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.
Integrity signals
Registry
Cites
Statistics
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?
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.
“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]
Whole-body γ3 KO mice have normal insulin sensitivity under basal conditions and glucose uptake during exercise.
“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]
Whole-body γ3 KO mice have reduced AMPK activity at rest, during exercise and in response to fasting.
“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]
Contraction-mediated glucose uptake was normal in β2 or γ3 KO mice.
“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]
AMPK α2 KO and α2 KD and α2iTg mice have normal or only modest reductions in glucose uptake during contractions.
“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]
AMPK γ3 KO and α2 KD mice have impaired glycogen resynthesis following exercise.
“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]
Cites
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 · see citing works
Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053 · see citing works
THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?
Hardie, D. G., Carling, D., & Carlson, M. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.821 · Cited by 1,436 · see citing works
Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., & Shulman, G. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625599 · Cited by 1,036 · see citing works
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 · see citing works
Hayashi, T., Hirshman, M. F., Kurth, E. J., Winder, W. W., & Goodyear, L. J. (1998) · Diabetes · doi:10.2337/diab.47.8.1369 · Cited by 774 · see citing works
Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754 · see citing works
A Mutation in PRKAG3 Associated with Excess Glycogen Content in Pig Skeletal Muscle
Denis Milan, A., Jeon, J., Looft, C., Amarger, V., Robic, A., Thelander, M., Rogel-Gaillard, C., Paul, S., Iannuccelli, N., Rask, L., et al. (2000) · Science · doi:10.1126/science.288.5469.1248 · Cited by 717 · see citing works
Self-citationActivation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases
Hong, S. P., Leiper, F. C., Woods, A., Carling, D., & Carlson, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1533136100 · Cited by 597 · see citing works
Jørgensen, S. B., Viollet, B., Andreelli, F., Frøsig, C., Birk, J. B., Schjerling, P., Vaulont, S., Richter, E. A., & Wojtaszewski, J. F. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306205200 · Cited by 553 · see citing works
Dealing with energy demand: the AMP-activated protein kinase
Kemp, B. E., Mitchelhill, K. I., Stapleton, D., Michell, B. J., Chen, Z., & Witters, L. A. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01340-1 · Cited by 521 · see citing works
Self-citationKozak, M. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.5073-5080.1989 · Cited by 472 · see citing works
Arad, M., Benson, D. W., Pérez‐Atayde, A. R., McKenna, W. J., Sparks, E. A., Kanter, R. J., McGarry, K., Seidman, J. G., & Seidman, C. E. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14571 · Cited by 460 · see citing works
Arad, M., Benson, D. W., Pérez‐Atayde, A. R., McKenna, W. J., Sparks, E. A., Kanter, R. J., McGarry, K., Seidman, J. G., & Seidman, C. E. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214571 · Cited by 441 · see citing works
AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen
Polekhina, G., Gupta, A., Michell, B. J., van Denderen, B., Murthy, S., Feil, S. C., Jennings, I. G., Campbell, D. J., Witters, L. A., Parker, M. W., et al. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00292-6 · Cited by 423 · see citing works
Self-citationWojtaszewski, J. F. P., MacDonald, C., Nielsen, J. N., Hellsten, Y., Hardie, D. G., Kemp, B. E., Kiens, B., & Richter, E. A. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00436.2002 · Cited by 348 · see citing works
Hudson, E. R., Pan, D. A., James, J., Lucocq, J. M., Hawley, S. A., Green, K. A., Baba, O., Terashima, T., & Hardie, D. G. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00249-5 · Cited by 332 · see citing works
Carling, D., & Grahame Hardie, D. (1989) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(89)90014-1 · Cited by 296 · see citing works
Wojtaszewski, J. F. P., Jørgensen, S. B., Hellsten, Y., Hardie, D. G., & Richter, E. A. (2002) · Diabetes · doi:10.2337/diabetes.51.2.284 · Cited by 261 · see citing works
