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AMPK β1 Deletion Reduces Appetite, Preventing Obesity and Hepatic Insulin Resistance
Open accessAbstract
The AMP-activated protein kinase (AMPK) is an alphabetagamma heterotrimer that regulates appetite and fuel metabolism. We have generated AMPK beta1(-/-) mice on a C57Bl/6 background that are viable, fertile, survived greater than 2 years, and display no visible brain developmental defects. These mice have a 90% reduction in hepatic AMPK activity due to loss of the catalytic alpha subunits, with modest reductions of activity detected in the hypothalamus and white adipose tissue and no change in skeletal muscle or heart. On a low fat or an obesity-inducing high fat diet, beta1(-/-) mice had reduced food intake, reduced adiposity, and reduced total body mass. Metabolic rate, physical activity, adipose tissue lipolysis, and lipogenesis were similar to wild type littermates. The reduced appetite and body mass of beta1(-/-) mice were associated with protection from high fat diet-induced hyperinsulinemia, hepatic steatosis, and insulin resistance. We demonstrate that the loss of beta1 reduces food intake and protects against the deleterious effects of an obesity-inducing diet.
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“AMPK β1 KO mice have reduced AMPK activity in liver but not skeletal muscle, are hyperphagic and as a result have lower body weight, adiposity and hepatic lipid accumulation, and are protected from high-fat diet induced insulin resistance [27].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [27]
In the citing paper
“AMPK β1 KO mice have reduced AMPK activity in liver but not skeletal muscle, are hyperphagic and as a result have lower body weight, adiposity and hepatic lipid accumulation, and are protected from high-fat diet induced insulin resistance [27].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [27]
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
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
Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB
Cai, D., Yuan, M., Frantz, D. F., Melendez, P. A., Hansen, L., Lee, J., & Shoelson, S. E. (2005) · Nature Medicine · doi:10.1038/nm1166 · Cited by 2,245
The Kinase LKB1 Mediates Glucose Homeostasis in Liver and Therapeutic Effects of Metformin
Shaw, R. J., Lamia, K. A., Vasquez, D., Koo, S.-H., Bardeesy, N., DePinho, R. A., Montminy, M., & Cantley, L. C. (2005) · Science · doi:10.1126/science.1120781 · Cited by 1,950
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
Self-citationAMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus
Minokoshi, Y., Alquier, T., Furukawa, N., Kim, Y.-B., Lee, A., Xue, B., Mu, J., Foufelle, F., Ferré, P., Birnbaum, M. J., et al. (2004) · Nature · doi:10.1038/nature02440 · Cited by 1,637
Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264
The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
Koo, S., Flechner, L., Qi, L., Zhang, X., Screaton, R. A., Jeffries, S., Hedrick, S. A., Xu, W., Boussouar, F., Brindle, P. K., et al. (2005) · Nature · doi:10.1038/nature03967 · Cited by 1,026
Petersen, K. F., Dufour, S., Befroy, D., Lehrke, M., Hendler, R. E., & Shulman, G. I. (2005) · Diabetes · doi:10.2337/diabetes.54.3.603 · Cited by 911
AMP-activated Protein Kinase Plays a Role in the Control of Food Intake
Andersson-Hall, U. K., Filipsson, K., Abbott, C. R., Woods, A., Smith, K. L., Bloom, S. R., Carling, D., & Small, C. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300557200 · Cited by 777
Ueki, K., Kondo, T., & Kahn, C. R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5434-5446.2004 · Cited by 686
Mammalian AMP-activated protein kinase subfamily
Stapleton, D., Mitchelhill, K. I., Gao, G., Widmer, J., Michell, B. J., Teh, T., House, C. M., Fernandez, C. S., Cox, T., Witters, L. A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.611 · Cited by 652
Self-citationHow Obesity Causes Diabetes: Not a Tall Tale
Lazar, M. A. (2005) · Science · doi:10.1126/science.1104342 · Cited by 577
