The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Exercise Increases Nuclear AMPK α2 in Human Skeletal Muscle
Open accessAbstract
An acute bout of exercise increases skeletal muscle glucose uptake, improves glucose homeostasis and insulin sensitivity, and enhances muscle oxidative capacity. Recent studies have shown an association between these adaptations and the energy-sensing 5' AMP-activated protein kinase (AMPK), the activity of which is increased in response to exercise. Activation of AMPK has been associated with enhanced expression of key metabolic proteins such as GLUT-4, hexokinase II (HKII), and mitochondrial enzymes, similar to exercise. It has been hypothesized that AMPK might regulate gene and protein expression through direct interaction with the nucleus. The purpose of this study was to determine if nuclear AMPK alpha(2) content in human skeletal muscle was increased by exercise. Following 60 min of cycling at 72 +/- 1% of VO(2peak) in six male volunteers (20.6 +/- 2.1 years; 72.9 +/- 2.1 kg; VO(2peak) = 3.62 +/- 0.18 l/min), nuclear AMPK alpha(2) content was increased 1.9 +/- 0.4-fold (P = 0.024). There was no change in whole-cell AMPK alpha(2) content or AMPK alpha(2) mRNA abundance. These results suggest that nuclear translocation of AMPK might mediate the effects of exercise on skeletal muscle gene and protein expression.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“In a feed forward fashion AMPK can translocate to the nucleus [24,27] where it regulates Histone de-aceytlases, transcription factors and transcriptional co-activators such as histone deacetylase 5 (HDAC5), myocyte enhancing factor 2 (MEF2) and peroxisome proliferator activated receptor-γ co-activator-1α (PGC-1α) respectively (Figure 1) [28][29][30].”
From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [27]
Citations
Cites
Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
Winder, W. W., Holmes, B. F., Rubink, D. S., Jensen, E. B., Chen, M., & Holloszy, J. O. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.6.2219 · Cited by 709
Invited Review: Contractile activity-induced mitochondrial biogenesis in skeletal muscle
Hood, D. A. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.3.1137 · Cited by 692
Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis
Bergeron, R., Ren, J. M., Cadman, K. S., Moore, I. K., Perret, P., Pypaert, M., Young, L. H., Semenkovich, C. F., & Shulman, G. I. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.6.e1340 · Cited by 561
Invited Review: Effects of acute exercise and exercise training on insulin resistance
Henriksen, E. J. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01219.2001 · Cited by 535
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
Self-citationHolmes, B. F., Kurth-Kraczek, E. J., & Winder, W. W. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.87.5.1990 · Cited by 489
Salt, I. P., Celler, J. W., Hawley, S. A., Prescott, A. R., Woods, A., Carling, D., & Hardie, D. G. (1998) · Biochemical Journal · doi:10.1042/bj3340177 · Cited by 437
Mechanism for Fatty Acid “Sparing” Effect on Glucose-induced Transcription
Kawaguchi, T., Osatomi, K., Yamashita, H., Kabashima, T., & Uyeda, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107895200 · Cited by 424
Musi, N., Fujii, N., Hirshman, M. F., Ekberg, I., Fröberg, S., Ljungqvist, O., Thorell, A., & Goodyear, L. J. (2001) · Diabetes · doi:10.2337/diabetes.50.5.921 · Cited by 371 · cited 1×
“AMPK complexes containing the catalytic 2 subunit are preferentially activated during exercise at intensities 70% VO2peak, in both normal (3) and type 2 diabetic subjects (4).”