Ciobanu, D. C., Bastiaansen, J. W. M., Malek, M., Helm, J. M., Woollard, J. R., Plastow, G. S., & Rothschild, M. F. (2001) · Genetics · doi:10.1093/genetics/159.3.1151 · Cited by 243 · see citing works
High-Fat Feeding Impairs Insulin-Stimulated GLUT4 Recruitment via an Early Insulin-Signaling Defect
Zierath, J. R., Houseknecht, K. L., Gnudi, L., & Kahn, B. B. (1997) · Diabetes · doi:10.2337/diab.46.2.215 · Cited by 238 · see citing works
Self-citationKoistinen, H. A., Galuska, D., Chibalin, A., Yang, J., Zierath, J. R., Holman, G. D., & Wallberg‐Henriksson, H. (2003) · Diabetes · doi:10.2337/diabetes.52.5.1066 · Cited by 231 · see citing works
Self-citationMahlapuu, M., Johansson, C., Lindgren, K., Hjälm, G., Barnes, B. R., Krook, A., Zierath, J., Andersson, L., & Marklund, S. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00147.2003 · Cited by 169 · see citing works
Self-citationIntrasteric control of AMPK via the γ1 subunit AMP allosteric regulatory site
Adams, J., Chen, Z.-P., van Denderen, B. V., Morton, C., Parker, M. W., Witters, L. A., Stapleton, D., & Kemp, B. (2004) · Protein Science · doi:10.1110/ps.03340004 · Cited by 166 · see citing works
Self-citationEffect of Contraction on Mitogen-activated Protein Kinase Signal Transduction in Skeletal Muscle
Ryder, J. W., Fahlman, R., Wallberg‐Henriksson, H., Alessi, D. R., Krook, A., & Zierath, J. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1457 · Cited by 162 · see citing works
Self-citationLooking at mRNA decay pathways through the window of molecular evolution
Culbertson, M. R., & Leeds, P. (2003) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(03)00014-5 · Cited by 147 · see citing works
Expression of the AMP‐activated protein kinase β1 and β2 subunits in skeletal muscle
Chen, Z., Heierhorst, J., Mann, R. J., Mitchelhill, K. I., Michell, B. J., Witters, L. A., Lynch, G. S., Kemp, B. E., & Stapleton, D. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01371-x · Cited by 134 · see citing works
Self-citationIsoform-specific Purification and Substrate Specificity of the 5′-AMP-activated Protein Kinase
Michell, B. J., Stapleton, D., Mitchelhill, K. I., House, C. M., Katsis, F., Witters, L. A., & Kemp, B. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28445 · Cited by 133 · see citing works
Self-citationWallberg‐Henriksson, H., ZETAN, N., & Henriksson, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47618-1 · Cited by 124 · see citing works
ETB receptor activation leads to activation and phosphorylation of NHE3
Peng, Y. S., Moe, O. W., Chu, T., Preisig, P. A., Yanagisawa, M., & Alpern, R. J. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.4.c938 · Cited by 107 · see citing works
Lebret, B., Roy, P. L., Monin, G., Lefaucheur, L. L., Caritez, J. C., Talmant, A., Elsen, J.-M., & Sellier, P. P. (1999) · Journal of Animal Science · doi:10.2527/1999.7761482x · Cited by 99 · see citing works
Postexercise glucose uptake and glycogen synthesis in skeletal muscle from GLUT4‐deficient mice
Ryder, J. W., Kawano, Y., Galuska, D., Fahlman, R., Wallberg‐Henriksson, H., Charron, M. J., & Zierath, J. R. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.15.2246 · Cited by 81 · see citing works
Self-citationExpression of β subunit isoforms of the Na+,K+‐ATPase is muscle type‐specific
Hundal, H. S., Marette, A., Ramlal, T., Liu, Z., & Klip, A. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80938-q · Cited by 74 · see citing works
Temperature regulation in subtropical tree bats
Genoud, M. (1993) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(93)90324-w · Cited by 54 · see citing works
Insulin Production by Engineered Muscle Cells
Gros, L., Riu, E., Montoliu, L., Ontiveros, M., Brigand, L. L., & Bosch, F. (1999) · Human Gene Therapy · doi:10.1089/10430349950018193 · Cited by 34 · see citing works
Inhibition of Hepatic Glucose Production by SDZ 51641
Young, D. A., Ho, R. S., Bell, P. A., Cohen, D. K., McIntosh, R. H., Nadelson, J., & Foley, J. E. (1990) · Diabetes · doi:10.2337/diab.39.11.1408 · Cited by 31 · see citing works
Flagged first, then by citations
1 of the 37 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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 · see citing works
“In mice in which the γ3 gene was deleted, glycogen resynthesis following exercise was reduced, whereas it was increased in the γ3 mutant transgenic animals (Barnes et al., 2004).”
BackgroundSteinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,633 · see citing works
PGC-1α, SIRT1 and AMPK, an energy sensing network that controls energy expenditure
Cantó, C., & Auwerx, J. (2009) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328328d0a4 · Cited by 1,624 · see citing works
Exercise, GLUT4, and skeletal muscle glucose uptake
Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407 · see citing works
“Activation of AMPK by AICAR in resting muscle results in increased glucose uptake (209), and this effect is lost when 2- or 3-AMPK subunits are deficient (21, 152, 216).”
The Human Obesity Gene Map: The 2005 Update
Rankinen, T., Zuberi, A., Chagnon, Y. C., Weisnagel, S. J., Argyropoulos, G., Walts, B., Pérusse, L., & Bouchard, C. (2006) · Obesity · doi:10.1038/oby.2006.71 · Cited by 1,119 · see citing works
AMP-activated protein kinase signaling in metabolic regulation
Long, Y. C. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29044 · Cited by 1,097 · see citing works
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works
“To provide in vivo evidence to support the above results, we used mice deficient in the AMPKg3 subunit (Barnes et al., 2004) The g3 is the predominant g-isoform in glycolytic skeletal muscle (Mahlapuu et al., 2004) and is critical for effective adaptations of glycolytic muscle to metabolic…”
MethodInfluentialSelf-citationAMPK 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 · see citing works
AMP-activated protein kinase: the current landscape for drug development
Steinberg, G. R., & Carling, D. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0019-2 · Cited by 757 · see citing works
Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
Sanders, M. J., Grondin, P., Hegarty, B. D., Snowden, M. A., & Carling, D. (2007) · Biochemical Journal · doi:10.1042/bj20061520 · Cited by 660 · see citing works
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 538 · see citing works
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 · see citing works
AMPK: a metabolic gauge regulating whole-body energy homeostasis
Lage, R., Diéguez, C., Vidal‐Puig, A., & López, M. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.09.007 · Cited by 503 · see citing works
Exercise-stimulated glucose uptake — regulation and implications for glycaemic control
Sylow, L., Kleinert, M., Richter, E. A., & Jensen, T. E. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.162 · Cited by 498 · see citing works
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 496 · see citing works
AMPK and the biochemistry of exercise: implications for human health and disease
Richter, E. A., & Ruderman, N. B. (2009) · Biochemical Journal · doi:10.1042/bj20082055 · Cited by 481 · see citing works
A second look into fibre typing – Relation to meat quality
Lefaucheur, L. (2009) · Meat Science · doi:10.1016/j.meatsci.2009.05.004 · Cited by 431 · see citing works
O'Neill, H. M., Maarbjerg, S. J., Crane, J. D., Jeppesen, J., Jørgensen, S. B., Schertzer, J. D., Shyroka, O., Kiens, B., van Denderen, B. J., Tarnopolsky, M. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105062108 · Cited by 406 · see citing works
“The phenotype of β2 null mice was similar to that of mice lacking α2 (7) or γ3 (8) subunits or muscle-specific overexpression of an α2 kinase dead (KD) mutation (9, 10).”
BackgroundSkeletal Muscle Glucose Uptake During Exercise: How is it Regulated?
Rose, A. J., & Richter, E. A. (2005) · Physiology · doi:10.1152/physiol.00012.2005 · Cited by 371 · see citing works
AMPK regulation of fatty acid metabolism and mitochondrial biogenesis: implications for obesity.
O’Neill, H. M., Holloway, G. P., & Steinberg, G. R. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.019 · Cited by 364 · see citing works
“muscle AMPK as the over-expression of AMPK c3 increases fatty acid oxidation and protects against high-fat diet induced accumulation of TAGs in skeletal muscle (Barnes et al., 2004).”
BackgroundAMP-Activated Protein Kinase in the Heart
Arad, M., Seidman, C. E., & Seidman, J. G. (2007) · Circulation Research · doi:10.1161/01.res.0000258446.23525.37 · Cited by 356 · see citing works
Scheffler, T. L., & Gerrard, D. E. (2007) · Meat Science · doi:10.1016/j.meatsci.2007.04.024 · Cited by 346 · see citing works
The Human Obesity Gene Map: The 2004 Update
Përusse, L., Rankinen, T., Zuberi, A. R., Chagnon, Y. C., Weisnagel, S. J., Argyropoulos, G. A., Walts, B., Snyder, E. E., & Bouchard, C. (2005) · Obesity Research · doi:10.1038/oby.2005.50 · Cited by 326 · see citing works
AMPK: Lessons from transgenic and knockout animals
Viollet, B. (2009) · Frontiers in bioscience · doi:10.2741/3229 · Cited by 314 · see citing works
“Recently, the role of AMPK in the regulation of muscle glycogen has been further investigated with AMPKγ3−/− and AMPKα2-KD mice and transgenic mice over-expressing AMPKγ mutants specifically in skeletal muscle (65,76,77).”
