Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2014, Article ID 504953, 10 pages
http://dx.doi.org/10.1155/2014/504953
Research Article

Insulin Regulates Glucose Consumption and Lactate Production through Reactive Oxygen Species and Pyruvate Kinase M2

1Department of Pathology, State Key Lab of Reproductive Medicine, Cancer Center, Nanjing Medical University, Nanjing 210029, China
2Department of Pathology, Anhui Medical University, Hefei 230032, China
3Department of Oncology, The First Affiliated Hospital of Nanjing Medical University, Nanjing 210029, China
4Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA

Received 12 February 2014; Accepted 11 April 2014; Published 8 May 2014

Academic Editor: Jinxiang Zhang

Copyright © 2014 Qi Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. D. R. Matthews, J. P. Hosker, A. S. Rudenski, B. A. Naylor, D. F. Treacher, and R. C. Turner, “Homeostasis model assessment: insulin resistance and β-cell function from fasting plasma glucose and insulin concentrations in man,” Diabetologia, vol. 28, no. 7, pp. 412–419, 1985. View at Google Scholar · View at Scopus
  2. H. Ying, A. C. Kimmelman, C. A. Lyssiotis et al., “Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism,” Cell, vol. 149, no. 3, pp. 656–670, 2012. View at Publisher · View at Google Scholar · View at Scopus
  3. O. Tavana and C. Zhu, “Too many breaks (brakes): pancreatic β-cell senescence leads to diabetes,” Cell Cycle, vol. 10, no. 15, pp. 2471–2484, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. T. Nowak and C. Suelter, “Pyruvate kinase: activation by and catalytic role of the monovalent and divalent cations,” Molecular and Cellular Biochemistry, vol. 35, no. 2, pp. 65–75, 1981. View at Publisher · View at Google Scholar · View at Scopus
  5. H. R. Christofk, M. G. V. Heiden, M. H. Harris et al., “The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth,” Nature, vol. 452, no. 7184, pp. 230–233, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. A. Daȩbrowska, J. Pietkiewicz, K. Daȩbrowska, E. Czapińska, and R. Danielewicz, “Interaction of M1 and M2 isozymes pyruvate kinase from human tissues with phospholipids,” Biochimica et Biophysica Acta, vol. 1383, no. 1, pp. 123–129, 1998. View at Publisher · View at Google Scholar · View at Scopus
  7. H.-S. Shi, D. Li, J. Zhang et al., “Silencing of PKM2 increases the efficacy of docetaxel in human lung cancer xenografts in mice,” Cancer Science, vol. 101, no. 6, pp. 1447–1453, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. Q. Sun, X. Chen, J. Ma et al., “Mammalian target of rapamycin up-regulation of pyruvate kinase isoenzyme type M2 is critical for aerobic glycolysis and tumor growth,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 10, pp. 4129–4134, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. W. Luo, H. Hu, R. Chang et al., “Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1,” Cell, vol. 145, no. 5, pp. 732–744, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. W. Yang, Y. Xia, H. Ji et al., “Nuclear PKM2 regulates β-catenin transactivation upon EGFR activation,” Nature, vol. 480, no. 7375, pp. 118–122, 2011. View at Publisher · View at Google Scholar · View at Scopus
  11. W. Dröge, “Free radicals in the physiological control of cell function,” Physiological Reviews, vol. 82, no. 1, pp. 47–95, 2002. View at Google Scholar · View at Scopus
  12. R. H. Burdon, “Superoxide and hydrogen peroxide in relation to mammalian cell proliferation,” Free Radical Biology and Medicine, vol. 18, no. 4, pp. 775–794, 1995. View at Publisher · View at Google Scholar · View at Scopus
  13. T. P. Szatrowski and C. F. Nathan, “Production of large amounts of hydrogen peroxide by human tumor cells,” Cancer Research, vol. 51, no. 3, pp. 794–798, 1991. View at Google Scholar · View at Scopus
  14. Q. Zhou, L.-Z. Liu, B. Fu et al., “Reactive oxygen species regulate insulin-induced VEGF and HIF-1α expression through the activation of p70S6K1 in human prostate cancer cells,” Carcinogenesis, vol. 28, no. 1, pp. 28–37, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. P. Kantharidis, B. Wang, R. M. Carew, and H. Y. Lan, “Diabetes complications: the microRNA perspective,” Diabetes, vol. 60, no. 7, pp. 1832–1837, 2011. View at Publisher · View at Google Scholar · View at Scopus