BackgroundLo, W., Duggan, L. J., Tolga, N. C., Emre, N. C. T., Belotserkovskya, R., Lane, W. S., Shiekhattar, R., & Berger, S. L. (2001) · Science · doi:10.1126/science.1062322 · Cited by 369
Cited by
Sorted by citations
Items 101–159 of 159
Shugrue, C., Alexandre, M., de Villalvilla, A. P. E. D., Kolodecik, T. R., Young, L. H., Gorelick, F. S., & Thrower, E. C. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00082.2012 · Cited by 18
AMPK/mTOR balance during exercise: implications for insulin resistance in aging muscle
Mingzheng, X., & You, W. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05362-4 · Cited by 22
Efeitos moleculares do exercício físico sobre as vias de sinalização insulínica
Ropelle, E. R., Pauli, J. R., & Carvalheira, J. B. C. (2005) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · doi:10.5016/297 · Cited by 16
Kim, N., Lee, J. O., Lee, H., Lee, S., Moon, J. W., Kim, S. J., Park, S. H., & Kim, H. S. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.03.023 · Cited by 16
Tharappel, A. M., Harish, C., Lakshmi, M. N., Harsha, K., Mallappa, O., Kumar, V. S., Shree, N., Geetha, V., Balamurali, G. V., Gopala, A. S., et al. (2014) · Cardiovascular Diabetology · doi:10.1186/1475-2840-13-27 · Cited by 16
Chan, F. K., Hsu, C., Li, T., Chen, W.-H., Tseng, K.-T., & Chao, P. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.05.008 · Cited by 16
Augmented muscle glycogen utilization following a single session of sprint training in hypoxia
Kasai, N., Tanji, F., Ishibashi, A., Ohnuma, H., Takahashi, H., Goto, K., & Suzuki, Y. (2021) · European Journal of Applied Physiology · doi:10.1007/s00421-021-04748-8 · Cited by 16
Tarini, V. A. F., Carnevali, L. C., Arida, R. M., Cunha, C. A., Alves, E. D. S., Seeleander, M. C. L., Schmidt, B. J., & Faloppa, F. (2012) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-012-0224-5 · Cited by 15
E-Cadherin: A conductor of cellular signaling
Kehrberg, R. J., & DeMali, K. A. (2025) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2025.102559 · Cited by 15
Targeting AMPK for Therapeutic Intervention in Type 2 Diabetes
Kodiha, M., & Stochaj, U. (2011) · InTech eBooks · doi:10.5772/20930 · Cited by 14
Qi, Z., Zhai, X., & Ding, S. (2013) · SpringerPlus · doi:10.1186/2193-1801-2-693 · Cited by 12
Leptin stimulation of COXIV is impaired in obese skeletal muscle myotubes
McAinch, A. J., Steinberg, G. R., Mollica, J. P., O’Brien, P. E., Dixon, J. B., Kemp, B. E., & Cameron‐Smith, D. (2007) · Obesity Research & Clinical Practice · doi:10.1016/j.orcp.2006.10.003 · Cited by 12
Self-citationGaidhu, M. P., & Ceddia, R. B. (2009) · Clinical Lipidology · doi:10.2217/clp.09.30 · Cited by 12
Gehlert, S., Klinz, F., Willkomm, L., Schiffer, T., Suhr, F., & Bloch, W. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050646 · Cited by 12
Saks, V. A., Schlattner, U., Tokarska-Schlattner, M., Wallimann, T., Bagur, R., Zorman, S., Pelosse, M., Santos, P. D. D., Boucher, F. R., Käämbre, T., et al. (2013) · Springer series in biophysics · doi:10.1007/978-3-642-38505-6_11 · Cited by 13
CaMK4: Structure, physiological functions, and therapeutic potential
Xu, H., Liang, Y., Gao, X., Chen, Y., Wang, Y., Wang, F., & Hou, X. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116204 · Cited by 11
Díaz‐Lara, J., Reisman, E., Botella, J., Probert, B., Burke, L. M., Bishop, D. J., & Lee, M. J. (2024) · Acta Physiologica · doi:10.1111/apha.14215 · Cited by 10
Ziegler, N., Bader, E., Epanchintsev, A., Margerie, D., Kannt, A., & Schmoll, D. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013990 · Cited by 10
Dzeja, P. P., & Terzic, A. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_24 · Cited by 10
The role of AMP-activated protein kinase in fuel selection by the stressed heart
Russell, R. R. (2003) · Current Hypertension Reports · doi:10.1007/s11906-003-0053-6 · Cited by 11
Ya, R., & Downs, S. M. (2012) · Zygote · doi:10.1017/s0967199412000457 · Cited by 9
Oligschlaeger, Y., Miglianico, M., Dahlmans, V. E. H., Rubio-Villena, C., Chanda, D., García-Gimeno, M. A., Coumans, W. A., Liu, Y., Voncken, J. W., Luiken, J. J. F. P., et al. (2016) · Biochemical Journal · doi:10.1042/bj20151035 · Cited by 9
Does AMPK bind glycogen in skeletal muscle or is the relationship correlative?
