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The 5′-AMP-activated Protein Kinase γ3 Isoform Has a Key Role in Carbohydrate and Lipid Metabolism in Glycolytic Skeletal Muscle
Open accessAbstract
5'-AMP-activated protein kinase (AMPK) is a metabolic stress sensor present in all eukaryotes. A dominant missense mutation (R225Q) in pig PRKAG3, encoding the muscle-specific gamma3 isoform, causes a marked increase in glycogen content. To determine the functional role of the AMPK gamma3 isoform, we generated transgenic mice with skeletal muscle-specific expression of wild type or mutant (225Q) mouse gamma3 as well as Prkag3 knockout mice. Glycogen resynthesis after exercise was impaired in AMPK gamma3 knock-out mice and markedly enhanced in transgenic mutant mice. An AMPK activator failed to increase skeletal muscle glucose uptake in AMPK gamma3 knock-out mice, whereas contraction effects were preserved. When placed on a high fat diet, transgenic mutant mice but not knock-out mice were protected against excessive triglyceride accumulation and insulin resistance in skeletal muscle. Transfection experiments reveal the R225Q mutation is associated with higher basal AMPK activity and diminished AMP dependence. Our results validate the muscle-specific AMPK gamma3 isoform as a therapeutic target for prevention and treatment of insulin resistance.
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“Interestingly, transgenic mice harboring the R225Q mutation in AMPK γ3 subunit have higher AMPK activity and glycogen levels and are protected from diet-induced insulin resistance [4], which is a likely effect of increased fatty acid oxidation and subsequent reduction in skeletal muscle lipids.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [4]
In the citing paper
“Whole-body γ3 KO mice have reduced AMPK activity at rest, during exercise and in response to fasting, but normal insulin sensitivity under basal conditions and glucose uptake during exercise [4,41].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [4]
In the citing paper
“Whole-body γ3 KO mice have reduced AMPK activity at rest, during exercise and in response to fasting, but normal insulin sensitivity under basal conditions and glucose uptake during exercise [4,41].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [4]
In the citing paper
“Although TBC1D1 expression or PAS phosphorylation was not assessed in skeletal muscle from β2 or γ3 KO mice, contraction-mediated glucose uptake was also normal [4,28], suggesting that the remaining subunit isoforms (likely contributing to maintained or elevated α1 AMPK activity) was sufficient to allow for normal glucose uptake.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [4]
In the citing paper
“AMPK α2 KO and α2 KD and α2iTg mice have normal or only modest reductions in glucose uptake during contractions [4,26,31,32,118-120].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [4]
In the citing paper
“It has been proposed that glycogen depletion and AMPK activation may play a role in insulin sensitizing effects of exercise given AMPK γ3 KO and α2 KD mice have impaired glycogen resynthesis following exercise [4,31].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [4]
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Items 201–300 of 317
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“Many mutations in the CBS domains also activate mtPPase, and some even reverse the effects of nucleotide from inhibition to activation (43), resembling the effects of mutations in cystathionine -synthase (44) and AMP-dependent protein kinase (45, 46).”
BackgroundSchönke, M., Myers, M. G., Zierath, J. R., & Björnholm, M. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2015 · Cited by 17
“Downregulation of AMPK activity in peripheral tissues reduces exercise capacity, worsens glucose tolerance, and promotes obesity and diabetes in several AMPK isoform-knockout or kinase-dead mouse models (7, 16, 39, 41, 42).”
InfluentialSelf-citationAMPKγ3 is dispensable for skeletal muscle hypertrophy induced by functional overload
Riedl, I., Osler, M. E., Björnholm, M., Egan, B., Nader, G. A., Chibalin, A., & Zierath, J. R. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00387.2015 · Cited by 16
Self-citationDiverse Signals Regulate Glucose Uptake into Skeletal Muscle
Wijesekara, N., Thong, F. S. L., Antonescu, C. N., & Klip, A. (2006) · Canadian Journal of Diabetes · doi:10.1016/s1499-2671(06)01006-9 · Cited by 16
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“However, several gain of function mutations in the AMPK subunits cause accumulation of glycogen in muscle and heart [10,11], but the mechanisms are not understood.”
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“Studies proved overexpression of AMPK in skeletal muscle tissue can increase fatty acid oxidation and prevent skeletal muscle lipid deposition induced by high-fat diet.[19] PGC-1α can regulate energy metabolism and induce mitochondrial biogenesis.”
