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AMPK and cell proliferation – AMPK as a therapeutic target for atherosclerosis and cancer
Open accessAbstract
AMPK is a serine/threonine protein kinase, which serves as an energy sensor in all eukaryotic cell types. Published studies indicate that AMPK activation strongly suppresses cell proliferation in non‐malignant cells as well as in tumour cells. These actions of AMPK appear to be mediated through multiple mechanisms including regulation of the cell cycle and inhibition of protein synthesis, de novo fatty acid synthesis, specifically the generation of mevalonate as well as other products downstream of mevalonate in the cholesterol synthesis pathway. Cell cycle regulation by AMPK is mediated by up‐regulation of the p53–p21 axis as well as regulation of TSC2–mTOR (mammalian target of rapamycin) pathway. The AMPK signalling network contains a number of tumour suppressor genes including LKB1, p53, TSC1 and TSC2, and overcomes growth factor signalling from a variety of stimuli (via growth factors and by abnormal regulation of cellular proto‐oncogenes including PI3K, Akt and ERK). These observations suggest that AMPK activation is a logical therapeutic target for diseases rooted in cellular proliferation, including atherosclerosis and cancer. In this review, we discuss about exciting recent advances indicating that AMPK functions as a suppressor of cell proliferation by controlling a variety of cellular events in normal cells as well as in tumour cells.
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Citations
Cites
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
The phosphoinositide 3-kinase pathway
Cantley, L. C. (2002) · Science · doi:10.1126/science.296.5573.1655 · Cited by 5,621
Sherr, C. J. (1996) · Science · doi:10.1126/science.274.5293.1672 · Cited by 5,379
The retinoblastoma protein and cell cycle control
Weinberg, R. A. (1995) · Cell · doi:10.1016/0092-8674(95)90385-2 · Cited by 4,862
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
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
Metformin and reduced risk of cancer in diabetic patients
Evans, J. M. M., Donnelly, L. A., Emslie-Smith, A. M., Alessi, D. R., & Morris, A. D. (2005) · BMJ · doi:10.1136/bmj.38415.708634.f7 · Cited by 2,388
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Cyclins and cancer II: Cyclin D and CDK inhibitors come of age
Hunter, T., & Pines, J. (1994) · Cell · doi:10.1016/0092-8674(94)90543-6 · Cited by 2,091
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
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
TOR, a Central Controller of Cell Growth
Schmelzle, T., & Hall, M. N. (2000) · Cell · doi:10.1016/s0092-8674(00)00117-3 · Cited by 1,924
Shaw, R. J., Kosmatka, M., Bardeesy, N., Hurley, R. L., Witters, L. A., DePinho, R. A., & Cantley, L. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308061100 · Cited by 1,797
Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Mäkelä, T. P., Alessi, D. R., & Hardie, D. G. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-28 · Cited by 1,665
AMP-activated protein kinase induces a p53-dependent metabolic checkpoint
Jones, R. G., Plas, D. R., Kubek, S., Buzzai, M., Mu, J., Xu, Y., Birnbaum, M. J., & Thompson, C. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.027 · Cited by 1,619
Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J., & Cantley, L. C. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00568-3 · Cited by 1,555
Very high risk of cancer in familial Peutz–Jeghers syndrome
Giardiello, F. M., Brensinger, J. D., Tersmette, A. C., Goodman, S. N., Petersen, G. M., Booker, S. V., Cruz–Correa, M., & Offerhaus, J. A. (2000) · Gastroenterology · doi:10.1053/gast.2000.20228 · Cited by 1,445
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 1,435
The AMP‐Activated Protein Kinase: Fuel Gauge of the Mammalian Cell?
