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Gene Review

PRKAB1  -  protein kinase, AMP-activated, beta 1 non...

Homo sapiens

Synonyms: 5'-AMP-activated protein kinase subunit beta-1, AMPK, AMPK subunit beta-1, AMPKb, HAMPKb
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Disease relevance of PRKAB1


Psychiatry related information on PRKAB1

  • Here, we identify a role for hypothalamic AMPK in the regulation of feeding behavior and in mediating the anorexic effects of C75 [6].
  • Accompanying this is a decrease in AMPK phosphorylation, reversible upon nicotinic acid treatment, indicating that fatty acids may modulate this kinase's activity after the metabolic challenges posed by food deprivation [7].

High impact information on PRKAB1

  • GSK3 inhibits the mTOR pathway by phosphorylating TSC2 in a manner dependent on AMPK-priming phosphorylation [8].
  • TSC2 Integrates Wnt and Energy Signals via a Coordinated Phosphorylation by AMPK and GSK3 to Regulate Cell Growth [8].
  • Several promising therapeutic strategies based on modulation of AMPK, HIF and other metabolic targets have been proposed to exploit the addiction of tumor cells to increased glucose uptake and glycolysis [9].
  • The adenosine monophosphate (AMP)-activated protein kinase (AMPK) has a crucial role in maintaining cellular energy homeostasis [10].
  • The rapid activation of AMPK in response to Ca(2+) signaling in T lymphocytes thus reveals that TCR triggering is linked to an evolutionally conserved serine kinase that regulates energy metabolism [10].

Chemical compound and disease context of PRKAB1


Biological context of PRKAB1

  • Haplotype structures and large-scale association testing of the 5' AMP-activated protein kinase genes PRKAA2, PRKAB1, and PRKAB1 with type 2 diabetes [16].
  • We find the most prominent expressed form of the hepatic AMPK catalytic subunit (alpha 1) is distinct from the previously cloned kinase subunit (alpha 2) [17].
  • Isoforms of the beta and gamma subunits present in the human genome sequence reveal that the AMPK consists of a family of isoenzymes [17].
  • The tissue distribution of the AMPK activity most closely parallels the low abundance 6-kilobase alpha 1 mRNA distribution and the alpha 1 immunoreactivity rather than alpha 2, with substantial amounts in kidney, liver, lung, heart, and brain [17].
  • Exercise for 3 h increased AdipoR1/R2 mRNA expression as well as phosphorylation of AMPK and acetyl coenzyme A carboxylase in muscle, but had no effect on circulating adiponectin [18].

Anatomical context of PRKAB1

  • Predominant {alpha}2/{beta}2/{gamma}3 AMPK activation during exercise in human skeletal muscle [19].
  • AMPK regulation of the growth of cultured human keratinocytes [20].
  • Importantly, the adipocyte hormones leptin and adiponectin also activate AMPK; remarkably, the same pathway is activated by certain antidiabetic agents such as thiazolidinediones [21].
  • The AMPK pathway in the hypothalamus and peripheral tissues coordinately integrates inputs from multiple hormones, peptides and nutrients to maintain energy homeostasis [5].
  • Activation of AMPK in adipose tissue can be achieved through situations such as fasting and exercise [22].

Associations of PRKAB1 with chemical compounds

  • The mammalian 5'-AMP-activated protein kinase (AMPK) is a heterotrimeric protein consisting of alpha-, beta-, and gamma-subunits [23].
  • Finally, we measured these same variables in addition to protein levels of AMP kinase (AMPK), acetyl phosphorylated AMPK, coenzyme A carboxylase, phosphorylated coenzyme A carboxylase, and phosphatidylinositol 3-kinase in muscle before and after 3 h of intensive exercise in a subgroup of five subjects [18].
  • LMW- and HMW-APM induce apoptosis in nondifferentiated THP-1 cells, reduce macrophage scavenger receptor (MSR) A mRNA expression, and stimulate phosphorylation of adenosine monophosphate-activated protein kinase (AMPK) [24].
  • Thus it is likely that the AMPK-GDE association is a novel mechanism regulating AMPK activity and the resultant fatty acid oxidation and glucose uptake [25].
  • It also increased AMPK and acetyl CoA carboxylase phosphorylation (P-AMPK and P-ACC) and decreased the concentration of malonyl CoA confirming that AMPK activation had occurred [20].

Other interactions of PRKAB1

  • Several nominal associations of variants in PRKAA2 and PRKAB1 with BMI appear to be consistent with statistical noise [16].
  • Porcine COC and DO contained transcripts that corresponded to the expected sizes of the designed primers for PRKAB1 and PRKAG1 [26].
  • These appear to be followed by the specific activation of AMPK and the up-regulation of p53, p21, and Bax by genistein [2].
  • The N-terminal region of beta2 differs significantly from that of the previously characterized isoform (beta1), suggesting that this region could play a role in isoform-specific AMPK activity [27].
  • Distinct protein kinases and transcription factors emerge as possible interfaces that integrate the mechanical (MAPKs and jun/fos) and metabolic (AMPK, HIF-1alpha and PPARalpha) stimuli into enhanced gene transcription in skeletal muscle [28].