BackgroundScheffler, T. L., Park, S., Roach, P. J., & Gerrard, D. E. (2016) · Physiological Reports · doi:10.14814/phy2.12802 · Cited by 15
Tobias, I. S., Lazauskas, K. K., Arevalo, J. A., Bagley, J. R., Brown, L. E., & Galpin, A. J. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00894.2017 · Cited by 14
AXIN1 knockout does not alter AMPK/mTORC1 regulation and glucose metabolism in mouse skeletal muscle
Li, J., Knudsen, J. R., Henríquez‐Olguín, C., Li, Z., Birk, J. B., Persson, K. W., Hellsten, Y., Offergeld, A., Jarassier, W., Grand, F. L., et al. (2021) · The Journal of Physiology · doi:10.1113/jp281187 · Cited by 14
“…is required for AMPK-stimulation of glucose uptake (Barnes et al. 2004; Jorgensen, 2004; Steinberg et al. 2010), insulin-sensitization post-exercise (Kjøbsted et al. 2017) and a range of other endurance exercise-mimicking adaptations (Barnes et al. 2004; Jørgensen et al. 2005; Nilsson et al. 2006).”
BackgroundZhao, C., Wang, C. F., Deng, X., Gao, Y., & Wu, C. (2006) · Journal of Animal Breeding and Genetics · doi:10.1111/j.1439-0388.2006.00607.x · Cited by 14
Xu, M., Li, X., Wang, J.-G., Du, P.-F., Hong, J., Gu, W., Zhang, Y., & Ning, G. (2005) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2005.06.012 · Cited by 17
Fine-tuning AMPK in physiology and disease using point-mutant mouse models
Ashraf, N., & Nostrand, J. L. V. (2024) · Disease Models & Mechanisms · doi:10.1242/dmm.050798 · Cited by 14
“First, the phenotypes of knock-in mice to AMPK knockout or knock-in controls should be compared, as can be done when comparing the high glycogen levels in the activating Ampkg3 R225Q knock-in mouse model with the lower glycogen levels in the phospho-mutant Mck-Fnip1 S220A mice (Barnes et al., 2004).”
BackgroundAMPK regulates the maintenance and remodelling of the neuromuscular junction
Ng, S. Y., Mikhail, A. I., Mattina, S. R., Mohammed, S. A., Khan, S., Desjardins, E. M., Lim, C., Phillips, S. M., Steinberg, G. R., & Ljubicic, V. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.102066 · Cited by 13
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Screening methods for AMP-activated protein kinase modulators: a patent review
Kim, J., Shin, J., & Ha, J. (2014) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2014.995626 · Cited by 13
“In line with this notion, increasing number of evidences has shown that inactivating mutations and genetic deletion of specific isoforms produced tissue-specific physiological results [109-111].”
BackgroundGaidhu, M. P., & Ceddia, R. B. (2009) · Clinical Lipidology · doi:10.2217/clp.09.30 · Cited by 12
A novel therapeutic approach to colorectal cancer in diabetes: role of metformin and rapamycin
Geagea, A. G., Rizzo, M., Jurjus, A. R., Cappello, F., Leone, A., Tomasello, G., Gracia, C., Kattar, S. A., Massaad-Massade, L., & Eid, A. A. (2019) · Oncotarget · doi:10.18632/oncotarget.26641 · Cited by 12
“In this context, observational studies have suggested that some anti-hyperglycemic agents like metformin, could decrease or prevent cancer risk [48] [49] could activate AMPK, a central regulator and an important target for controlling”
BackgroundRegulation of exercise-stimulated glucose uptake in skeletal muscle
Koh, H.-J. (2016) · Annals of Pediatric Endocrinology & Metabolism · doi:10.6065/apem.2016.21.2.61 · Cited by 12
Evaluation of the effects and mechanisms of bioactive components present in hypoglycemic plants
Bogle, I., & Mendes, M. J. S. (2015) · UCL Discovery (University College London) · Cited by 12
Viollet, B., & Foretz, M. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_18 · Cited by 14
“However, a slightly reduced basal and contraction‐stimulated rates of glucose uptake was evidenced in transgenic AMPK3 R225Q mutant mice (Barnes et al. 2004, Yu et al. 2006), suggesting that enhanced glycogen accumulation is not due to a single mechanism.”
