chen, K., Daiber, A., Wenzel, P., Münzel, T. F., & Keaney, J. F. (2008) · Circulation · doi:10.1161/circulationaha.108.784289 · Cited by 150
Cellular energy sensing and signaling by AMP-activated protein kinase
Winder, W. W., & Thomson, D. M. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0008-7 · Cited by 142
“Studies on alpha1 and alpha2 AMPK knockout mice have failed to show a consistent deficiency in muscle insulin sensitivity [184, 185], although whole body insulin sensitivity seems to be reduced with the alpha2 knockout.”
Nutrient sensing and metabolic decisions
Lindsley, J. E., & Rutter, J. P. (2004) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpc.2004.06.014 · Cited by 146
“Indeed, they found that AMPKa2 / mice excrete increased levels of catecholamines (Viollet et al., 2003b).”
InfluentialSun, Y., Zhou, S., Guo, H., Zhang, J., Ma, T., Zheng, Y., Zhang, Z., & Cai, L. (2019) · Metabolism · doi:10.1016/j.metabol.2019.154002 · Cited by 145
Akt activation: A potential strategy to ameliorate insulin resistance
Zhang, Z., Liu, H., & Liu, J. (2017) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2017.10.004 · Cited by 143
Effects of cannabinoid receptors on skeletal muscle oxidative pathways
Cavuoto, P., McAinch, A. J., Hatzinikolas, G., Cameron‐Smith, D., & Wittert, G. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.12.038 · Cited by 142
LKB1 and AMPK in cell polarity and division
Williams, T., & Brenman, J. E. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.01.008 · Cited by 141
Timpani, C. A., Hayes, A., & Rybalka, E. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.08.015 · Cited by 134
“cise and hypoglycaemia) stimulates ATP-producing pathways to restore energy homeostasis [128].”
BackgroundWilliams, T., Courchet, J., Viollet, B., Brenman, J. E., & Polleux, F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013660108 · Cited by 123
“To assess the role of AMPKα during cortical development, we used transgenic mice that were ubiquitously inactivated for the AMPKα1 gene (AMPKα1) (11) and conditionally inactivated for AMPKα2 (AMPKα2) (12, 13).”
Self-citationSuburu, J., & Chen, Y. Q. (2012) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2012.03.003 · Cited by 134
“AMPK directly inhibits ACACA, HMG-CoA reductase, and SREBP-1, Prostaglandins Other Lipid Mediat.”
BackgroundInfluentialThe Role of Autophagy in Skeletal Muscle Diseases
Xia, Q., Huang, X., Huang, J., Zheng, Y., March, M., Li, J., & Wei, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.638983 · Cited by 137
Pu, P., Wang, X.-A., Salim, M., Zhu, L., Wang, L., Chen, K.-J., Xiao, J., Deng, W., Shi, H., Jiang, H., et al. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.002 · Cited by 122
AMP-activated protein kinase modulates tau phosphorylation and tau pathology in vivo
Domise, M., Didier, S., Marinangeli, C., Zhao, H., Chandakkar, P., Buée, L., Viollet, B., Davies, P., Marambaud, P., & Vingtdeux, V. (2016) · Scientific Reports · doi:10.1038/srep26758 · Cited by 124
Self-citationLoss of Lkb1 in Adult β Cells Increases β Cell Mass and Enhances Glucose Tolerance in Mice
Fu, A., Ng, A. C., Depatie, C., Wijesekara, N., He, Y., Wang, G., Bardeesy, N. M., Scott, F. W., Touyz, R. M., Wheeler, M. B., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.008 · Cited by 120
“Although Ampk a1 knockout mice display normal glucose tolerance (Viollet et al., 2003), this may be due to the combined effects of loss of Ampk a1 from other tissues that influence glucose metabolism.”
BackgroundRequirement of the ATM/p53 Tumor Suppressor Pathway for Glucose Homeostasis
Armata, H. L., Golebiowski, D., Jung, D. Y., Ko, H. J., Kim, J. K., & Sluss, H. K. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00347-10 · Cited by 121
“In addition, AMPK -deficient mice develop muscle insulin resistance (45), which is not observed in p53 mice.”