InfluentialSrivastava, 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 297 · see citing works
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 · see citing works
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
“The regulatory γ 3 protein has received special interest, as naturally occurring mutations result in pronounced pathological alterations that may be linked with changes in glycogen metabolism (Milan et al. 2000; Barnes et al. 2004).”
BackgroundRole of Skeletal Muscle in Insulin Resistance and Glucose Uptake
Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive physiology · doi:10.1002/j.2040-4603.2020.tb00136.x · Cited by 283 · see citing works
Treebak, J. T., Glund, S., Deshmukh, A. S., Klein, D. K., Long, Y. C., Jensen, T. E., Jørgensen, S. B., Viollet, B., Andersson, L., Neumann, D., et al. (2006) · Diabetes · doi:10.2337/db06-0175 · Cited by 281 · see citing works
“This observation was reinforced by recent reports showing that knockout of either the catalytic 2 (but not 1 AMPK isoform) or the regulatory 3 AMPK subunit completely abolishes AICAR-induced glucose transport (4,5).”
BackgroundMethodInfluentialSelf-citationTargeting 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
Role 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
“It has previously been shown that AICAR-induced glucose uptake is completely prevented in muscle from the α2- and γ 3-AMPK KO mice and the AMPK kinase-dead mouse, while contraction-induced glucose uptake ex vivo is normal in α2- and γ 3-AMPK KO muscles and only partially reduced in AMPK kinase dead muscles (Mu et al.…”
BackgroundInfluentialZhang, L., Keung, W., Samokhvalov, V., Wang, W. J., & Lopaschuk, G. D. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.09.014 · Cited by 257 · see citing works
AMPK signaling and its targeting in cancer progression and treatment
Hsu, C.-C., Peng, D., Cai, Z., & Lin, H. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.04.006 · Cited by 257 · see citing works
Signaling Specificity of Interleukin-6 Action on Glucose and Lipid Metabolism in Skeletal Muscle
Al-Khalili, L., Bouzakri, K., Glund, S., Lönnqvist, F., Koistinen, H. A., & Krook, A. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0490 · Cited by 250 · see citing works
“For example, mutations in the 3-subunit of AMPK lead to a constitutively active enzyme, which leads to enhanced glycogen accumulation (58, 59).”
Chibalin, A. V., Leng, Y., Vieira, E., Krook, A., Björnholm, M., Long, Y. C., Kotova, O., Zhong, Z., Sakane, F., Steiler, T., et al. (2008) · Cell · doi:10.1016/j.cell.2007.12.035 · Cited by 232 · see citing works
Self-citationAMPK and the Adaptation to Exercise
Spaulding, H. R., & Yan, Z. (2022) · Annual Review of Physiology · doi:10.1146/annurev-physiol-060721-095517 · Cited by 231 · see citing works
Mashili, F. L., Austin, R. L., Deshmukh, A. S., Fritz, T., Caidahl, K., Bergdahl, K., Zierath, J. R., Chibalin, A., Moller, D. E., Kharitonenkov, A., et al. (2011) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.1177 · Cited by 222 · see citing works
“The content of the pre-buffer has been described previously [24].”
MethodSelf-citationMedical Sequencing at the Extremes of Human Body Mass
Ahituv, N., Kavaslar, N., Schackwitz, W., Ustaszewska, A., Martin, J., Hébert, S., Doelle, H., Ersoy, B. A., Kryukov, G. V., Schmidt, S., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/513471 · Cited by 221 · see citing works
Jensen, T. E., Rose, A. J., Jørgensen, S. B., Brandt, N., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00456.2006 · Cited by 214 · see citing works
“Although studies using various transgenic mouse models have demonstrated that glucose uptake stimulation by the adenosine analog 5-aminoimidazole4-carboxamide-1- -4-ribofuranoside (AICAR) requires expression of the catalytic 2-AMPK, the regulatory 3-subunit of AMPK, and the AMPK kinase (AMPKK) LKB1 (4, 26, 31, 37), th…”
BackgroundAMPK 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 211 · see citing works
The coordination of nuclear and mitochondrial communication during aging and calorie restriction
Finley, L. W. S., & Haigis, M. C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.003 · Cited by 207 · see citing works
“…ability of AICAR treatment to lower whole body glucose levels is abolished in mice lacking the catalytic a2 subunit of AMPK, and g3225Q mice are protected against diet-induced skeletal muscle insulin resistance (Mu et al., 2001; Barnes et al., 2004; Jorgensen et al., 2004; Long and Zierath, 2006).”
