Selective suppression of AMP-activated protein kinase in skeletal muscle: update on ‘lazy mice’
Abstract
AMP-activated protein kinase (AMPK) is becoming recognized as a critical regulator of energy metabolism in cells. Using a mouse model in which we specifically blocked AMPK activity in muscles, we have demonstrated that activation of AMPK is necessary for the effects of 5-aminoimidazole-4-carboxamide riboside (‘AICAR’) and hypoxia, and is possibly required for a portion of exercise-induced glucose uptake. These same mice could not maintain sufficient glycogen in their skeletal muscle and it was rapidly depleted when the animals were subjected to mild exercise. Using isolated strips, we observed muscle hypertrophy and increased tiredness in the AMPK-deficient muscle. We also performed microarray analysis and showed dramatic changes of transcription profile in muscles of the lazy mice. These could have a significant impact on muscle function and may contribute to the observed phenotype.
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LKB1-MKO and AMPK α2 KO, β2 KO and α2 KD mice have lower starting glycogen levels in skeletal muscle.
“LKB1-MKO and AMPK α2 KO, β2 KO and α2 KD mice have lower starting glycogen levels in skeletal muscle [17,138-140], supporting a role for AMPK in glycogen synthesis.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [140]
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“Our results reinforce previous observations showing that AMPK-defective mice have impaired glycogen metabolism (Barnes et al., 2005a; Fujii et al., 2007; Mu et al., 2003).”
ResultManagement 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 855 · see citing works
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Apelin Stimulates Glucose Utilization in Normal and Obese Insulin-Resistant Mice
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AMPK in skeletal muscle function and metabolism
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“In line with this, genetic deletion of AMPKg3 or overexpression of an AMPKa2 kinase dead construct in skeletal muscle markedly reduces glycogen resynthesis after exercise (125, 367).”
BackgroundAMPK and the biochemistry of exercise: implications for human health and disease
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Skeletal Muscle Glucose Uptake During Exercise: How is it Regulated?
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“In AMPKα2−/−, AMPKγ3−/−, AMPKα2-KD and AMPKα2i mice ex vivo contraction-stimulated glucose uptake is normal (17,65) or only moderately reduced (64,66).”
AMPK and Exercise: Glucose Uptake and Insulin Sensitivity
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Predominant α2/β2/γ3 AMPK activation during exercise in human skeletal muscle
Birk, J. B., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.120972 · Cited by 293 · see citing works
“In muscle lacking catalytic or regulatory AMPK isoforms, glycogen metabolism is also affected (Mu et al. 2003; Barnes et al. 2004; Jorgensen et al. 2004).”
BackgroundAMPK activity is diminished in tissues of IL-6 knockout mice: the effect of exercise.
Kelly, M., Keller, C., Avilucea, P. R., Keller, P., Luo, Z., Xiang, X., Giralt, M., Hidalgo, J., Saha, A. K., Pedersen, B. K., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.188 · Cited by 289 · see citing works
Targeting the AMPK pathway for the treatment of Type 2 diabetes
Viollet, B. (2009) · Frontiers in bioscience · doi:10.2741/3460 · Cited by 281 · see citing works
“whole body AMPKα1 and AMPKα2 knock-out (KO) mice (59-62).”
The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration
Thomson, D. M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103125 · Cited by 267 · see citing works
“Initial observations in dominant-negative AMPK (AMPK-DN) transgenic mice in which a dominant negative AMPKα2 subunit was overexpressed under the muscle creatine kinase promoter (expressed in heart and skeletal muscle) showed that EDL muscles tended to be larger than in wild-type (WT) mice, suggesting that AMPK might n…”
BackgroundRole of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise
Jørgensen, S. B., Richter, E. A., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109942 · Cited by 261 · see citing works
“The finding that glycogen breakdown during treadmill running in muscle from either the AMPK kinase-dead mouse, or the α2- or γ 3-AMPK KO mouse is not compromised (Mu et al. 2003; Barnes et al. 2004; Jorgensen et al. 2005) could support such a view.”
