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The role of AMP‐activated protein kinase in mitochondrial biogenesis
Open accessAbstract
While it has been known for more than 75 years that physical activity is associated with increased mitochondrial content in muscle, the molecular mechanism for this adaptive process has only recently been elucidated. This brief review examines existing studies that have identified AMPK‐activated protein kinase (AMPK) and several other key regulators of mitochondrial biogenesis, including peroxisome proliferator‐activated receptor‐γ coactivator‐1α and ‐1β, calcium/calmodulin‐dependent protein kinase IV, and nitric oxide. In addition, the potential role of mitochondrial dysfunction in the pathogenesis of insulin resistance associated with ageing and type 2 diabetes mellitus is also discussed.
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Cites
Calcium's Role in Mechanotransduction during Muscle Development
Benavides Damm, T., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,502
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864
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
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734
Cellular mechanisms of insulin resistance
Shulman, G. I. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10583 · Cited by 2,714
Self-citationImpaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
Petersen, K. F., Dufour, S., Befroy, D., Garcia, R., & Shulman, G. I. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031314 · Cited by 2,193
Self-citationMitochondrial dysfunction in the elderly: possible role in insulin resistance
Petersen, K. F., Befroy, D., Dufour, S., Dziura, J., Ariyan, C., Rothman, D. L., DiPietro, L., Cline, G. W., & Shulman, G. I. (2003) · Science · doi:10.1126/science.1082889 · Cited by 2,107
Self-citationPatti, M. E., Butte, A. J., Crunkhorn, S., Cusi, K., Berria, R., Kashyap, S., Miyazaki, Y., Kohane, I., Costello, M., Saccone, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1032913100 · Cited by 1,952
Cited by
Adipocyte dysfunctions linking obesity to insulin resistance and type 2 diabetes.
Guilherme, A., Virbasius, J. V., Puri, V., & Czech, M. P. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2391 · Cited by 2,292
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655
AMPK and PPARδ Agonists Are Exercise Mimetics
Narkar, V. A., Downes, M., Yu, R. T., Embler, E., Wang, Y.-X., Banayo, E., Mihaylova, M. M., Nelson, M. C., Zou, Y., Juguilon, H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.051 · Cited by 1,222
Role of Mitochondrial Dysfunction in Insulin Resistance
Kim, J.-A., Wei, Y., & Sowers, J. R. (2008) · Circulation Research · doi:10.1161/circresaha.107.165472 · Cited by 1,103
Transcriptional control of mitochondrial biogenesis: the central role of PGC-1
Ventura-Clapier, R., Garnier, A., & Veksler, V. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn098 · Cited by 932
Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742
Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740
UCP2 mediates ghrelin’s action on NPY/AgRP neurons by lowering free radicals
Andrews, Z. B., Liu, Z.-W., Walllingford, N., Erion, D. M., Borok, E., Friedman, J. M., Tschöp, M. H., Shanabrough, M., Cline, G., Shulman, G. I., et al. (2008) · Nature · doi:10.1038/nature07181 · Cited by 710
Self-citationMitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment
Golpich, M., Amini, E., Mohamed, Z., Azman Ali, R., Mohamed Ibrahim, N., & Ahmadiani, A. (2017) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12655 · Cited by 532
AMPK: restoring metabolic homeostasis over space and time
Trefts, E., & Shaw, R. J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.015 · Cited by 448
Gibala, M. J., McGee, S. L., Garnham, A. P., Howlett, K. F., Snow, R. J., & Hargreaves, M. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90880.2008 · Cited by 427
Mungai, P. T., Waypa, G. B., Jairaman, A., Prakriya, M., Dokic, D., Ball, M. K., & Schumacker, P. T. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05124-11 · Cited by 385
Choi, C. S., Savage, D. B., Kulkarni, A., Yu, X. X., Liu, Z.-X., Morino, K., Kim, S., Distefano, A., Samuel, V. T., Neschen, S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704213200 · Cited by 383
Self-citationAMPK 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