BackgroundAMP-activated protein kinase pathway and bone metabolism
Jeyabalan, J., Shah, M., Viollet, B., & Chenu, C. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0306 · Cited by 120
Self-citationGuigas, B., Taleux, N., Foretz, M., Détaille, D., Andréelli, F., Viollet, B., & Hue, L. (2007) · Biochemical Journal · doi:10.1042/bj20070105 · Cited by 122
Self-citationSchulz, E., Anter, E., Zou, M., & Keaney, J. F. (2005) · Circulation · doi:10.1161/circulationaha.105.546812 · Cited by 114
AMPKα1 deficiency amplifies proinflammatory myeloid APC activity and CD40 signaling
Carroll, K. C., Viollet, B., & Suttles, J. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0313157 · Cited by 115
Self-citationPpm1E is an in cellulo AMP-activated protein kinase phosphatase
Voß, M., Paterson, J., Kelsall, I. R., Martín‐Granados, C., Hastie, C. J., Peggie, M. W., & Cohen, P. T. W. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.08.010 · Cited by 111
AMP-Activated Protein Kinase and Metabolic Control
Viollet, B., & Andréelli, F. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-17214-4_13 · Cited by 113
Self-citationBone Cell Bioenergetics and Skeletal Energy Homeostasis
Riddle, R. C., & Clemens, T. L. (2017) · Physiological Reviews · doi:10.1152/physrev.00022.2016 · Cited by 108
Xin, X., Zhou, L., Reyes, C. M., Liu, F., & Dong, L. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00427.2010 · Cited by 101
AMP-Activated Kinase Restricts Rift Valley Fever Virus Infection by Inhibiting Fatty Acid Synthesis
Moser, T. S., Schieffer, D., & Cherry, S. R. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002661 · Cited by 102
Knauf, C., Cani, P. D., Ait-Belgnaoui, A., Bénani, A., Dray, C., Cabou, C., Colom, A., Uldry, M., Rastrelli, S., Sabatier, E., et al. (2008) · Endocrinology · doi:10.1210/en.2008-0180 · Cited by 100
Self-citationRole of AMP‐Activated Protein Kinase in Cancer Therapy
Rehman, G., Shehzad, A., Khan, A. L., & Hamayun, M. (2014) · Archiv der Pharmazie · doi:10.1002/ardp.201300402 · Cited by 107
Sun, G., Tarasov, A. I., McGinty, J., McDonald, A., Xavier, G. D. S., Gorman, T., Marley, A. E., French, P. M. W., Parker, H., Gribble, F. M., et al. (2010) · Diabetologia · doi:10.1007/s00125-010-1692-1 · Cited by 99
“The existence of two separate AMPKα subunit genes has so far hindered investigations of the role AMPK activity plays in controlling glucose homeostasis in mammals, since the unconditional deletion of both isoforms leads to early embryonic lethality in mice [11].”
BackgroundSelf-citationRole of AMPK in pancreatic beta cell function
Fu, A., Eberhard, C. E., & Screaton, R. A. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.020 · Cited by 103
Lin, V. C.-H., Tsai, Y.-C., Lin, J.-N., Fan, L.-L., Pan, M., Ho, C., Wu, J., & Way, T. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf301499e · Cited by 90
Slattery, M. L., Herrick, J. S., Lundgreen, A., Fitzpatrick, F. A., Curtin, K., & Wolff, R. K. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq142 · Cited by 89
AMP-Activated Protein Kinase: A New Beta-Cell Glucose Sensor?
Leclerc, I., & Rutter, G. A. (2004) · Diabetes · doi:10.2337/diabetes.53.suppl_3.s67 · Cited by 91
“It might be mentioned, however, that whereas inactivation of the 2 isoform of AMPK catalytic subunit in mice is without effect on insulin secretion from isolated islets (but leads to glucose intolerance due to elevated catecholamine levels) (78), inactivation of the 1 complex has no effect on either parameter (79).”
BackgroundJiang, X., Tan, H., Teng, S., Chan, Y.-T., Wang, D., & Wang, N. (2019) · Cancers · doi:10.3390/cancers11050647 · Cited by 85
“Each of the subunits has two or three isoforms (α1 and α2; β1 and β2; γ1, γ2 and γ3) that are encoded by different genes [24].”