BackgroundWitczak, C. A., Sharoff, C. G., & Goodyear, L. J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8244-6 · Cited by 250 · see citing works
AMP-activated protein kinase, stress responses and cardiovascular diseases
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Sarcopenia and Muscle Aging: A Brief Overview
Dao, T., Green, A. E., Kim, Y.-A., Bae, S., Ha, K., Gariani, K., Lee, M.-R., Menzies, K. J., & Ryu, D. (2020) · Endocrinology and Metabolism · doi:10.3803/enm.2020.405 · Cited by 228 · see citing works
Aguilar, V. M., Alliouachene, S., Sotiropoulos, A., Sobering, A. K., Athéa, Y., Djouadi, F., Miraux, S., Thiaudière, E., Foretz, M., Viollet, B., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.006 · Cited by 182 · see citing works
Wojtaszewski, J. F. P., Birk, J. B., Frøsig, C., Holten, M., Pilegaard, H., & Dela, F. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.082669 · Cited by 170 · see citing works
“Of course it cannot be excluded that the changes are purely associative but an interesting note is that in mouse muscle, expressing a kinase dead α2 AMPK construct, contractile properties are impaired (Mu et al. 2003).”
BackgroundSteinberg, G. R., O'Neill, H. M., Dzamko, N. L., Galic, S., Naim, T., Koopman, R., Jørgensen, S. B., Honeyman, J., Hewitt, K., Chen, Z.-P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102434 · Cited by 164 · see citing works
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 165 · see citing works
“One important finding is that activation of muscular AMPK by physical activity (one of the most potent physiological AMPK activator) or by a pharmacological compound called AICAR (5-amino-imidazole-4-carboxamide ribonucleoside, metabolized to ZMP which is an analogy of AMP) increases muscle glucose uptake concomitantl…”
BackgroundRecent Advances in Understanding Integrative Control of Potassium Homeostasis
Youn, J. H., & McDonough, A. A. (2008) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163241 · Cited by 152 · see citing works
Hunter, R. W., Treebak, J. T., Wojtaszewski, J. F. P., & Sakamoto, K. (2011) · Diabetes · doi:10.2337/db10-1148 · Cited by 151 · see citing works
“As an alternative approach, we used a genetically engineered mouse model, AMPK KD, in which AMPK is inactivated by transgenic over-expression of a dominant inhibitory AMPKa2 mutant in muscle cells (6), and established that catalytic activity of AMPK is necessary to elicit AICAR-stimulated glycogen synthesis most likel…”
MethodAMPK‐independent pathways regulate skeletal muscle fatty acid oxidation
Dzamko, N., Schertzer, J. D., Ryall, J. G., Steel, R., Macaulay, S. L., Wee, S., Chen, Z., Michell, B. J., Oakhill, J. S., Watt, M. J., et al. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159814 · Cited by 147 · see citing works
“2007b) may be due to secondary effects on cardiac metabolism which reduces cardiac output or perfusion (Mu et al. 2003).”
BackgroundMethodLee-Young, R. S., Griffee, S. R., Lynes, S. E., Bracy, D. P., Ayala, J. E., McGuinness, O. P., & Wasserman, D. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021048 · Cited by 145 · see citing works
Han, S. M., NamKoong, C., Jang, P., Park, I.-S., Hong, S. W., Katakami, H., Chun, S., Kim, S., Park, J.-Y., Lee, K.-U., et al. (2005) · Diabetologia · doi:10.1007/s00125-005-1913-1 · Cited by 147 · see citing works
“Plasmids encoding c-Myc-tagged forms of DN-α1-AMPK with a mutation altering Asp157 to alanine [14] and of DN-α2-AMPK with a mutation altering Lys45 to arginine [15] were the kind gifts of Dr J.”
MethodNutrient 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 142 · see citing works
“Therefore, several recent studies have used AICAR in combination with either metformin (which activates AMPK by an AMP-independent mechanism; Hardie et al., 2003) or a dominantnegative, kinase-inactive mutant of AMPK (Mu et al., 2001) to argue that the observed effects directly involve AMPK.”