BackgroundInfluentialKopietz, F., Rupar, K., Berggreen, C., Säll, J., Vertommen, D., Degerman, E., Rider, M. H., & Göransson, O. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00065.2020 · Cited by 11
Guo, Q., Wicks, J. C., Yen, C., Scheffler, T. L., Richert, B. T., Schinckel, A. P., Grant, A. L., & Gerrard, D. E. (2020) · Meat Science · doi:10.1016/j.meatsci.2020.108418 · Cited by 11
Pathways Involved In Lipid-Induced Insulin Resistance In Obesity
Watt, M. J., & Steinberg, G. R. (2007) · Future Lipidology · doi:10.2217/17460875.2.6.659 · Cited by 11
Ryder, J. W., Long, Y. C., Nilsson, E., Mahlapuu, M., & Zierath, J. R. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.090829 · Cited by 10
“AMPKγ 3 knockout mice are completely AICAR resistant for glucose transport; however, the effect of in vitro muscle contraction on glucose transport is preserved (Barnes et al. 2004).”
BackgroundInfluentialSelf-citationWu, L., Zhuang, Z., Jia, W., Li, Y., Lu, Y., Xu, M., Bai, H., Wang, Z., Chang, G., & Jiang, Y. (2024) · Poultry Science · doi:10.1016/j.psj.2024.104613 · Cited by 9
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An asparagine residue mediates intramolecular communication in nucleotide-regulated pyrophosphatase
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“PRKAG3, as the leading gene associated with overall breast cancer risk, also named as AMPKγ3, has been considered a potential target of cancer treatment due to its function in regulating glucose/lipid metabolism and skeletal muscle glycogen content (32,33).”
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Increased Hepatic Insulin Sensitivity in Mice Lacking Inhibitory Leptin Receptor Signals
Tom, R. Z., Sjögren, R. J. O., Vieira, E. C., Glund, S., Iglesias‐Gutiérrez, E., García-Rovés, P. M., Myers, M. G., & Björnholm, M. (2011) · Endocrinology · doi:10.1210/en.2010-0040 · Cited by 8
“Extensor digitorum longus (EDL) and soleus muscles were removed from anesthetized mice (avertin, 2,2,2-tribromo ethanol and tertiary amyl alcohol at 16 l/g body weight, ip), and in vitro 2-deoxyglucose transport was assessed as previously described (25).”
MethodMechanisms of exercise- and training-induced fatty acid oxidation in skeletal muscle
Miura, S., Tadaishi, M., Kamei, Y., & Ezaki, O. (2014) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.3.43 · Cited by 9
Role of the AMPKγ3 isoform in hypoxia-stimulated glucose transport in glycolytic skeletal muscle
Deshmukh, A. S., Glund, S., Tom, R. Z., & Zierath, J. R. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00125.2009 · Cited by 7
Self-citationLiu, L., Wang, B., He, Y., Tao, W., Liu, Z., & Wang, M. (2016) · Biological Trace Element Research · doi:10.1007/s12011-016-0890-1 · Cited by 7
Genetic Dissection of the Physiological Role of Skeletal Muscle in Metabolic Syndrome
Hagiwara, N. (2014) · New Journal of Science · doi:10.1155/2014/635146 · Cited by 8
“exhibited a more specific phenotype, mainly deficiency in glycogen synthesis after exercise [225], reflecting the highlevel expression of the γ3 subunit in glycolytic fibers [226].”
BackgroundSkeletal muscle lipid metabolism and the adipomuscular axis
Sugden, M. C., & Holness, M. J. (2006) · Future Lipidology · doi:10.2217/17460875.1.2.153 · Cited by 7
“In particular, the γ3 isoform has been suggested to play a role in the regulation of carbohydrate metabolism in muscle [37].”
BackgroundLKB1 suppresses KSHV reactivation and promotes primary effusion lymphoma progression
Li, G., Li, Y., Tang, X., Wang, L., Yue, S., He, S., & Li, T. (2024) · Journal of Virology · doi:10.1128/jvi.00604-24 · Cited by 6
Skeletal Muscle Adaptation to Exercise
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Self-citationRole of adenosine monophosphate-activated protein kinase in the control of energy homeostasis
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Biswas, D., Espino-González, E., Ahwazi, D., Freemantle, J. B., Ehrlich, A. M., Jomard, C., Brorson, J., Schou, A. N., Farup, J., Gondin, J., et al. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102294 · Cited by 5
“Deletion of any one of the three subunits, AMPK α 2 [23,33,34], AMPK β 2 [35,36], or AMPK γ 3 [8,37,38], abolishes this response.”