Hardie, D. G., & Carling, D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00259.x · Cited by 1,317
Yokota, T., Oritani, K., Takahashi, I., Ishikawa, J., Matsuyama, A., Ouchi, N., Kihara, S., Funahashi, T., Tenner, A. J., Tomiyama, Y., et al. (2000) · Blood · doi:10.1182/blood.v96.5.1723 · Cited by 1,297
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
Phosphorylation and Functional Inactivation of TSC2 by Erk
Ma, L., Chen, Z., Erdjument-Bromage, H., Tempst, P., & Pandolfi, P. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.031 · Cited by 1,268
Fingar, D. C., & Blenis, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207542 · Cited by 1,247
The AMP-activated protein kinase pathway – new players upstream and downstream
Hardie, D. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01540 · Cited by 1,143
Graña, X., & Reddy, E. P. (1995) · PubMed · Cited by 1,139
Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E
Fingar, D. C., Salama, S., Tsou, C., Harlow, E., & Blenis, J. (2002) · Genes & Development · doi:10.1101/gad.995802 · Cited by 1,093
The LKB1 tumor suppressor negatively regulates mTOR signaling
Shaw, R. J., Bardeesy, N., Manning, B. D., Lopez, L., Kosmatka, M., DePinho, R. A., & Cantley, L. C. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.06.007 · Cited by 1,077
Insulin Activation of Rheb, a Mediator of mTOR/S6K/4E-BP Signaling, Is Inhibited by TSC1 and 2
Garami, A., Zwartkruis, F. J. T., Nobukuni, T., Joaquin, M., Roccio, M., Stocker, H., Kozma, S. C., Hafen, E., Bos, J. L., & Thomas, G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00220-x · Cited by 1,043
Minireview: The AMP-Activated Protein Kinase Cascade: The Key Sensor of Cellular Energy Status
Hardie, D. G. (2003) · Endocrinology · doi:10.1210/en.2003-0982 · Cited by 994
Bowker, S. L., Majumdar, S. R., Veugelers, P., & Johnson, J. A. (2006) · Diabetes Care · doi:10.2337/diacare.29.02.06.dc05-1558 · Cited by 933
Fingar, D. C., Richardson, C. J., Tee, A. R., Cheatham, L., Tsou, C., & Blenis, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.200-216.2004 · Cited by 868
Bolster, D. R., Crozier, S. J., Kimball, S. R., & Jefferson, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200171200 · Cited by 851
Ouchi, N., Kobayashi, H., Kihara, S., Kumada, M., Sato, K., Inoue, T., Funahashi, T., & Walsh, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310389200 · Cited by 759 · cited 1×
“On the other hand, Ouchi et al. (2004) reported that AMPK activation by adiponectin increased Akt signalling.”
BackgroundSize Control in Animal Development
Conlon, I., & Raff, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80563-2 · Cited by 743
Bråkenhielm, E., Veitonmäki, N., Cao, R., Kihara, S., Matsuzawa, Y., Zhivotovsky, B., Funahashi, T., & Cao, Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308671100 · Cited by 732
Arita, Y., Kihara, S., Ouchi, N., Maeda, K., Kuriyama, H., Okamoto, Y., Kumada, M., Hotta, K., Nishida, M., Takahashi, M., et al. (2002) · Circulation · doi:10.1161/01.cir.0000018622.84402.ff · Cited by 695
Adiponectin: A Novel Adipokine Linking Adipocytes and Vascular Function
Goldstein, B. J., & Scalia, R. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0518 · Cited by 647
Self-citationSynthesis and antitumor activity of an inhibitor of fatty acid synthase
Kuhajda, F. P., Pizer, E. S., Li, J. N., Mani, N. S., Frehywot, G. L., & Townsend, C. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3450 · Cited by 567
Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products
van Slegtenhorst, M. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.6.1053 · Cited by 565
Adiponectin and Breast Cancer Risk
Mantzoros, C., Petridou, E., Dessypris, N., Chavelas, C., Dalamaga, M., Alexe, D. M., Papadiamantis, Y., Markopoulos, C., Spanos, E., Chrousos, G., et al. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031804 · Cited by 533
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 473
Wu, X., Motoshima, H., Mahadev, K., Stalker, T. J., Scalia, R., & Goldstein, B. J. (2003) · Diabetes · doi:10.2337/diabetes.52.6.1355 · Cited by 463
Self-citationHorman, S., Browne, G. J., Krause, U., Patel, J. V., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C. G., & Rider, M. H. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01077-1 · Cited by 454
Association of serum adiponectin levels with breast cancer risk.