Kodiha, M., Rassi, J. G., Brown, C. M., & Stochaj, U. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00176.2007 · Cited by 138 · see citing works
“Many genes change their expression levels when a dominant-negative allele of AMPK- 2 is highly overexpressed over the endogenous wild-type -subunit in skeletal muscles of transgenic mice (20).”
BackgroundGruzman, A., Babai-Shani, G., & Sasson, S. (2009) · The Review of Diabetic Studies · doi:10.1900/rds.2009.6.13 · Cited by 128 · see citing works
“The activation of muscle AMPK by exogenous compounds or by contraction recruits GLUT-4 to the plasma membrane and augments the rate of glucose transport in a non-insulin-dependent manner [52, 53].”
BackgroundROLE of exercise in maintaining the integrity of the neuromuscular junction
Nishimune, H., Stanford, J. A., & Mori, Y. (2013) · Muscle & Nerve · doi:10.1002/mus.24095 · Cited by 125 · see citing works
AMPK and transcriptional regulation
McGee, S. L. (2007) · Frontiers in bioscience · doi:10.2741/2907 · Cited by 101 · see citing works
Leick, L., Fentz, J., Biensø, R. S., Knudsen, J. G., Jeppesen, J. F., Kiens, B., Wojtaszewski, J. F. P., & Pilegaard, H. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00648.2009 · Cited by 101 · see citing works
Maarbjerg, S., Jørgensen, S. B., Rose, A. J., Jeppesen, J. F., Jensen, T. E., Treebak, J. T., Birk, J. B., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90653.2008 · Cited by 93 · see citing works
“In accordance with earlier reports characterizing the AMPK-KD mice as “lazy” (36), it was noticed that AMPK-KD mice were exercise intolerant, and a treadmill exercise capacity test of noncatheterized animals was conducted to examine this further.”
MethodResultKristensen, J. M., Treebak, J. T., Schjerling, P., Goodyear, L. J., & Wojtaszewski, J. F. P. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00417.2013 · Cited by 87 · see citing works
Role of AMPK in regulation of LC3 lipidation as a marker of autophagy in skeletal muscle
Fritzen, A. M., Frøsig, C., Jeppesen, J. F., Jensen, T. E., Lundsgaard, A., Serup, A. K., Schjerling, P., Proud, C. G., Richter, E. A., & Kiens, B. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.03.005 · Cited by 82 · see citing works
5′‐AMP‐activated protein kinase regulates skeletal muscle glycogen content and ergogenics
Barnes, B. R., Glund, S., Long, Y. C., Hjälm, G., Andersson, L., & Zierath, J. R. (2005) · The FASEB Journal · doi:10.1096/fj.04-3221com · Cited by 80 · see citing works
“AMPK has been linked to exercise tolerance and performance (14, 29).”
BackgroundInfluentialZwetsloot, K. A., Westerkamp, L. M., Holmes, B. F., & Gavin, T. P. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159871 · Cited by 78 · see citing works
Jensen, T. E., Wojtaszewski, J. F. P., & Richter, E. A. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01979.x · Cited by 77 · see citing works
“Importantly, the lack of suppressive effect on protein synthesis seems to translate into increased fibre size in some of the AMPK-deficient mouse models as soleus and EDL muscles from KD AMPK mice have been reported to have 5% and 20% greater cross-sectional areas than wild-type (Mu et al. 2003).”
BackgroundFunctional role of AMP‐activated protein kinase in the heart during exercise
Musi, N., Hirshman, M. F., Arad, M., Xing, Y., FUJII, N. L., Pomerleau, J. M., Ahmad, F., Berul, C. I., Seidman, J. G., Tian, R., et al. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.02.052 · Cited by 77 · see citing works
Exercise-induced molecular mechanisms promoting glycogen supercompensation in human skeletal muscle
Hingst, J. R., Bruhn, L., Hansen, M. B., Rosschou, M. F., Birk, J. B., Fentz, J., Foretz, M., Viollet, B., Sakamoto, K., Færgeman, N. J., et al. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.07.001 · Cited by 79 · see citing works
“In line, deletion of either AMPK g3 or functional AMPK a2 is associated with reduced glycogen storage following exercise [21,57,58].”