Zhou, Z., Zhao, J., de Cruz, C. R., Xu, H. T., Wang, L., & Xu, Q. (2023) · Fish Physiology and Biochemistry · doi:10.1007/s10695-023-01234-0 · Cited by 5
“It can regulate the metabolism of fatty acids, cholesterol, and glucose and affect nutrients’ metabolism through downstream proteins (Hayashi et al. 2000; Barnes et al. 2004).”
BackgroundJanzen, N. R., Whitfield, J., Murray‐Segal, L., Kemp, B. E., Hawley, J. A., & Hoffman, N. J. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.859246 · Cited by 5
“, 2020), chronic whole-body AMPK γ3 KO mice (Barnes et al., 2004), muscle-specific AMPK β1β2 KO (O’Neill et al.”
BackgroundWang, H., Zheng, A., Arias, E. B., & Cartee, G. D. (2022) · FACETS · doi:10.1139/facets-2021-0166 · Cited by 5
“The role of γ 3-AMPK could be evaluated using genetically modified mouse models that lack γ 3-AMPK expression (Barnes et al. 2004; Rhein et al. 2021).”
BackgroundVariation in the ovine PRKAG3 gene
Yang, G., Zhou, H., Wang, R., & Hickford, J. G. H. (2015) · Gene · doi:10.1016/j.gene.2015.05.021 · Cited by 5
Kokhan, A. S., Солдатов, А. А., Golovina, I. V., Bogdanovich, Y. V., Shalagina, N. E., & Rychkova, V. N. (2023) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s002209302306008x · Cited by 4
Effects of fibre type and diffusion distance on mouse skeletal muscle glycogen content in vitro
Søgaard, P., Szekeres, F. L. M., Holmström, M., Larsson, D., Harlén, M., García-Rovés, P. M., & Chibalin, A. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22223 · Cited by 4
“INCUBATION PROTOCOL In this study we have utilized a standard protocol for in vitro glucose uptake in isolated mouse skeletal muscle [Barnes et al., 2004; Terada et al., 2006].”
MethodLong, Y. C., & Zierath, J. R. (2005) · Diabetologia · doi:10.1007/s00125-005-0032-3 · Cited by 4
“Furthermore, AMPK induces fatty acid oxidation by direct phosphorylation of acetyl-CoA decarboxylase [2].”
BackgroundInfluentialSelf-citationAnashkin, V. A., Kirillova, E. A., Orlov, V. N., & Baykov, A. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115768 · Cited by 3
“A similar modulation of the regulation of cystathionine β -synthase by S-adenosyl methionine [7] and AMP-dependent protein kinase by AMP and ATP has been reported [4,22].”
BackgroundEffects of Acute Bouts of Swimming Exercise on AMPKα2 Expression in Mouse Skeletal Muscle
Wang, Y., & Zhang, Y. (2010) · Journal of Exercise Science & Fitness · doi:10.1016/s1728-869x(10)60002-0 · Cited by 3
“In vitro AICAR-incubated muscles from transgenic mice where reduction of AMPK signaling by either overexpressing a kinase-dead AMPKα2 or knocking out the catalytic α2 isoform could completely abolish AICAR-stimulated glucose uptake (Barnes et al. 2004; Jørgensen et al. 2004).”
MethodScheffler, T. L., & Gerrard, D. E. (2016) · Journal of Animal Science · doi:10.2527/jas.2015-0055 · Cited by 3
Spatial insulin signalling in isolated skeletal muscle preparations
Søgaard, P., Szekeres, F. L. M., García-Rovés, P. M., Larsson, D., Chibalin, A., & Zierath, J. R. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22470 · Cited by 3
“Instead, isolated skeletal muscles preparations are used to study the influence of insulin signalling on glucose uptake and utilisation [Holloszy et al., 1986; Wallberg-Henriksson et al., 1987; Bonen et al., 1994; Song et al., 1999; Wallberg-Henriksson and Zierath, 2001; Barnes et al., 2004].”