Analytical, diagnostic and therapeutic context of PRKAB1

  • In a recent report, Koo et al identify the transcriptional regulator TORC2 (Transducer of Regulated CREB activity 2) as a pivotal component of the gluconeogenic program.1 Both insulin and AMPK increase the phosphorylation of TORC2, while glucagon suppresses it [29].
  • Selenium activated AMPK in tumor xenografts as well as in colon cancer cell lines, and this activation seemed to be essential to the decrease in COX-2 expressions [30].
  • Sequence analysis of cDNA clones encoding these subunits reveals that they are related to yeast proteins that interact with SNF1, providing further evidence that the regulation and function of AMPK and SNF1 have been conserved throughout evolution [31].
  • Given that AMPK plays an important role in preventing cardiac ischemic/reperfusion damage, it is possible that in these diabetic hearts, the accelerated damage observed during exposure to ischemia/reperfusion could be a likely outcome of a compromised activation of AMPK [32].
  • When analyzed by immunoblotting with the antibody against Thr172-phosphorylated AMPK, the phosphorylation of AMPK was increased (2.5-fold) and decreased (0.4-fold) in cells expressing CA and DN LKB1, respectively, as compared with Lac-Z expressing control cells [33].


  1. Adiponectin and adiponectin receptors. Kadowaki, T., Yamauchi, T. Endocr. Rev. (2005) [Pubmed]
  2. Combination of 5-fluorouracil and genistein induces apoptosis synergistically in chemo-resistant cancer cells through the modulation of AMPK and COX-2 signaling pathways. Hwang, J.T., Ha, J., Park, O.J. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  3. AICAR, an activator of AMP-activated protein kinase, down-regulates the insulin receptor expression in HepG2 cells. Nakamaru, K., Matsumoto, K., Taguchi, T., Suefuji, M., Murata, Y., Igata, M., Kawashima, J., Kondo, T., Motoshima, H., Tsuruzoe, K., Miyamura, N., Toyonaga, T., Araki, E. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  4. Minireview: the AMP-activated protein kinase cascade: the key sensor of cellular energy status. Hardie, D.G. Endocrinology (2003) [Pubmed]
  5. AMPK integrates nutrient and hormonal signals to regulate food intake and energy balance through effects in the hypothalamus and peripheral tissues. Xue, B., Kahn, B.B. J. Physiol. (Lond.) (2006) [Pubmed]
  6. C75, a fatty acid synthase inhibitor, reduces food intake via hypothalamic AMP-activated protein kinase. Kim, E.K., Miller, I., Aja, S., Landree, L.E., Pinn, M., McFadden, J., Kuhajda, F.P., Moran, T.H., Ronnett, G.V. J. Biol. Chem. (2004) [Pubmed]
  7. Sequential changes in the signal transduction responses of skeletal muscle following food deprivation. de Lange, P., Farina, P., Moreno, M., Ragni, M., Lombardi, A., Silvestri, E., Burrone, L., Lanni, A., Goglia, F. FASEB J. (2006) [Pubmed]
  8. TSC2 Integrates Wnt and Energy Signals via a Coordinated Phosphorylation by AMPK and GSK3 to Regulate Cell Growth. Inoki, K., Ouyang, H., Zhu, T., Lindvall, C., Wang, Y., Zhang, X., Yang, Q., Bennett, C., Harada, Y., Stankunas, K., Wang, C.Y., He, X., Macdougald, O.A., You, M., Williams, B.O., Guan, K.L. Cell (2006) [Pubmed]
  9. Glucose metabolism and cancer. Shaw, R.J. Curr. Opin. Cell Biol. (2006) [Pubmed]
  10. Regulation of the energy sensor AMP-activated protein kinase by antigen receptor and Ca2+ in T lymphocytes. Tamás, P., Hawley, S.A., Clarke, R.G., Mustard, K.J., Green, K., Hardie, D.G., Cantrell, D.A. J. Exp. Med. (2006) [Pubmed]
  11. AMP-activated protein kinase--development of the energy sensor concept. Hardie, D.G., Hawley, S.A., Scott, J.W. J. Physiol. (Lond.) (2006) [Pubmed]
  12. Effects of adenosine on myocardial glucose and palmitate metabolism after transient ischemia: role of 5'-AMP-activated protein kinase. Jaswal, J.S., Gandhi, M., Finegan, B.A., Dyck, J.R., Clanachan, A.S. Am. J. Physiol. Heart Circ. Physiol. (2006) [Pubmed]
  13. AMP-activated protein kinase: role in metabolism and therapeutic implications. Schimmack, G., Defronzo, R.A., Musi, N. Diabetes, obesity & metabolism. (2006) [Pubmed]
  14. Inhibition of lipid synthesis through activation of AMP kinase: an additional mechanism for the hypolipidemic effects of berberine. Brusq, J.M., Ancellin, N., Grondin, P., Guillard, R., Martin, S., Saintillan, Y., Issandou, M. J. Lipid Res. (2006) [Pubmed]