BackgroundThe Importance of Fatty Acids as Nutrients during Post-Exercise Recovery
Lundsgaard, A.-M., Fritzen, A. M., & Kiens, B. (2020) · Nutrients · doi:10.3390/nu12020280 · Cited by 72 · see citing works
“Other findings in mice lacking either functional AMPKα2 or AMPKγ3 also showed lower skeletal muscle glycogen levels compared with WT in recovery after 30–90 min of treadmill running [79,80] and 2 h of swimming exercise [81].”
BackgroundMiyamoto, L., Toyoda, T., Hayashi, T., Yonemitsu, S., Nakano, M., Tanaka, S., Ebihara, K., Masuzaki, H., Hosoda, K., Ogawa, Y., et al. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01034.2006 · Cited by 72 · see citing works
“The glycogen concentration in the gastrocnemius muscles of mice that muscle-specifically express a dominant-negative kinase-dead form of the -isoform is about half that observed in nontransgenic mice (31), although glycogen synthase (GS) activity and glycogen phosphorylase (GP) activity are not significantly different…”
BackgroundNLRP3 and IL ‐1 β in macrophages as critical regulators of metabolic diseases
McGettrick, A. F., & O'Neill, L. A. J. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12169 · Cited by 66 · see citing works
“In a microarray study the expression of a dominant negative form of AMPK in skeletal muscles led to the increased expression of 234 genes and the decreased expression of 130 genes [58].”
BackgroundThe Role of Hif-1 1 in Hypoxic Response in the Skeletal Muscle
Mason, S. D., & Johnson, R. S. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-75434-5_18 · Cited by 65 · see citing works
“in the skeletal muscle, through the use of a dominant negative form of AMPK’s catalytic α subunit, results in the muscles being more sensitive to, and slower to recover from, fatigue ( 46 ), and demonstrates the importance of AMPK during exercise.”
BackgroundBarnes, B. R., Long, Y. C., Steiler, T. L., Leng, Y., Galuska, D., Wojtaszewski, J. F. P., Andersson, L., & Zierath, J. R. (2005) · Diabetes · doi:10.2337/diabetes.54.12.3484 · Cited by 60 · see citing works
Hancock, C. R., Janssen, E., & Terjung, R. L. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00885.2005 · Cited by 54 · see citing works
Sensing and responding to energetic stress: Evolution of the AMPK network
Craig, P. M., Moyes, C. D., & LeMoine, C. M. R. (2018) · Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.11.001 · Cited by 46 · see citing works
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“This is in accordance with the findings that the muscle glycogen levels during post-exercise recovery, after 30–90 min of treadmill running or 2 h of swimming, were lower in mice lacking functional AMPK than in WT (Mu et al. 2003; Barnes et al. 2004; Jørgensen et al. 2005).”
MethodResultInfluentialCellular and molecular pathways controlling muscle size in response to exercise
Attwaters, M., & Hughes, S. M. (2021) · FEBS Journal · doi:10.1111/febs.15820 · Cited by 45 · see citing works
Lee, R. S., Ayala, J. E., Fueger, P. T., Mayes, W. H., Kang, L., & Wasserman, D. H. (2010) · International Journal of Obesity · doi:10.1038/ijo.2010.220 · Cited by 42 · see citing works
Tohyama, D., & Yamaguchi, A. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.126 · Cited by 40 · see citing works
AMPK Signaling Regulates the Age-Related Decline of Hippocampal Neurogenesis
Wang, B. Z., Yang, J. J., Zhang, H., Smith, C., & Jin, K. (2019) · Aging and Disease · doi:10.14336/ad.2019.0102 · Cited by 40 · see citing works
“If in the nucleus, it is involved in regulating gene expression [36, 37].”