BackgroundMethodSelf-citationAssociation study of AMP-activated protein kinase subunit genes in polycystic ovary syndrome
Sproul, K., Jones, M. R., Azziz, R., & Goodarzi, M. O. (2009) · European Journal of Endocrinology · doi:10.1530/eje-09-0245 · Cited by 3
Ampk alpha2 T172 activation dictates exercise performance and energy transduction in skeletal muscle
Montalvo, R. N., Li, X., Many, G. M., Sagendorf, T. J., Yu, Q., Shen, W., Wase, N. V., Burgardt, A. R., Zhang, T., Gritsenko, M., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeb3338 · Cited by 5
“Previous combinations of deletion of the Ampk α 1/2, β 1/2, or γ 1/2/3 genes all caused disruption protein stoichiometry in Ampk holoenzyme and its protein complexes ( 30 , 37 – 39 ).”
Maintaining Energy Balance in Health and Disease: Role of the AMP-Activated Protein Kinase
Scott, J. W. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_9 · Cited by 2
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Contributions of AMP kinase to the Pathogenesis of Type 2 Diabetes and Neurodegenerative Diseases
Kodiha, M., Mahboubi, H., & Stochaj, U. (2013) · Wiley eBooks · doi:10.1002/9781118395318.ch22 · Cited by 2
Skeletal muscle AMP kinase as a target to prevent pathogenesis of Type 2 diabetes
Krook, A., Long, Y. C., & Zierath, J. R. (2007) · Expert Review of Endocrinology & Metabolism · doi:10.1586/17446651.2.4.477 · Cited by 2
Self-citationROLE OF AMPK SUBUNITS IN SKELETAL MUSCLE mTOR SIGNALING
Deshmukh, A. S., Treebak, J. T., Long, Y. C., Viollet, B., Zierath, J. R., & Ribosomal, S. (2008) · Cited by 2
Self-citationEskesen, N. O., Kjøbsted, R., Birk, J. B., Henriksen, N. S., Andersen, N. R., Ringholm, S., Pilegaard, H., Wojtaszewski, J. F. P., & Wojtaszewski, J. F. P. (2024) · Acta Physiologica · doi:10.1111/apha.14213 · Cited by 1
“18,23,24 In parallel, glycogen utilization during contractions was equal between genotypes (Figure S5E).”
InfluentialKwak, S. E., Wang, H., Pan, X., Duan, D., & Cartee, G. D. (2024) · The FASEB Journal · doi:10.1096/fj.202401859r · Cited by 1
Woodworth‐Hobbs, M. E. (2009) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.2812 · Cited by 1
“Because activation of AMPK decreases expression of genes involved in lipid synthesis (3), an increase in the phosphorylated:total AMPK ratio suggests that intramyocellular lipid content should be decreased with palmitate treatment.”
BackgroundAMPK and the Metabolic Syndrome
Viollet, B., & Andréelli, F. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch17 · Cited by 1
Structural and functional studies on nucleotide binding to AMP-activated protein kinase
Saiu, P. (2010) · UCL Discovery (University College London) · Cited by 1
Nutrient and energy sensing in skeletal muscle
Deshmukh, A. S. (2009) · Figshare · Cited by 1
Dissection of molecular basis on a causative mutation for ear size QTL on chromosome 7 in pigs
Duan, Y. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3932 · Cited by 1
Younis, S., Naboulsi, R., Wang, X., Cao, X., Larsson, M., Sargsyan, E., Bergsten, P., Welsh, N., & Andersson, L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/540914 · Cited by 1
Self-citationGlund, S. (2007) · Figshare
Skeletal muscle metabolic flexibility : The roles of AMP-activated protein kinase and calcineurin
Long, Y. C. (2007) · Figshare
Studies on exercise and glycogen re-synthesis in skeletal muscles of pigs with the PRKAG3 mutation
Granlund, A. (2011) · Epsilon Open Archive (Sveriges lantbruksuniversitet biblioteket (Swedish University of Agricultural Sciences))
Ahlsén, M. (2006) · Figshare
Insulin Signalling and TBC1D1 in skeletal muscle metabolism
Szekeres, F. L. M. (2011) · Figshare
Die Rolle der AMP-Kinase bei der Regulation des Vasotonus
Kreutz, C.-P. (2013) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.16547
Central and peripheral mechanisms regulating energy and glucose homeostasis
Tom, R. Z. (2013) · Figshare