Liu, C., Liang, B., Wang, Q., Wu, J., & Zou, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102491 · Cited by 81
RetractedTargeting AMPK for cardiac protection: Opportunities and challenges
Kim, M., & Tian, R. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.12.004 · Cited by 83
“There are a number of genetic models for reduced AMPK activity including deletions of α1, α2, β1, β2 or γ3 subunit of AMPK in mice [60,77-79].”
BackgroundSlattery, M. L., & Fitzpatrick, F. A. (2009) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-08-0191 · Cited by 82
“Overall, LKB1 is a prominent, widely expressed AMPK kinase that governs whole-body insulin sensitivity via this signaling pathway (32, 33).”
BackgroundLi, Z., Guo, H., Li, J. X., Ma, T., Zhou, S., Zhang, Z., Miao, L., & Cai, L. (2020) · Clinical Science · doi:10.1042/cs20191088 · Cited by 80
Insulin resistance and fuel homeostasis: the role of AMP‐activated protein kinase
Hegarty, B. D., Turner, N. A., Cooney, G. J., & Kraegen, E. W. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01968.x · Cited by 78
“In order to address this issue, animals have been generated with genetic manipulations to knockout global a1 or a2 AMPK expression (Viollet et al. 2003a,b), or to abolish total AMPK activity specifically within the skeletal muscle (Mu et al. 2001).”
BackgroundOllila, S., Domènech‐Moreno, E., Laajanen, K., Wong, I. P. L., Tripathi, S., Pentinmikko, N., Gao, Y., Yan, Y., Niemelä, E. H., Wang, T. C., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci93597 · Cited by 75
Self-citationThe AMP-regulated kinase family: Enigmatic targets for diabetes therapy
Rutter, G. A., & Leclerc, I. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.05.020 · Cited by 75
“…inactivated for AMPK2 throughout the body show defective glucose tolerance as a result of altered sympathetic tone, but insulin secretion from isolated islets is normal (Viollet et al., 2003b); mice inactivated for AMPK1 displayed no obvious defects in glucose homeostasis (Viollet et al., 2003a).”
Function of the master energy regulator adenosine monophosphate‐activated protein kinase in stroke
Manwani, B., & McCullough, L. D. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23207 · Cited by 76
“AMPK a2 also modulates the activity of the autonomic nervous system, insofar as AMPK a2 knockout mice (but not AMPK a1 knockout mice) have increased catecholamine urinary excretion and increased adrenergic tone (Viollet et al., 2003).”
BackgroundSlattery, M. L., John, E. M., Torres-Mejı́a, G., Lundgreen, A., Herrick, J. S., Baumgartner, K. B., Hines, L. M., Stern, M. C., & Wolff, R. K. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs163 · Cited by 71
“Central to the CHIEF pathway are tumor suppressor genes, such as STK11 or LKB1 (serine/threonine protein kinase 11), which governs whole-body insulin sensitivity (6,7); mTOR (mammalian Target of Rapamycin), which is involved in normal energy homeostasis and inhibition of tumor growth (8); and PTEN (phosphatase tensin…”
BackgroundTherapeutic Potential of AMP-Activated Protein Kinase in Alzheimer’s Disease
Wang, X., Zimmermann, H. R., & Ma, T. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181043 · Cited by 64
Changes in Components of Energy Regulation in Mouse Cortex with Increases in Wakefulness
Nikonova, E. V., Naidoo, N. N., Zhang, L., Romer, M. A., Cater, J. R., Scharf, M. T., Galante, R. J., & Pack, A. I. (2010) · SLEEP · doi:10.1093/sleep/33.7.889 · Cited by 68
New Strategies in Prostate Cancer: Targeting Lipogenic Pathways and the Energy Sensor AMPK
Zadra, G., Priolo, C., Patnaik, A., & Loda, M. F. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-1955 · Cited by 69
Zhuo, L., Fu, B., Bai, X., Zhang, B., Wu, L., Cui, J., Cui, S., Ribao, W., Chen, X., & Cai, G. (2011) · Cellular Physiology and Biochemistry · doi:10.1159/000330077 · Cited by 69
Diet, obesity and diabetes: a current update
Walker, C. G., Zariwala, M. G., Holness, M. J., & Sugden, M. C. (2006) · Clinical Science · doi:10.1042/cs20060150 · Cited by 62
Neurath, K. M., Keough, M. P., Mikkelsen, T., & Claffey, K. P. (2006) · Glia · doi:10.1002/glia.20326 · Cited by 67
“Mouse genetic deletion studies have shown that AMPKa2-null mice demonstrate glucose intolerance and reduced insulin sensitivity, while the AMPKa1-null mice do not show any appreciable alterations (Viollet et al., 2003a; Viollet et al., 2003b).”