Backgroundde Wendt, C., Espelage, L., Eickelschulte, S., Springer, C. A., Toska, L., Scheel, A. K., Bedou, A. D., Benninghoff, T., Cames, S., Stermann, T., et al. (2021) · Diabetes · doi:10.2337/db21-0587 · Cited by 39 · see citing works
Steinberg, G. R. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-009 · Cited by 38 · see citing works
“2008), while those with reduced AMPK have low levels of glycogen (Mu et al. 2003; Thomson et al. 2007).”
BackgroundAMPK and Insulin Action - Responses to Ageing and High Fat Diet
Frøsig, C., Jensen, T. E., Jeppesen, J. F., Pehmøller, C. K., Treebak, J. T., Maarbjerg, S., Kristensen, J. M., Sylow, L., Alsted, T. J., Schjerling, P., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062338 · Cited by 34 · see citing works
“Animals used were age 4.2 6 0.1 month (Young) or 18.0 6 0.2 month (Old) C57BL/6J male mice overexpressing a muscle-specific, kinase-dead a 2AMPK construct (AMPK KD), as described by Mu et al. [15,16] and corresponding WT littermates.”
InfluentialDiacylglycerol kinase-δ regulates AMPK signaling, lipid metabolism, and skeletal muscle energetics
Jiang, L. Q., Barbosa, T. D. C., Massart, J., Deshmukh, A. S., Löfgren, L., Duque-Guimaraes, D. E., Ozilgen, A., Osler, M. E., Chibalin, A., & Zierath, J. R. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00209.2015 · Cited by 34 · see citing works
Contraction‐regulated mTORC1 and protein synthesis: Influence of AMPK and glycogen
Knudsen, J. R., Li, Z., Persson, K. W., Li, J., Henríquez‐Olguín, C., & Jensen, T. E. (2020) · The Journal of Physiology · doi:10.1113/jp279780 · Cited by 33 · see citing works
“Consistent with this, muscle-specific dominant-negative kinase-dead AMPK (KD-AMPK) mice displayed greater skeletal muscle cross-sectional area in soleus (+5%) and extensor digitorum longus (+20%) (Mu et al. 2003) and muscle-specific AMPK α-dKO mice displayed similar magnitudes of increase in the muscle weight of the t…”
BackgroundGlund, S., Treebak, J. T., Long, Y. C., Barrès, R., Viollet, B., Wojtaszewski, J. F. P., & Zierath, J. R. (2008) · Endocrinology · doi:10.1210/en.2008-1204 · Cited by 34 · see citing works
ORM Promotes Skeletal Muscle Glycogen Accumulation via CCR5-Activated AMPK Pathway in Mice
Qin, Z., Wan, J.-J., Sun, Y., Wang, P., Su, D., Lei, H., & Liu, X. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00302 · Cited by 33 · see citing works
AMPK activation with AICAR provokes an acute fall in plasma [K+]
Zheng, D., Perianayagam, A., Lee, D. H., Brannan, M. D., Yang, L. E., Tellalian, D., Chen, P., Lemieux, K., Marette, A., Youn, J. H., et al. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00464.2007 · Cited by 30 · see citing works
“The AICAR-stimulated decrease in plasma glucose in NTg (33, 34) served as the positive control.”
InfluentialŁukaszuk, B., Bialuk, I., Górski, J., Zajączkiewicz, M., Winnicka, M. M., & Chabowski, A. (2012) · Lipids · doi:10.1007/s11745-012-3678-x · Cited by 30 · see citing works
“Likewise, decreased AMPK activation (present study and [39]) could contribute to the shorter time till exhaustion as it was shown in mice expressing a dominant negative AMPK [40].”
BackgroundAbbott, M. J., Bogachus, L. D., & Turcotte, L. P. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00807.2010 · Cited by 30 · see citing works
Ost, M., Werner, F., Dokas, J., Klaus, S., & Voigt, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094689 · Cited by 27 · see citing works
“decreased [29,30].”