Miyoshi, Y., Funahashi, T., Kihara, S., Taguchi, T., Tamaki, Y., Matsuzawa, Y., & Noguchi, S. (2003) · PubMed · Cited by 451
Role of the AMP-activated protein kinase in the cellular stress response
Corton, J. M., Gillespie, J. G., & Hardie, D. G. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00070-1 · Cited by 428
AMPK, the metabolic syndrome and cancer
Luo, Z., Saha, A. K., Xiang, X., & Ruderman, N. B. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.12.011 · Cited by 426
Woods, A., Azzout-Marniche, D., Foretz, M., Stein, S. C., Lemarchand, P., Ferré, P., Foufelle, F., & Carling, D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6704-6711.2000 · Cited by 403
Kimura, N., Tokunaga, C., Dalal, S., Richardson, C., Yoshino, K., Hara, K., Kemp, B. E., Witters, L. A., Mimura, O., & Yonezawa, K. (2003) · Genes to Cells · doi:10.1046/j.1365-2443.2003.00615.x · Cited by 372
Imamura, K., Ogura, T., Kishimoto, A., Kaminishi, M., & Esumi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5627 · Cited by 344
Rattan, R., Giri, S., Singh, A. K., & Singh, I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507443200 · Cited by 339
Cheng, S. W. Y., Fryer, L. G. D., Carling, D., & Shepherd, P. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300534200 · Cited by 331
Lukas, J., Bartkova, J., & Bartek, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.6917 · Cited by 327
The Peutz-Jegher Gene Product LKB1 Is a Mediator of p53-Dependent Cell Death
Karuman, P., Gozani, O., Odze, R. D., Zhou, X. C., Zhu, H., Shaw, R., Brien, T. P., Bozzuto, C. D., Ooi, D., Cantley, L. C., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00258-1 · Cited by 322
Motoshima, H., Wu, X., Mahadev, K., & Goldstein, B. J. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.049 · Cited by 308
Self-citationGrowth suppression by Lkb1 is mediated by a G 1 cell cycle arrest
Tiainen, M., Ylikorkala, A., & Mäkelä, T. P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9248 · Cited by 301
Foretz, M., Carling, D., Guichard, C., Ferré, P., & Foufelle, F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.14767 · Cited by 256
Circulating Adiponectin and Endometrial Cancer Risk
Dal Maso, L., Augustin, L. S. A., Karalis, A., Talamini, R., Franceschi, S., Trichopoulos, D., Mantzoros, C. S., & La Vecchia, C. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031716 · Cited by 256
New roles for the LKB1→AMPK pathway
Hardie, D. G. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.01.006 · Cited by 255
Plasma Adiponectin and Gastric Cancer
Ishikawa, M., Kitayama, J., Kazama, S., Hiramatsu, T., Hatano, K., & Nagawa, H. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.466.11.2 · Cited by 253
Inhibition of fatty acid and cholesterol synthesis by stimulation of AMP‐activated protein kinase
Henin, N., Vincent, M. ‐., Gruber, H. E., & Van Den Berghe, G. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.7.7737463 · Cited by 251
Xiang, X., Saha, A. K., Wen, R., Ruderman, N. B., & Luo, Z. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.133 · Cited by 251
Igata, M., Motoshima, H., Tsuruzoe, K., Kojima, K., Matsumura, T., Kondo, T., Taguchi, T., Nakamaru, K., Yano, M., Kukidome, D., et al. (2005) · Circulation Research · doi:10.1161/01.res.0000185823.73556.06 · Cited by 245
Self-citationMehenni, H., Gehrig, C., Nezu, J.-I., Oku, A., Shimane, M., Rossier, C., Guex, N., Blouin, J.-L., Scott, H. S., & Antonarakis, S. E. (1998) · The American Journal of Human Genetics · doi:10.1086/302159 · Cited by 219