BackgroundGregor, M., Zeöld, A., Oehler, S., Andrä, K., FUCHS, P. C., Weigel, G., Hardie, D. G., & Wiche, G. (2006) · Journal of Cell Science · doi:10.1242/jcs.02891 · Cited by 65
“Bar, 10 m. Jo ur na l o f C el l S ci en ce 1869Plectin-AMPK scaffolding changes in expression levels of subunits have been described in AMPK 2 knockout mice (Viollet et al., 2003).”
BackgroundInfluentialMcCarthy, A. D., Cortizo, A. M., & Sedlinsky, C. (2016) · World Journal of Diabetes · doi:10.4239/wjd.v7.i6.122 · Cited by 58
Lefort, N., St.-Amand, E., Morasse, S., Côté, C. H., & Marette, A. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90362.2008 · Cited by 57
Wu, K., Huang, C., Shi, X., Chen, F., Xu, Y., Pan, Y., Luo, Z., & Liu, X. (2016) · Scientific Reports · doi:10.1038/srep38716 · Cited by 57
Xu, T., Guo, L., Wang, P., Song, J., Le, Y., Viollet, B., & Miao, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051217 · Cited by 58
“No evidence indicates inflammation in AMPKa2 mice, either [43].”
BackgroundSelf-citationAMP-activated kinase is a regulator of fibroblast growth factor 23 production
Glosse, P., Feger, M., Mutig, K., Chen, H., Hirche, F., Hasan, A. A., Gaballa, M. M. S., Hocher, B., Lang, F. J. W., & Föller, M. (2018) · Kidney International · doi:10.1016/j.kint.2018.03.006 · Cited by 56
Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1
Rudolph, M. J., Amodeo, G. A., Bai, Y., & Tong, L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.181 · Cited by 56
“AMP-activated protein kinase (AMPK) is a master metabolic regulator and an important target for drug development against diabetes, obesity, and other diseases [1–5].”
BackgroundEid, H. M., Ouchfoun, M., Brault, A., Vallerand, D., Musallam, L., Arnason, J. T., & Haddad, P. S. (2014) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2014/645812 · Cited by 55
AMP-activated Protein Kinase Regulates β-Catenin Transcription via Histone Deacetylase 5
Zhao, J., Yue, W., Zhu, M. J., & Du, . (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199372 · Cited by 56
Dong, K., Wu, M., Liu, X., Huang, Y., Zhang, D., Wang, Y., Yan, L., & Shi, D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.007 · Cited by 54
Regulation of class III (Vps34) PI3Ks
Yan, Y., & Backer, J. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350239 · Cited by 57
Beall, C., Piipari, K., Al‐Qassab, H., Smith, M. A., Parker, N., Carling, D., Viollet, B., Withers, D. J., & Ashford, M. L. J. (2010) · Biochemical Journal · doi:10.1042/bj20100231 · Cited by 54
Self-citationChemical Genetics of Acetyl-CoA Carboxylases
Zu, X., Zhong, J., Luo, D., Tan, J., Zhang, Q., Wu, Y., Liu, J., Cao, R., Wen, G., & Cao, D. (2013) · Molecules · doi:10.3390/molecules18021704 · Cited by 54
Insight on Transcriptional Regulation of the Energy Sensing AMPK and Biosynthetic mTOR Pathway Genes
Sukumaran, A., Choi, K., & Dasgupta, B. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00671 · Cited by 62
Horikoshi, M., Hara, K., Ohashi, J., Miyake, K., Tokunaga, K., Ito, C., Kasuga, M., Nagai, R., & Kadowaki, T. (2006) · Diabetes · doi:10.2337/diabetes.55.04.06.db05-0727 · Cited by 52
AMPK Localization: A Key to Differential Energy Regulation
Afinanisa, Q., Cho, M., & Seong, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222010921 · Cited by 58