Søgaard, P., Harlén, M., Long, Y. C., Szekeres, F. L. M., Barnes, B. R., Chibalin, A., & Zierath, J. R. (2010) · Journal of Biological Systems · doi:10.1142/s0218339010003494
Self-citationRegulation of metabolism and inflammation in liver and skeletal muscle
Nerstedt, A. (2013) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Molecular dissection of pathways regulating glucose and lipid metabolism using siRNA
Rune, A. (2009) · Figshare
L’AMP-activated protein kinase : de la régulation énergétique au syndrome métabolique
Andréelli, F., Bayen, É., Liaigre, A., Jacquier, D., Sebaaly, G., Foretz, M., Roussel, R., Marre, M., & Viollet, B. (2006) · Sang thrombose vaisseaux
Novel pharmaceutical approaches to regulate glucose homeostasis
Sundbom, M. (2010) · Figshare
Effects of AMPK Activation on Insulin Sensitivity and Metabolism
Tom, R. Z., García-Rovés, P. M., Sjögren, R. J. O., Jiang, L. Q., Holmström, M., Deshmukh, A. S., Vieira, E. C., Chibalin, A., Björnholm, M., & Zierath, J. R. (2014)
Self-citationPathways controlling metabolic and hypertrophic responses in skeletal muscle
Riedl, I. (2015) · Figshare
Postmortem metabolism in porcine skeletal muscle
England, E. M. (2015) · VTechWorks (Virginia Tech)
McFadden, J. W. (2009) · VTechWorks (Virginia Tech)
St-Amand, E. (2015) · Corpus Université Laval (Université Laval)
Effects of Postmeal Walking on Postprandial Glucose Control and Oxidative Stress
Knurick, J. R. (2015)
Investigating IL-15 Metabolic Impact and Its Mechanism of Action in Skeletal Muscle Cells
Nadeau, L. (2017) · uO Research (University of Ottawa) · doi:10.20381/ruor-20334
“AMPK plays quite an important role in promoting fatty acid oxidation as inducing a gain-of-function mutation in AMPKγ3 prevented obesity in mice by increasing fatty acid oxidation in skeletal muscle (Barnes et al. 2004).”
BackgroundVlavcheski, F. (2018) · Brock University Digital Repository (Brock University)
Detecting novel effects of exercise or AMPK activation in human skeletal muscle
Lassiter, D. G. (2018) · Figshare
Can exercise mitigate the negative metabolic effects associated with sleep loss
Saner, N. J. (2019) · Victoria University Research Repository (Victoria University)
Metadata
- Authors
- Barnes, B. R., Marklund, S., Steiler, T. L., Walter, M., Hjälm, Amarger, V., Mahlapuu, M., Leng, Y., Johansson, C., Galuska, D., Lindgren, K., Åbrink, M., Stapleton, D., Zierath, J. R., & Andersson, L.
- Affiliations
- Karolinska Institutet (SE)
- Swedish University of Agricultural Sciences (SE)
- Uppsala University (SE)
- Corresponding author
- Zierath, Juleen R.
- Andersson, Leif
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-09
- Volume
- 279
- Issue
- 37
- Pages
- 38441-38447
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2147553969
- Cited by
- 317
- References
- 37
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 9 · 2023: 7 · 2022: 4 · 2021: 8 · 2020: 15 · 2019: 15 · 2018: 9 · 2017: 14 · 2016: 21 · 2015: 17 · 2014: 21 · 2013: 17 · 2012: 10
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Svenska Forskningsrådet Formas
- Karolinska Institutet
- Vetenskapsrådet
- Uppsala Universitet
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
- Keywords
- AMPK, PRKAG3, skeletal muscle, glycogen resynthesis, physical activity, skeletal muscle glucose uptake, triglyceride accumulation, insulin resistance, high-fat diet, carbohydrate metabolism, lipid metabolism
- MeSH terms
- Animals, Blood Glucose, Glucose, Glycogen, Glycolysis, Insulin, Mice, Transgenic, Models, Genetic, Multienzyme Complexes, Protein Kinases, RNA, Messenger, Swine, Temperature, Transfection, Triglycerides, Protein Serine-Threonine Kinases, DNA, Complementary, Mice, Knockout, Muscle, Skeletal, COS Cells, Protein Isoforms, Mutation, Missense, Reverse Transcriptase Polymerase Chain Reaction, Lipid Metabolism, Mice, AMP-Activated Protein Kinases
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