Effects of feed deprivation on the AMPK signaling pathway in skeletal muscle of broiler chickens
Hu, X., Liu, L., Song, Z., Sheikhahmadi, A., Wang, Y., & Buyse, J. G. (2015) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2015.10.007 · Cited by 26 · see citing works
Lee, R. S., Bonner, J. S., Mayes, W. H., Iwueke, I. C., Barrick, B. A., Hasenour, C. M., Kang, L., & Wasserman, D. H. (2012) · Diabetologia · doi:10.1007/s00125-012-2787-7 · Cited by 24 · see citing works
“Male, 18-weekold C57BL/6J mice (Jackson Laboratories, Bar Harbor, ME, USA) and 16-week-old C57BL/6 mice expressing a musclespecific kinase-dead Ampkα2 (also known as Prkaa2) subunit (α2-KD) [18] were used.”
Regulation of Mitochondrial Biogenesis in Metabolic Syndrome
Rolo, A. P., Gomes, A. P., & Palmeira, C. M. (2011) · Current Drug Targets · doi:10.2174/138945011795529056 · Cited by 19 · see citing works
Reciprocity Between Skeletal Muscle AMPK Deletion and Insulin Action in Diet-Induced Obese Mice
Lantier, L., Williams, A. S., Williams, I. M., Guérin, A., Bracy, D. P., Goelzer, M., Foretz, M., Viollet, B., Hughey, C. C., Wasserman, D. H., et al. (2020) · Diabetes · doi:10.2337/db19-1074 · Cited by 21 · see citing works
“This may be directly linked to the critical importance of AMPK in the control of glycogen mass (33-40).”
BackgroundDiverse 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 17 · see citing works
Stride, N. O., Larsen, S., Treebak, J. T., HANSEN, C. N., Hey‐Mogensen, M., Speerschneider, T., Jensen, T. E., Jeppesen, J. F., Wojtaszewski, J. F. P., Richter, E. A., et al. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00033 · Cited by 20 · see citing works
“We hypothesized that the common effector mechanism of AMPK in these pathologies could be disturbances in mitochondrial substrate utilization and therefore aimed at characterizing mitochondrial substrate utilization in a mouse model over-expressing a dominant negative isoform of the catalytic AMPKα2 subunit as describe…”
BackgroundMethodResultInfluentialControl of microvascular P o 2kinetics following onset of muscle contractions: role for AMPK
Kano, Y., Poole, D. C., Sudo, M., Hirachi, T., Miura, S., & Ezaki, O. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00294.2011 · Cited by 16 · see citing works
AMPKγ3 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 17 · see citing works
Obesity-dependent dysregulation of glucose homeostasis in kinase suppressor of ras 2 − /− mice
Henry, M. D., Costanzo-Garvey, D. L., Klutho, P. J., & Lewis, R. E. (2014) · Physiological Reports · doi:10.14814/phy2.12053 · Cited by 14 · see citing works
“Similarly, sedentary mice expressing dominant negative AMPK catalytic subunits in skeletal muscle (Mu et al. 2003) and ksr2 / mice (Costanzo-Garvey et al. 2009) show a similar depletion of glycogen in the gastrocnemius.”
BackgroundFree Fatty Acid Impairs Myogenic Differentiation through the AMPK α -MicroRNA 206 Pathway
Jiang, A., Guo, H., Zhang, L., Jiang, X., Zhang, X., Wu, W., & Liu, H. (2021) · Molecular and Cellular Biology · doi:10.1128/mcb.00327-21 · Cited by 10 · see citing works
“(WT) mice, suggesting that AMPKa might negatively regulate basal muscle mass (44).”
BackgroundRole of 5′AMP-activated protein kinase in skeletal muscle
Treebak, J. T., & Wojtaszewski, J. F. P. (2008) · International Journal of Obesity · doi:10.1038/ijo.2008.117 · Cited by 10 · see citing works
Skeletal muscle mitochondrial respiration in AMPK α2 kinase‐dead mice
Larsen, S., Kristensen, J. M., Stride, N. O., Wojtaszewski, J. F. P., Helge, J. W., & Dela, F. (2011) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02399.x · Cited by 6 · see citing works
“AMPKa2 KD mice are characterized by exercise intolerance and a reduced spontaneous activity level, attributed to impaired cardiac function (Mu et al. 2003).”