AMPK is essential for energy homeostasis regulation and glucose sensing by POMC and AgRP neurons
Claret, M., Smith, M. A., Batterham, R. L., Selman, C., Choudhury, A. I., Fryer, L. G. D., Clements, M., Al‐Qassab, H., Heffron, H., Xu, A. W., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31516 · Cited by 522
Muscle-specific Pparg deletion causes insulin resistance
Hevener, A. L., He, W., Barak, Y., Le, J., Bandyopadhyay, G. K., Olson, P., Wilkes, J. J., Evans, R. M., & Olefsky, J. M. (2003) · Nature Medicine · doi:10.1038/nm956 · Cited by 501
Self-citationThe AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity
Viollet, B., Andreelli, F., Jørgensen, S. B., Perrin, C., Geloen, A., Flamez, D., Mu, J., Lenzner, C., Baud, O., Bennoun, M., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16567 · Cited by 499
Self-citationChronic Exposure to Interleukin-6 Causes Hepatic Insulin Resistance in Mice
Klover, P. J., Zimmers, T. A., Koniaris, L. G., & Mooney, R. A. (2003) · Diabetes · doi:10.2337/diabetes.52.11.2784 · Cited by 488
AMP-activated protein kinase, super metabolic regulator
Kemp, B. E., Stapleton, D., Campbell, D. J., Chen, Z.-P., Murthy, S., Walter, M., Gupta, A., Adams, J. J., Katsis, F., van Denderen, B., et al. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310162 · Cited by 474
Self-citationSteinberg, G. R., Michell, B. J., van Denderen, B. J. W., Watt, M. J., Carey, A. L., Fam, B. C., Andrikopoulos, S., Proietto, J., Görgün, C. Z., Carling, D., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.005 · Cited by 424
Self-citationForetz, M., Ancellin, N., Andréelli, F., Saintillan, Y., Grondin, P., Kahn, A., Thorens, B., Vaulont, S., & Viollet, B. (2005) · Diabetes · doi:10.2337/diabetes.54.5.1331 · Cited by 406
Hypothalamic CaMKK2 Contributes to the Regulation of Energy Balance
Anderson, K. A., Ribar, T. J., Lin, F., Noeldner, P. K., Green, M. F., Muehlbauer, M. J., Witters, L. A., Kemp, B. E., & Means, A. R. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.02.011 · Cited by 385
Self-citationMitchelhill, K. I., Stapleton, D., Gao, G., House, C. M., Michell, B. J., Katsis, F., Witters, L. A., & Kemp, B. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41951-x · Cited by 338
Self-citationCNTF reverses obesity-induced insulin resistance by activating skeletal muscle AMPK
Watt, M. J., Dzamko, N. L., Thomas, W. G., Rose‐John, S., Ernst, M., Carling, D., Kemp, B. E., Febbraio, M. A., & Steinberg, G. R. (2006) · Nature Medicine · doi:10.1038/nm1383 · Cited by 282
Self-citationScott, J. W., van Denderen, B. J. W., Jørgensen, S. B., Honeyman, J. E., Steinberg, G. R., Oakhill, J. S., Iseli, T. J., Koay, A. Z., Gooley, P. R., Stapleton, D., et al. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.10.005 · Cited by 262
Self-citationCarling, D., Aguan, K., Woods, A., Verhoeven, A., Beri, R. K., Brennan, C. H., Sidebottom, C., Davison, M. D., & Scott, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78143-5 · Cited by 253
Andréelli, F., Foretz, M., Knauf, C., Cani, P. D., Perrin, C., Iglesias, M. A., Pillot, B., Bado, A., Tronche, F., Mithieux, G., et al. (2006) · Endocrinology · doi:10.1210/en.2005-0898 · Cited by 244
Thornton, C., Snowden, M. A., & Carling, D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12443 · Cited by 240
Chen, M. B., McAinch, A. J., Macaulay, S. L., Castelli, L. A., O’Brien, P. E., Dixon, J. B., Cameron‐Smith, D., Kemp, B. E., & Steinberg, G. R. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1980 · Cited by 201
Self-citationHorike, N., Sakoda, H., Kushiyama, A., Ono, H., Fujishiro, M., Kamata, H., Nishiyama, K., Uchijima, Y., Kurihara, Y., Kurihara, H., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802537200 · Cited by 197
Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase
Townley, R. A., & Shapiro, L. S. (2007) · Science · doi:10.1126/science.1137503 · Cited by 190
Viollet, B., Mounier, R., Leclerc, J., Yazigi, A., Foretz, M., & Andréelli, F. (2007) · Diabetes & Metabolism · doi:10.1016/j.diabet.2007.10.004 · Cited by 168