Frankish, B. P., & Murphy, R. M. (2024) · Essays in Biochemistry · doi:10.1042/ebc20240006 · Cited by 7
Xu, H., Frankenberg, N. T., Lamb, G. D., Gooley, P. R., Stapleton, D., & Murphy, R. M. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00047.2016 · Cited by 7
Metabolic Consequences of Obesity and Their Management
Freemark, M. (2005) · Clinical Pediatric Endocrinology · doi:10.1002/9780470987117.ch20 · Cited by 7
The Link Between Dietary Timing and Exercise Performance Through Adipocyte AMPKα2 Signaling
Kim, S., Baek, J., & Kim, M. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136061 · Cited by 6
AMP-Activated Protein Kinase: A Metabolic Stress Sensor in the Heart
Pelosse, M., Tokarska-Schlattner, M., & Schlattner, U. (2015) · Springer eBooks · doi:10.1007/978-3-319-15263-9_10 · Cited by 4
Wette, S. G., Lamb, G. D., & Murphy, R. M. (2021) · Acta Physiologica · doi:10.1111/apha.13730 · Cited by 4
Paromomycin targets HDAC1-mediated SUMOylation and IGF1R translocation in glioblastoma
Min, Z., Guo, Y., & Ning, L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1490878 · Cited by 3
Matrix mechanics couple contractility to metabolic adaptation in cancer cells
Toth, J. M., Jaganathan, A., Basir, R., Pieuchot, L., Shen, Y., Reinhart‐King, C. A., & Shenoy, V. B. (2026) · Acta Biomaterialia · doi:10.1016/j.actbio.2026.06.056 · Cited by 3
Scheffler, T. L., & Gerrard, D. E. (2016) · Journal of Animal Science · doi:10.2527/jas.2015-0055 · Cited by 3
Freemark, M. (2009) · Wiley eBooks · doi:10.1002/9781444316728.ch20 · Cited by 3
Lü, H. (2017) · Current Pharmacology Reports · doi:10.1007/s40495-017-0091-4 · Cited by 2
Contributions of AMP kinase to the Pathogenesis of Type 2 Diabetes and Neurodegenerative Diseases
Kodiha, M., Mahboubi, H., & Stochaj, U. (2013) · Wiley eBooks · doi:10.1002/9781118395318.ch22 · Cited by 2
Cellular lipids in the molecular pathogenesis of obesity
Matumba, M. G., Ayeleso, A. O., Ntambi, J. M., & Mukwevho, E. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95582-9.00006-1 · Cited by 1
Srivastava, S. P., Kopasz-Gemmen, O., Kunamneni, A., Thurman, A., Yoshida, S., Ozkan, E. E., Swaroop, V., Nanwani, R., Arora, A., Joshi, A., et al. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03078-y · Cited by 1
The epigenetic landscape of skeletal muscle in response to exercise and aging
Champsi, S., & Hood, D. A. (2026) · FEBS Journal · doi:10.1111/febs.70591 · Cited by 1
Gao, J., Xu, Y., Jiang, W., Wang, Z., Wang, L., & Zhang, H. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153885 · Cited by 1
Epigenetics in the Pathophysiology of Type 2 Diabetes
Ling, C. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-385083-6.00018-8 · Cited by 1
Epigenetics and Type 2 Diabetes
Ling, C., Rönn, T., & Nitert, M. D. (2011) · Springer eBooks · doi:10.1007/978-1-84882-644-1_9 · Cited by 1
Egan, B. (2008) · Dublin City University Open Access Institutional Repository (Dublin City University)
Regulation of skeletal muscle glucose transporter 4 expression in fructose-fed exercised rats
Goyaram, V. (2013) · Open University of Cape Town (University of Cape Town)