BackgroundMethodInfluentialÖztürk, M., Bolkent, S., Dağıstanlı, F. K., Tunçdemi̇r, M., Yılmazer, S., & Akkan, A. G. (2006) · Acta Diabetologica · doi:10.1007/s00592-006-0214-6 · Cited by 5 · see citing works
“AMP-activated protein kinase (AMPK) activation in beta cells is induced by the adenosine analogue, AICAR, which is phosphorylated to form ZMP, an analogue of 5’-AMP [1–5].”
BackgroundSanglard, L. P., Márquez, D. E. C., da Silva, W., Fontes, M. M. D. S., Costa, T. C., Júnior, D. T. V., Gionbelli, M. P., Serão, N. V. L., Sampaio, C. B., & Duarte, M. D. S. (2022) · Ciência Rural · doi:10.1590/0103-8478cr20210917 · Cited by 3 · see citing works
Effects 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 · see citing works
“Activation of AMPK by 5-amino-4-imidazolecarboxamide-riboside (AICAR) has been demonstrated to increase muscle glucose uptake in vivo and in vitro via an acute insulin-independent mechanism (Mu et al. 2001; Bergeron et al. 1999).”
BackgroundShen, X., Chen, J., & Tang, X. (2012) · Scientia Sinica Chimica · doi:10.1360/032012-333 · Cited by 2 · see citing works
Maione, D., Cicero, A. F. G., Bacchelli, S., Cosentino, E. R., Esposti, D. D., Senaldi, R., Strocchi, E., D’Addato, S., & Borghi, C. (2013) · Physiological Research · doi:10.33549/physiolres.932484 · Cited by 1 · see citing works
Participation of AMPK in the Control of Skeletal Muscle Mass
Egawa, T. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_12 · Cited by 1 · see citing works
AMPK and the Metabolic Syndrome
Viollet, B., & Andréelli, F. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch17 · Cited by 1 · see citing works
Glund, S. (2007) · Figshare
Kinase cascades in the regulation of glucose homeostasis
Steiler, T. L. (2005) · Figshare
micein skeletal muscle of adenylate kinase-deficient Contraction-mediated phosphorylation of AMPK is
Hancock, C. R., Janssen, E., Terjung, R. L., Zierath, J. R., Kulkarni, S. S., Karlsson, H., Szekeres, F. L. M., Chibalin, A., Bontemps, F., Oscarsson, J., et al. (2015)
CaMKKbeta/AMPK Negatively Regulates Adiposity
Peng, I. (2011) · eScholarship (California Digital Library)
St-Amand, E. (2015) · Corpus Université Laval (Université Laval)
Jørgensen, S. B., Nielsen, J. N., Birk, J. B., Olsen, G. S., Viollet, B., Andreelli, F., Schjerling, P., Vaulont, S., Hardie, D. G., Hansen, B. F., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.12.3074 · Cited by 241 · see citing works
“In agreement with this observation, 10 min of contractile activity increased GS activity similarly in control muscle and muscle from the AMPK dead mouse (32) and from the two KO models used in the present study (S.”
Method
- Authors
- Mu, J., Barton, E. R., & Birnbaum, M. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Pennsylvania (US)
- Corresponding author
- Mu, J.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2003-02-01
- Volume
- 31
- Issue
- 1
- Pages
- 236-241
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W1975883334
- Cited by
- 93
- References
- 0
- Citations by year
- 2022: 1 · 2021: 3 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 5 · 2014: 3 · 2013: 5 · 2012: 5
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- AMPK, skeletal muscle, energy metabolism, AICAR, hypoxia, glycogen depletion, muscle fatigue, muscle hypertrophy, gene expression profiling, gene expression
- MeSH terms
- Aminoimidazole Carboxamide, Animals, Hypoxia, Enzyme Inhibitors, Glycogen, Glycogen Synthase, Hypertrophy, Multienzyme Complexes, Mutation, Phenotype, Physical Conditioning, Animal, Ribonucleotides, Time Factors, Transcription, Genetic, Protein Serine-Threonine Kinases, Muscle, Skeletal, Mice, AMP-Activated Protein Kinases
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