BackgroundLiver-Specific Activation of AMPK Prevents Steatosis on a High-Fructose Diet
Woods, A., Williams, J., Muckett, P. J., Mayer, F. V., Liljevald, M., Bohlooly‐Y, M., & Carling, D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.011 · Cited by 207 · see citing works
Tbc1d1 mutation in lean mouse strain confers leanness and protects from diet-induced obesity
Chadt, A., Leicht, K., Deshmukh, A. S., Jiang, L. Q., Scherneck, S., Bernhardt, U., Dreja, T., Vogel, H., Schmolz, K., Kluge, R., et al. (2008) · Nature Genetics · doi:10.1038/ng.244 · Cited by 201 · see citing works
Self-citationThirupathi, A., & de Souza, C. T. (2017) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-017-0576-y · Cited by 198 · see citing works
Garcia-Roves, P. M., Osler, M. E., Holmström, M. H., & Zierath, J. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805078200 · Cited by 190 · see citing works
Self-citationEnhanced muscle insulin sensitivity after contraction/exercise is mediated by AMPK
Kjøbsted, R., Munk-Hansen, N., Birk, J. B., Foretz, M., Viollet, B., Björnholm, M., Zierath, J. R., Treebak, J. T., & Wojtaszewski, J. F. P. (2017) · Diabetes · doi:10.2337/db16-0530 · Cited by 178 · see citing works
“Animals used in this study were AMPKa1a2 muscle-specific double-knockout (mdKO) and whole-body AMPKg3 KO female mice with corresponding wild-type (WT) littermates as controls (35,36,38).”
MethodSelf-citationJørgensen, 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 176 · see citing works
“The signal obtained using the 3-antibody has previously been verified against bacterially expressed His-tagged 3-protein (26), and the signal is abolished in muscle lysates from 3-KO mice (3).”
MethodWojtaszewski, 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
“Also, it is now well established that the content of γ 3 protein and/or the functionality of this isoform influences important metabolic processes, for example muscular glucose transport and glycogen synthesis (Milan et al. 2000; Barnes et al. 2004).”
BackgroundmTOR signaling in tumorigenesis
Xu, K. L., Liu, P., & Wei, W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.10.007 · Cited by 167 · see citing works
AICAr, a Widely Used AMPK Activator with Important AMPK-Independent Effects: A Systematic Review
Višnjić, D., Lalić, H., Dembitz, V., Tomić, B., & Smoljo, T. (2021) · Cells · doi:10.3390/cells10051095 · Cited by 164 · see citing works
“AICAr-induced glucose uptake in skeletal muscle was abolished in the knockout of the α 2 [32,33,35] and α 3 isoforms of AMPK [34].”
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
Nur77 Regulates Lipolysis in Skeletal Muscle Cells
Maxwell, M., Cleasby, M. E., Harding, A. S., Stark, A., Cooney, G. J., & Muscat, G. E. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409580200 · Cited by 158 · see citing works
The CBS Domain: A Protein Module with an Emerging Prominent Role in Regulation
Baykov, A. A., Tuominen, H. K., & Lahti, R. (2011) · ACS Chemical Biology · doi:10.1021/cb200231c · Cited by 157 · see citing works
Burwinkel, B., Scott, J. W., Bührer, C., van Landeghem, F. K. H., Cox, G. F., Wilson, C. J., Hardie, D. G., & Kilimann, M. W. (2005) · The American Journal of Human Genetics · doi:10.1086/430840 · Cited by 152 · see citing works
“Activation of AMPK increases glucose uptake by causing acute activation or translocation, as well as increased expression, of both GLUT1 and GLUT4 (Hayashi et al. 1998; Kurth-Kraczek et al. 1999; Barnes et al. 2002; Fryer et al. 2002) in several tissues, including the heart (Russell et al. 1999).”
BackgroundAMPK‐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
“…also found that carbohydrate oxidation was also maintained during treadmill exercise supporting previous findings demonstrating that glucose uptake is not impaired in skeletal muscle of mice with AMPK deficiency (Jorgensen et al. 2003; Barnes et al. 2004; Fujii et al. 2005; Thomson et al. 2007b).”