  15. Long-term activation of adenosine monophosphate-activated protein kinase attenuates pressure-overload-induced cardiac hypertrophy. Li, H.L., Yin, R., Chen, D., Liu, D., Wang, D., Yang, Q., Dong, Y.G. J. Cell. Biochem. (2007) [Pubmed]
  16. Haplotype structures and large-scale association testing of the 5' AMP-activated protein kinase genes PRKAA2, PRKAB1, and PRKAB1 with type 2 diabetes. Sun, M.W., Lee, J.Y., de Bakker, P.I., Burtt, N.P., Almgren, P., Råstam, L., Tuomi, T., Gaudet, D., Daly, M.J., Hirschhorn, J.N., Altshuler, D., Groop, L., Florez, J.C. Diabetes (2006) [Pubmed]
  17. 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., Kemp, B.E. J. Biol. Chem. (1996) [Pubmed]
  18. Circulating adiponectin and expression of adiponectin receptors in human skeletal muscle: associations with metabolic parameters and insulin resistance and regulation by physical training. Blüher, M., Bullen, J.W., Lee, J.H., Kralisch, S., Fasshauer, M., Klöting, N., Niebauer, J., Schön, M.R., Williams, C.J., Mantzoros, C.S. J. Clin. Endocrinol. Metab. (2006) [Pubmed]
  19. Predominant {alpha}2/{beta}2/{gamma}3 AMPK activation during exercise in human skeletal muscle. Birk, J.B., Wojtaszewski, J.F. J. Physiol. (Lond.) (2006) [Pubmed]
  20. AMPK regulation of the growth of cultured human keratinocytes. Saha, A.K., Persons, K., Safer, J.D., Luo, Z., Holick, M.F., Ruderman, N.B. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  21. Obesity and the role of adipose tissue in inflammation and metabolism. Greenberg, A.S., Obin, M.S. Am. J. Clin. Nutr. (2006) [Pubmed]
  22. Functions of AMP-activated protein kinase in adipose tissue. Daval, M., Foufelle, F., Ferré, P. J. Physiol. (Lond.) (2006) [Pubmed]
  23. Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase. Gao, G., Fernandez, C.S., Stapleton, D., Auster, A.S., Widmer, J., Dyck, J.R., Kemp, B.E., Witters, L.A. J. Biol. Chem. (1996) [Pubmed]
  24. Different effects of adiponectin isoforms in human monocytic cells. Neumeier, M., Weigert, J., Schäffler, A., Wehrwein, G., Müller-Ladner, U., Schölmerich, J., Wrede, C., Buechler, C. J. Leukoc. Biol. (2006) [Pubmed]
  25. Glycogen debranching enzyme association with beta-subunit regulates AMP-activated protein kinase activity. Sakoda, H., Fujishiro, M., Fujio, J., Shojima, N., Ogihara, T., Kushiyama, A., Fukushima, Y., Anai, M., Ono, H., Kikuchi, M., Horike, N., Viana, A.Y., Uchijima, Y., Kurihara, H., Asano, T. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  26. Adenosine 5'-Monophosphate Kinase-Activated Protein Kinase (PRKA) Activators Delay Meiotic Resumption in Porcine Oocytes. Mayes, M.A., Laforest, M.F., Guillemette, C., Gilchrist, R.B., Richard, F.J. Biol. Reprod. (2007) [Pubmed]
  27. Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle. Thornton, C., Snowden, M.A., Carling, D. J. Biol. Chem. (1998) [Pubmed]
  28. Normal mammalian skeletal muscle and its phenotypic plasticity. Hoppeler, H., Flück, M. J. Exp. Biol. (2002) [Pubmed]
  29. More TORC for the gluconeogenic engine. Cheng, A., Saltiel, A.R. Bioessays (2006) [Pubmed]
  30. Selenium Regulates Cyclooxygenase-2 and Extracellular Signal-Regulated Kinase Signaling Pathways by Activating AMP-Activated Protein Kinase in Colon Cancer Cells. Hwang, J.T., Kim, Y.M., Surh, Y.J., Baik, H.W., Lee, S.K., Ha, J., Park, O.J. Cancer Res. (2006) [Pubmed]
  31. Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro. Woods, A., Cheung, P.C., Smith, F.C., Davison, M.D., Scott, J., Beri, R.K., Carling, D. J. Biol. Chem. (1996) [Pubmed]
  32. AMPK control of myocardial fatty acid metabolism fluctuates with the intensity of insulin-deficient diabetes. Kewalramani, G., An, D., Kim, M.S., Ghosh, S., Qi, D., Abrahani, A., Pulinilkunnil, T., Sharma, V., Wambolt, R.B., Allard, M.F., Innis, S.M., Rodrigues, B. J. Mol. Cell. Cardiol. (2007) [Pubmed]
  33. LKB1, an upstream AMPK kinase, regulates glucose and lipid metabolism in cultured liver and muscle cells. Imai, K., Inukai, K., Ikegami, Y., Awata, T., Katayama, S. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
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