Yeo, W. K. (2010) · RMIT Research Repository (RMIT University Library) · doi:10.25439/rmt.27351036
MacKrell, J. G. (2013) · Deep Blue (University of Michigan)
Metcalfe, R. S. (2015) · The University of Bath Online Publications Store (The University of Bath) · doi:10.13140/rg.2.1.4944.0088
Neto, F., & Ribeiro, A. (2015) · Aleph UCLA Undergraduate Research Journal for the Humanities and Social Sciences
Fathi, M. (2016) · Journal of Advances in Medical and Biomedical Research
Freemark, M. (2005) · CRC Press eBooks · doi:10.1201/9781420038798.ch11
The Role of AMP-Activated Protein Kinase (AMPK) in Hypoxic Chemotransduction by the Carotid Body
Jordan, H. L. (2012) · OhioLink ETD Center (Ohio Library and Information Network)
Yousefi, M., & TaheriChadorneshin, H. (2018) · DOAJ (DOAJ: Directory of Open Access Journals)
Hardman, S. E. (2014) · ScholarsArchive (Brigham Young University)
Skeletal muscle fat metabolism during post-exercise recovery in humans
Kimber, N. E. (2004)
Current literature in diabetes
(2003) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.349
(2014) · CRC Press eBooks · doi:10.1201/b16783-2
Paromomycin Inhibits HDAC1-Dependent SUMOylation and IGF1R Membrane Translocation in Glioblastoma
Mitchell, S., Brown, O., & Walker, J. (2023) · Specialty journal of Pharmacognosy Phytochemistry and Biotechnology · doi:10.51847/zlsy1ptrqd
Ribeiro, J. N. D. S., Ribeiro, P. L. B. D. S., de Vasconcelos, A. R., Guimarães, F. L. R., Júnior, F. F. L., Cruz, P. W. D. S., Carvalho, B. D. M., & Vancea, D. M. M. (2026) · Revista Multidisciplinar do Nordeste Mineiro · doi:10.66104/yb7x0d86
Wang, H., Hao, J., Bae, J. H., & Cartee, G. D. (2026) · Experimental Gerontology · doi:10.1016/j.exger.2026.113212
Estrogen Dependent Regulation of the Amp-Activated Protein Kinase Pathway
Lipovka, Y. (2015) · UA Campus Repository (The University of Arizona)
Metadata
- Authors
- McGee, S. L., Howlett, K. F., Starkie, R. L., Cameron-Smith, D., Kemp, B. E., & Hargreaves, M.
- Affiliations
- Deakin University (AU)
- Exercise, Muscle and Metabolism Unit, School of Health Sciences, Deakin University, Burwood, Australia
- St Vincent's Hospital Melbourne (AU)
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2003-04-01
- Volume
- 52
- Issue
- 4
- Pages
- 926-928
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2124798116
- Cited by
- 160
- References
- 25
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 6 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 12 · 2019: 2 · 2018: 3 · 2017: 7 · 2016: 10 · 2015: 10 · 2014: 7 · 2013: 8 · 2012: 9
- FWCI
- 2.77
- Type
- journal article
- Language
- en
- Open access
- green
- figshare.com
- Licence
- cc-by
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- AMPK, AMPKα2, nuclear translocation, physical activity, skeletal muscle, GLUT4, hexokinase 2, insulin sensitivity, glucose uptake, mitochondrial enzymes, gene expression regulation, cycling exercise
- MeSH terms
- Adult, Cell Nucleus, Humans, Male, Multienzyme Complexes, Oxygen Consumption, RNA, Messenger, Time Factors, Exercise, Protein Serine-Threonine Kinases, Muscle, Skeletal, 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