BackgroundResultExercise-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 · see citing works
Kjøbsted, R., Treebak, J. T., Fentz, J., Lantier, L., Viollet, B., Birk, J. B., Schjerling, P., Björnholm, M., Zierath, J. R., & Wojtaszewski, J. F. P. (2014) · Diabetes · doi:10.2337/db14-1402 · Cited by 135 · see citing works
“1, 3E, and 8, the animals used in this study were muscle-specific kinase-dead a2-AMPK (AMPK KD) (32), muscle-specific a2- and a1-AMPK double-knockout (AMPK mdKO) (33), and g3-AMPK KO mice (34) with corresponding WT littermates used as controls.”
MethodSelf-citationDasgupta, B., & Milbrandt, J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.01.005 · Cited by 133 · see citing works
Wright, D. C., Geiger, P. C., Holloszy, J. O., & Han, D. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00561.2004 · Cited by 131 · see citing works
“(2) showed that deletion of AMPK 3, while preventing AICAR-induced glucose transport, had no effect on contraction-induced increases in glucose transport activity in rat fast-twitch muscle, suggesting that a compensatory increase in stimulation of glucose transport by the Ca(2) -signaling pathway had occurred.”
BackgroundExpanding roles for AMPK in skeletal muscle plasticity
Mounier, R., Théret, M., Lantier, L., Foretz, M., & Viollet, B. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.02.009 · Cited by 130 · see citing works
Deshmukh, A. S., Coffey, V. G., Zhong, Z., Chibalin, A., Hawley, J. A., & Zierath, J. R. (2006) · Diabetes · doi:10.2337/db05-1419 · Cited by 126 · see citing works
Self-citationAMPK-mediated regulation of transcription in skeletal muscle
McGee, S. L., & Hargreaves, M. (2010) · Clinical Science · doi:10.1042/cs20090533 · Cited by 111 · see citing works
Andersson, L. (2008) · Genetica · doi:10.1007/s10709-008-9312-4 · Cited by 110 · see citing works
“The functional significance of the PRKAG3 locus has been further explored by the development of R225Q transgenic mice and PRKAG3 knockout mice, and the causal nature of the R225Q and V224I substitutions were supported by the results of transfection experiments (Barnes et al. 2004).”
BackgroundSelf-citationLuptak, I., Shen, M., He, H., Hirshman, M. F., Musi, N., Goodyear, L. J., Yan, J., Wakimoto, H., Morita, H., Arad, M., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30658 · Cited by 108 · see citing works
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 106 · see citing works
Brandauer, J., Vienberg, S. G., Agerholm, M., Ringholm, S., Risis, S., Larsen, P. S., Kristensen, J. M., Frøsig, C., Leick, L., Fentz, J., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.259515 · Cited by 105 · see citing works
“Skeletal muscle from AMPK γ3 KO mice rapidly fatigues during acute intensive exercise (Barnes et al. 2005) and shows reduced glycogen re-synthesis during recovery (Barnes et al. 2004), indicating a key role of the AMPK γ3 subunit in supporting muscle bioenergetics in response to exercise.”
BackgroundSelf-citationRowe, G. C., Safdar, A., & Arany, Z. P. (2014) · Circulation · doi:10.1161/circulationaha.113.001590 · Cited by 104 · see citing works
“Conversely, mice engineered to express an activated form of AMPK have higher mitochondrial content and more β-oxidation and are resistant to fatigue.(38,39) Other metabolic sensors are less conclusively implicated in exercise adaptations but likely also play a role, including the aging-associated sirtuin family of pro…”
Lee, M.-S., Kim, I.-H., Kim, C.-T., & Kim, Y. (2011) · The Journal of Nutrition · doi:10.3945/jn.111.146050 · Cited by 100 · see citing works
Tang, W., Li, S., Liu, Y., Huang, M., & Ho, C. (2013) · Journal of Functional Foods · doi:10.1016/j.jff.2013.08.007 · Cited by 101 · see citing works
Treebak, J. T., Taylor, E. B., Witczak, C. A., An, D., Toyoda, T., Koh, H., Xie, J., Feener, E. P., Wojtaszewski, J. F. P., Hirshman, M. F., et al. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00297.2009 · Cited by 100 · see citing works
“The ability of the AMPK activator AICAR to increase glucose uptake in skeletal muscle is dependent on both the 2and 3-subunits of AMPK (2, 26), and in the current study we found that S711 of TBC1D4 is regulated by AMPK.”