Growth arrest by the LKB1 tumor suppressor: induction of p21WAF1/CIP1
Tiainen, M. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.13.1497 · Cited by 199
Nagata, D., Takeda, R., Sata, M., Satonaka, H., Suzuki, E., Nagano, T., & Hirata, Y. (2004) · Circulation · doi:10.1161/01.cir.0000136025.96811.76 · Cited by 198
LKB1, a protein kinase regulating cell proliferation and polarity
Boudeau, J., Sapkota, G., & Alessi, D. R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00642-2 · Cited by 190
Connections between growth and the cell cycle
Neufeld, T. P., & Edgar, B. A. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80122-1 · Cited by 183
Zhang, Y., Shewry, P. R., Jones, H., Barcelo, P., Lazzeri, P. A., & Halford, N. G. (2001) · The Plant Journal · doi:10.1046/j.1365-313x.2001.01167.x · Cited by 181
Androgens, lipogenesis and prostate cancer
Swinnen, J. V., Heemers, H., de Sande, T. V., Schrijver, E. D., Brusselmans, K., Heyns, W., & Verhoeven, G. (2004) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2004.10.013 · Cited by 176
Adiponectin induces growth arrest and apoptosis of MDA-MB-231 breast cancer cell
Kang, J. H., Lee, Y. Y., Yu, B. Y., Yang, B. S., Cho, K. H., Yoon, D. K., & Roh, Y. K. (2005) · Archives of Pharmacal Research · doi:10.1007/bf02978210 · Cited by 171
Ylikorkala, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.1.45 · Cited by 166
Krause, U., Bertrand, L., & Hue, L. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03074.x · Cited by 163
Forcet, C., Etienne‐Manneville, S., Gaude, H., Fournier, L., Debilly, S., Salmi, M., Baas, A. F., Olschwang, S., Clevers, H. C., & Billaud, M. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi139 · Cited by 157
Leclerc, I., Kahn, A., & Doiron, B. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00745-5 · Cited by 139
Carrera, A. (2004) · Journal of Cell Science · doi:10.1242/jcs.01311 · Cited by 83
Menéndez, J. A., & Lupu, R. (2004) · PubMed · Cited by 77
Jimenez, A. I., Fernández, P., Domı́nguez, O., Dopazo, A., & Sánchez‐Céspedes, M. (2003) · PubMed · Cited by 68
The Effects of Statins on Endothelium, Inflammation and Cardioprotection
Elrod, J. W., & Lefer, D. J. (2005) · Drug News & Perspectives · doi:10.1358/dnp.2005.18.4.908656 · Cited by 34
Kyriakis, J. M. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-26 · Cited by 26
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Budanov, A. V., & Karin, M. (2008) · Cell · doi:10.1016/j.cell.2008.06.028 · Cited by 1,326
Regulation of Immune Responses by mTOR
Powell, J. D., Pollizzi, K. N., Heikamp, E. B., & Horton, M. R. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075024 · Cited by 836
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Dasgupta, B., & Milbrandt, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610068104 · Cited by 723
Alimova, I. N., Liu, B., Fan, Z., Edgerton, S. M., Dillon, T., Lind, S. E., & Thor, A. D. (2009) · Cell Cycle · doi:10.4161/cc.8.6.7933 · Cited by 523
Zheng, B., Jeong, J. H., Asara, J. M., Yuan, Y.-Y., Granter, S. R., Chin, L., & Cantley, L. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.026 · Cited by 359
Metadata
- Authors
- Motoshima, H., Goldstein, B. J., Igata, M., & Araki, E.
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2006-06-19
- Volume
- 574
- Issue
- 1
- Pages
- 63-71
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- OpenAlex
- W1563676220
- Cited by
- 527
- References
- 80
- FWCI
- 12.16
- Type
- journal article
- Language
- en
- Open access
- green
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