Gorovits, N., & Charron, M. J. (2003) · Biochemistry and Molecular Biology Education · doi:10.1002/bmb.2003.494031030227 · Cited by 52
Han, Y., He, M., Marin, T., Shen, H., Wang, W., Lee, T.-Y., Hong, H.-C., Jiang, Z., Garland, T., Shyy, J. Y.-J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103982118 · Cited by 53
Optimum arginine requirement of juvenile black sea bream,Sparus macrocephalus
Zhou, F., Xiong, W., Xiao, J., Shao, Q., Bergo, O. N., Hua, Y., & Chai, X. (2010) · Aquaculture Research · doi:10.1111/j.1365-2109.2009.02474.x · Cited by 50
AMPK Alpha 1-Induced RhoA Phosphorylation Mediates Vasoprotective Effect of Estradiol
Gayard, M., Guilluy, C., Rousselle, A., Viollet, B., Henrion, D., Pacaud, P., Loirand, G., & Rolli‐Derkinderen, M. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.228304 · Cited by 50
Self-citationYang, Y., Zhao, Z., Liu, Y., Kang, X., Zhang, H., & Meng, M. (2014) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.12723 · Cited by 50
Aging, senescence and mitochondria: the PGC-1/ERR axis
Vernier, M., & Giguère, V. (2020) · Journal of Molecular Endocrinology · doi:10.1530/jme-20-0196 · Cited by 52
Föller, M., Jaumann, M., Dettling, J., Saxena, A., Pakladok, T., Muñoz, C., Ruth, P., Sopjani, M., Seebohm, G., Rüttiger, L., et al. (2012) · The FASEB Journal · doi:10.1096/fj.12-208132 · Cited by 48
“The ampk / mice have been described previously (53).”
BackgroundNeuroprotective effects of statins against amyloid β-induced neurotoxicity
Huang, C., Li, H., & Lin, C. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.226379 · Cited by 50
“The involvement of AMPK in diabetes mellitus is demonstrated by insulin resistance, with associated high levels of plasma glucose and low levels of insulin in mice with ablated AMPK (Viollet et al., 2003).”
Background
Metadata
- Authors
- Viollet, B., Andreelli, F., Jørgensen, S. B., Perrin, C., Flamez, D., Mu, J., Wojtaszewski, J. F. P., Schuit, F. C., Birnbaum, M., Richter, E., Burcelin, R., & Vaulont, S.
- Affiliations
- Institut Cochin (FR)
- Institut Cochin, Dpt GDPM, 24 rue du faubourg Saint-Jacques 75014 Paris, France
- University of Copenhagen (DK)
- Centre National de la Recherche Scientifique (FR)
- Diabetes Research Center, Brussels, Belgium
- Howard Hughes Medical Institute (US)
- Corresponding author
- Viollet, B.
- Vaulont, S.
- ORCID
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2003-02-01
- Volume
- 31
- Issue
- 1
- Pages
- 216-219
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2060836453
- Cited by
- 241
- References
- 0
- Citations by year
- 2026: 2 · 2024: 3 · 2023: 2 · 2022: 8 · 2021: 13 · 2020: 8 · 2019: 8 · 2018: 11 · 2017: 10 · 2016: 12 · 2015: 8 · 2014: 19 · 2013: 19 · 2012: 21
- FWCI
- 2.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- AMPK, glucose homeostasis, insulin resistance, glucose-stimulated insulin secretion, pancreatic islets, muscle glycogen synthesis, insulin sensitivity, sympathetic nervous system, catecholamine excretion, knockout mice
- MeSH terms
- Animals, Glucose Tolerance Test, Glycogen, Mice, Transgenic, Models, Biological, Multienzyme Complexes, Mutation, Protein Serine-Threonine Kinases, Mice, Knockout, Muscle, Skeletal, Catalytic Domain, Mice, AMP-Activated Protein Kinases
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