Lai, Y., Kviklyte, S., Vertommen, D., Lantier, L., Foretz, M., Viollet, B., Hallén, S., & Rider, M. H. (2014) · Biochemical Journal · doi:10.1042/bj20131673 · Cited by 98 · see citing works
AMPK and TBC1D1 Regulate Muscle Glucose Uptake After, but Not During, Exercise and Contraction
Kjøbsted, R., Roll, J. L. W., Jørgensen, N. O., Birk, J. B., Foretz, M., Viollet, B., Chadt, A., Al-Hasani, H., & Wojtaszewski, J. F. P. (2019) · Diabetes · doi:10.2337/db19-0050 · Cited by 97 · 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
“Genetic animal models, in which a single catalytic or regulatory AMPK subunit has been knocked out ( 1, 2, or 3), reveal essentially normal glucose uptake during intermittent tetanic electrical stimulation of ex vivo incubated muscles (3, 24), although recently, AMPK 1-knockout was shown to decrease twitch-stimulated…”
BackgroundThe role of ampk in controlling metabolism and mitochondrial biogenesis during exercise
Marcinko, K., & Steinberg, G. R. (2014) · Experimental Physiology · doi:10.1113/expphysiol.2014.082255 · Cited by 92 · see citing works
“Skeletal muscle is enriched in the ACC2 isoform which is phosphorylated at Ser221 in response to muscle contractions; an effect associated with reductions in ACC activity and malonyl-CoA and increased rates of skeletal muscle FA oxidation (Barnes et al., 2004; Jorgensen et al., 2004; Fujii et al., 2005; Steinberg et a…”
BackgroundLangendorf, C. G., Ngoei, K. R. W., Scott, J. W., Ling, N. X. Y., Issa, S. M. A., Gorman, M. A., Parker, M. W., Sakamoto, K., Oakhill, J. S., & Kemp, B. E. (2016) · Nature Communications · doi:10.1038/ncomms10912 · Cited by 92 · see citing works
AMP-activated protein kinase and the metabolic syndrome
Fryer, L. G., & Carling, D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330362 · Cited by 91 · see citing works
Dissecting the role of AMP-activated protein kinase in human diseases
Li, J., Zhong, L., Wang, F., & Zhu, H. (2017) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2016.12.003 · Cited by 89 · see citing works
Kristensen, 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
Kulkarni, S. S., Karlsson, H., Szekeres, F. L. M., Chibalin, A., Krook, A., & Zierath, J. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.268292 · Cited by 86 · see citing works
Self-citationCostford, S. R., Kavaslar, N., Ahituv, N., Chaudhry, S. N., Schackwitz, W., Dent, R., Pennacchio, L. A., McPherson, R., & Harper, M. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000903 · Cited by 85 · see citing works
Wojtaszewski, J. F. P., & Richter, E. A. (2006) · Essays in Biochemistry · doi:10.1042/bse0420031 · Cited by 109 · see citing works
“Interestingly, however, knockout of either the 1 or the 2 catalytic subunit of AMPK, or the 3 regulatory subunit, does not cause any inhibition of glucose transport in electrically stimulated incubated mouse muscle [20,21].”
BackgroundWolfgang, M. J., & Lane, M. D. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.25.050304.092532 · Cited by 84 · see citing works
Targeting 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 82 · see citing works
Relationship between AMPK and the transcriptional balance of clock-related genes in skeletal muscle
Vieira, E. C., Nilsson, E. C., Nerstedt, A., Ormestad, M., Long, Y. C., García-Rovés, P. M., Zierath, J. R., & Mahlapuu, M. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90510.2008 · Cited by 80 · see citing works
“Moreover, AMPK 3 R225Q transgenic mice were protected against excessive triglyceride accumulation in skeletal muscle and dietaryinduced insulin resistance, presumably because of an increase in lipid oxidation (2).”
InfluentialSelf-citation5′‐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
“Similarly, skeletal muscle glycogen levels (Table 2) and rates of resynthesis after exercise are blunted in Prkag3/ mice ( 13 ).”
BackgroundMethodResultInfluentialSelf-citationJensen, 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
“The AICAR effect appears to be at least partially dependent on AMPK, as a2 and c3 AMPK KO EDL muscles lose part of the suppression of insulin-stimulated S6K1 and 4E-BP1 phosphorylation (Deshmukh et al. 2008).”