Yau, S. Y., Li, A., Hoo, R. L. C., Ching, Y. P., Christie, B. R., Lee, T. M. C., Xu, A., & So, K.-F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415219111 · Cited by 326
AMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286
Mitochondrial adaptations to physiological vs. pathological cardiac hypertrophy
Abel, E. D., & Doenst, T. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr015 · Cited by 263
TBK1 at the Crossroads of Inflammation and Energy Homeostasis in Adipose Tissue
Zhao, P., Wong, K. I., Sun, X., Reilly, S. M., Uhm, M., Liao, Z., Skorobogatko, Y., & Saltiel, A. R. (2018) · Cell · doi:10.1016/j.cell.2018.01.007 · Cited by 250
Eid, H. M., Martineau, L. C., Saleem, A., Muhammad, A., Vallerand, D., Benhaddou-Andaloussi, A., Nistor, L., Afshar, A., Arnason, J. T., & Haddad, P. S. (2010) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200900218 · Cited by 218
Agonist-modulated Regulation of AMP-activated Protein Kinase (AMPK) in Endothelial Cells
Levine, Y. C., Li, G. K., & Michel, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702182200 · Cited by 207
Wang, L., Mascher, H., Psilander, N., Blomstrand, E., & Sahlin, K. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00086.2011 · Cited by 181
Role of mitochondrial homeostasis and dynamics in Alzheimer's disease
Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175
Gomes, A. P., Duarte, F. V., Nunes, P., Hubbard, B. P., Teodoro, J. S., Varela, A. T., Jones, J. G., Sinclair, D. A., Palmeira, C. M., & Rolo, A. P. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.008 · Cited by 159
Bhatti, G. K., Reddy, A. P., Reddy, P. H., & Bhatti, J. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00369 · Cited by 145
Nitric Oxide in Skeletal Muscle: Role on Mitochondrial Biogenesis and Function
Tengan, C., Rodrigues, G., & Godinho, R. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131217160 · Cited by 123
Yeo, W. K., McGee, S. L., Carey, A. L., Paton, C. D., Garnham, A. P., Hargreaves, M., & Hawley, J. A. (2010) · Experimental Physiology · doi:10.1113/expphysiol.2009.049353 · Cited by 117
Seo, S., Lee, M.-S., Chang, E., Shin, Y., Oh, S., Kim, I.-H., & Kim, Y. (2015) · Nutrients · doi:10.3390/nu7095385 · Cited by 100
“AMPK also regulates energy metabolism by increasing the gene expression of PGC-1α and SIRT1, which are involved in fatty acid oxidation [7–10,44].”
BackgroundMorris, G., Anderson, G., Berk, M., & Maes, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8477-8 · Cited by 96
Coll, T., Álvarez-Guardia, D., Barroso, E., Gómez-Foix, A. M., Palomer, X., Laguna, J. C., & Vázquez-Carrera, M. (2010) · Endocrinology · doi:10.1210/en.2009-1211 · Cited by 90
Chowdhury, S. K. R., Dobrowsky, R. T., & Fernyhough, P. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.06.007 · Cited by 82
Han, C. Y., Ki, S. H., Kim, Y. W., Noh, K., Lee, D. Y., Kang, B., Ryu, J.-H., Jeon, R., Kim, E. H., Hwang, S. J., et al. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3190 · Cited by 63
Shen, W., Hao, J., Tian, C., Ren, J., Yang, L., Li, X., Luo, C., Cotma, C. W., & Liu, J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002328 · Cited by 63
Augmenting energy expenditure by mitochondrial uncoupling: A role of AMP-activated protein kinase
Klaus, S., Keipert, S., Rossmeisl, M., & Kopecky, J. (2012) · Genes & Nutrition · doi:10.1007/s12263-011-0260-8 · Cited by 44
Hawley, J. A., Gibala, M. J., & Bermon, S. (2007) · Journal of Sports Sciences · doi:10.1080/02640410701607411 · Cited by 43
H. Swerdlow, R. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072535 · Cited by 35
Dibutyltin promotes oxidative stress and increases inflammatory mediators in BV-2 microglia cells
Chantong, B., Kratschmar, D. V., Lister, A., & Odermatt, A. (2014) · Toxicology Letters · doi:10.1016/j.toxlet.2014.03.001 · Cited by 34
Nitric oxide in exercise physiology: past and present perspectives
Mueller, B. J., Roberts, M. D., Mobley, C. B., Judd, R. L., & Kavazis, A. N. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2024.1504978 · Cited by 32
Metadata
- Authors
- Reznick, R. M., & Shulman, G. I.
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2006-06-19
- Volume
- 574
- Issue
- 1
- Pages
- 33-39
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- OpenAlex
- W2158905364
- Cited by
- 373
- References
- 48
- FWCI
- 8.60
- Type
- journal article
- Language
- en
- Open access
- green
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