Posttranslational Modifications of the 5′-AMP-activated Protein Kinase β1 Subunit
Mitchelhill, K. I., Michell, B. J., House, C. M., Stapleton, D., Dyck, J. R. B., Gamble, J., Ullrich, C., Witters, L. A., & Kemp, B. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24475 · Cited by 158
Self-citationKim, J.-H., Kim, J. E., Liu, H.-Y., Cao, W., & Chen, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708568200 · Cited by 154
Gentry, M. S., Dowen, R. H., Worby, C. A., Mattoo, S., Ecker, J. R., & Dixon, J. E. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704094 · Cited by 150
Dasgupta, B., & Milbrandt, J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.01.005 · Cited by 136
Iseli, T. J., Walter, M., van Denderen, B. J. W., Katsis, F., Witters, L. A., Kemp, B. E., Michell, B. J., & Stapleton, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412993200 · Cited by 134
Self-citationExpression 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
Self-citationInterleukin-6 release from human skeletal muscle during exercise: relation to AMPK activity
MacDonald, C., Wojtaszewski, J. F. P., Pedersen, B. K., Kiens, B., & Richter, E. A. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00242.2003 · Cited by 105
Steinberg, G. R., Watt, M. J., Fam, B. C., Proietto, J., Andrikopoulos, S., Allen, A. M., Febbraio, M. A., & Kemp, B. E. (2006) · Endocrinology · doi:10.1210/en.2005-1587 · Cited by 103
Self-citationRole of malonyl-CoA in heart disease and the hypothalamic control of obesity
Folmes, C. D. L., & LOPASCHUK, G. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.10.008 · Cited by 98
Sell, H., Dietze‐Schroeder, D., Eckardt, K., & Eckel, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.010 · Cited by 78
AMP-activated Protein Kinase Subunit Interactions
Iseli, T. J., Oakhill, J. S., Bailey, M. F., Wee, S., Walter, M., van Denderen, B. J., Castelli, L. A., Katsis, F., Witters, L. A., Stapleton, D., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708298200 · Cited by 35
Self-citationGlund, 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 35
Research works printed but not linked: 1
- Altschul, 1990, J. Mol. Biol., 215, 403, 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
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López, M., Varela, L., Vazquez, M. J., Rodríguez‐Cuenca, S., González, C. R., Velagapudi, V., Morgan, D. A., Schoenmakers, E., Agassandian, K., Lage, R., et al. (2010) · Nature Medicine · doi:10.1038/nm.2207 · Cited by 686
Metadata
- Authors
- Dzamko, N., van Denderen, B. J. W., Hevener, A. L., Jørgensen, S. B., Honeyman, J., Galic, S., Chen, Z.-P., Watt, M. J., Campbell, D. J., Steinberg, G. R., & Kemp, B. E.
- Affiliations
- The University of Melbourne (AU)
- University of California, Los Angeles (US)
- University of Copenhagen (DK)
- Monash University (AU)
- Corresponding author
- Steinberg, Gregory R.
- Kemp, Bruce E.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 285
- Issue
- 1
- Pages
- 115-122
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2804155
- OpenAlex
- W2028308875
- Cited by
- 175
- References
- 43
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 7 · 2022: 12 · 2021: 11 · 2020: 13 · 2019: 8 · 2018: 10 · 2017: 9 · 2016: 16 · 2015: 9 · 2014: 14 · 2013: 15 · 2012: 15
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Regulation of Appetite and Obesity
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- AMPK, appetite regulation, dietary intake, obesity, hepatic insulin resistance, hyperinsulinemia, hepatic steatosis, high-fat diet, knockout mice, adipose tissue lipolysis, lipogenesis, metabolic rate
- MeSH terms
- AMP-Activated Protein Kinase Kinases, Animals, Appetite, Body Weight, Carbon Dioxide, Darkness, Dietary Fats, Fasting, Feeding Behavior, Gene Expression Regulation, Gluconeogenesis, Insulin, Insulin Resistance, Liver, Mice, Inbred C57BL, Obesity, Organ Specificity, Oxidation-Reduction, Oxygen, Protein Kinases, Respiration, Gene Deletion, Protein Subunits, Hepatocytes, Mice
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