BackgroundInfluentialMethotrexate Promotes Glucose Uptake and Lipid Oxidation in Skeletal Muscle via AMPK Activation
Pirkmajer, S., Kulkarni, S. S., Tom, R. Z., Ross, F. A., Hawley, S. A., Hardie, D. G., Zierath, J. R., & Chibalin, A. (2014) · Diabetes · doi:10.2337/db14-0508 · Cited by 80 · see citing works
“Furthermore, MTX enhanced AICAR-stimulated AMPK phosphorylation in WT and AMPK-g3 soleus muscle, despite low endogenous expression in WT soleus muscle (28,36).”
BackgroundMethodInfluentialSelf-citationGeneral aspects of muscle glucose uptake
Alvim, R. D. O., CHEUHEN, M. R., MACHADO, S. R., de Sousa, A. G. P., & SANTOS, P. C. J. L. (2015) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765201520140225 · Cited by 80 · see citing works
LKB1 and AMPK and the regulation of skeletal muscle metabolism
Koh, H.-J., Brandauer, J., & Goodyear, L. J. (2008) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e3282fb7b76 · Cited by 78 · 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
Long, Y. C., Barnes, B. R., Mahlapuu, M., Steiler, T. L., Martinsson, S., Leng, Y., Wallberg‐Henriksson, H., Andersson, L., & Zierath, J. R. (2005) · Diabetologia · doi:10.1007/s00125-005-1962-5 · Cited by 77 · see citing works
Self-citationChronic elevated calcium blocks AMPK-induced GLUT-4 expression in skeletal muscle
Park, S., Scheffler, T. L., Gunawan, A. M., Shi, H., Zeng, C., Hannon, K. M., Grant, A. L., & Gerrard, D. E. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00114.2008 · Cited by 76 · see citing works
Kjøbsted, R., Pedersen, A. J. T., Hingst, J. R., Sabaratnam, R., Birk, J. B., Kristensen, J. M., Højlund, K., & Wojtaszewski, J. F. P. (2016) · Diabetes · doi:10.2337/db15-1034 · Cited by 75 · see citing works
“Thus, in rodent skeletal muscle, AMPKg3 is reported to be involved in glucose uptake, insulin sensitivity, and mitochondrial biogenesis (5,41,43), whereas overexpression of an active AMPK-g1 subunit increases GLUT4 protein content and decreases PDK4 mRNA, potentially enhancing glucose uptake and glycolytic flux, respe…”
BackgroundBultot, L., Jensen, T. E., Lai, Y., Madsen, A. B., Collodet, C., Kviklyte, S., Deák, M., Yavari, A., Foretz, M., Ghaffari, S., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00237.2016 · Cited by 75 · see citing works
“, soleus) mouse muscles, as previously described (2, 49).”
BackgroundMethodInfluentialThe 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
Collodet, C., Foretz, M., Deák, M., Bultot, L., Métairon, S., Viollet, B., Lefebvre, G., Raymond, F., Parisi, A., Civiletto, G., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900841r · Cited by 74 · see citing works
Lessons to learn about postmortem metabolism using the AMPKγ3R200Q mutation in the pig
Scheffler, T. L., Park, S., & Gerrard, D. E. (2011) · Meat Science · doi:10.1016/j.meatsci.2011.04.030 · Cited by 74 · see citing works
“Further, Barnes et al. (2004) demonstrated that γ3R225Q mice maintain higher rates of fatty acid oxidation when exposed a high fat diet, thereby protecting them against triglyceride accumulation and insulin resistance.”
BackgroundBarré, L. K., Richardson, C., Hirshman, M. F., Brozinick, J. T., Fiering, S., Kemp, B. E., Goodyear, L. J., & Witters, L. A. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00369.2006 · Cited by 72 · see citing works
“Based on transfection of COS cells, the R225Q 3 mutation is reported to activate AMPK (5).”
BackgroundKong, B. C., Hudson, N. J., Seo, D., Lee, S., Khatri, B., Lassiter, K., Cook, D., Piekarski, A., Dridi, S., Anthony, N. B., et al. (2017) · BMC Genomics · doi:10.1186/s12864-016-3471-y · Cited by 72 · see citing works
Osler, M. E., & Zierath, J. R. (2007) · Endocrinology · doi:10.1210/en.2007-1441 · Cited by 71 · see citing works
“Also, much attention has been directed toward the particular contribution of the -subunit, because mutations of the 1- of 3-subunit have been associated with enhancements associated with an exercise response and increased energy metabolism (31, 74).”
Self-citation
- 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 › Adipose Tissue and Metabolism
- Health Sciences › Medicine › Rheumatology › 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
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