  16. P. P. Medina and F. J. Slack, “MicroRNAs and cancer: an overview,” Cell Cycle, vol. 7, no. 16, pp. 2485–2492, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Srikantan, M. Gorospe, and K. Abdelmohsen, “Senescence-associated microRNAs linked to tumorigenesis,” Cell Cycle, vol. 10, no. 19, pp. 3211–3212, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. R. Garzon, G. Marcucci, and C. M. Croce, “Targeting microRNAs in cancer: rationale, strategies and challenges,” Nature Reviews Drug Discovery, vol. 9, no. 10, pp. 775–789, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. R. J. A. Frost and E. N. Olson, “Control of glucose homeostasis and insulin sensitivity by the Let-7 family of microRNAs,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 52, pp. 21075–21080, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. S. D. Jordan, M. Krüger, D. M. Willmes et al., “Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism,” Nature Cell Biology, vol. 13, no. 4, pp. 434–448, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Jajoo, D. Mukherjea, T. Kaur et al., “Essential role of NADPH oxidase-dependent reactive oxygen species generation in regulating microRNA-21 expression and function in prostate cancer,” Antioxidants & Redox Signaling, vol. 19, no. 16, pp. 1863–1876, 2013. View at Publisher · View at Google Scholar
  22. R. Huxley, A. Ansary-Moghaddam, A. B. de González, F. Barzi, and M. Woodward, “Type-II diabetes and pancreatic cancer: a meta-analysis of 36 studies,” British Journal of Cancer, vol. 92, no. 11, pp. 2076–2083, 2005. View at Publisher · View at Google Scholar · View at Scopus
  23. H. B. el-Serag, H. Hampel, and F. Javadi, “The association between diabetes and hepatocellular carcinoma: a systematic review of epidemiologic evidence,” Clinical Gastroenterology and Hepatology, vol. 4, no. 3, pp. 369–380, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. V. Rottiers and A. M. Naar, “MicroRNAs in metabolism and metabolic disorders,” Nature Reviews Molecular Cell Biology, vol. 13, no. 4, pp. 239–250, 2012. View at Publisher · View at Google Scholar
  25. Q. Xu, L.-Z. Liu, X. Qian et al., “MiR-145 directly targets p70S6K1 in cancer cells to inhibit tumor growth and angiogenesis,” Nucleic Acids Research, vol. 40, no. 2, pp. 761–774, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. Z.-M. Shi, J. Wang, Z. Yan et al., “MiR-128 inhibits tumor growth and angiogenesis by targeting p70S6K1,” PLoS ONE, vol. 7, no. 3, Article ID e32709, 2012. View at Publisher · View at Google Scholar · View at Scopus
  27. A. R. Saltiel and C. R. Kahn, “Insulin signalling and the regulation of glucose and lipid metabolism,” Nature, vol. 414, no. 6865, pp. 799–806, 2001. View at Publisher · View at Google Scholar · View at Scopus
  28. T. Hitosugi, S. Kang, M. G. V. Heiden et al., “Tyrosine phosphorylation inhibits PKM2 to promote the warburg effect and tumor growth,” Science Signaling, vol. 2, no. 97, Article ID ra73, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. K. Yamada and T. Noguchi, “Regulation of pyruvate kinase M gene expression,” Biochemical and Biophysical Research Communications, vol. 256, no. 2, pp. 257–262, 1999. View at Publisher · View at Google Scholar · View at Scopus
  30. R. Fukuda, H. Zhang, J.-W. Kim, L. Shimoda, C. V. Dang, and G. Semenza, “HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells,” Cell, vol. 129, no. 1, pp. 111–122, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. K.-W. Tsai, H.-W. Kao, H.-C. Chen, S.-J. Chen, and W.-C. Lin, “Epigenetic control of the expression of a primate-specific microRNA cluster in human cancer cells,” Epigenetics, vol. 4, no. 8, pp. 587–592, 2009. View at Publisher · View at Google Scholar · View at Scopus
  32. H. M. O'Hagan, H. P. Mohammad, and S. B. Baylin, “Double strand breaks can initiate gene silencing and SIRT1-dependent onset of DNA methylation in an exogenous promoter CpG island,” PLoS Genetics, vol. 4, no. 8, Article ID e1000155, 2008. View at Publisher · View at Google Scholar · View at Scopus
  33. H. O'Hagan, W. Wang, S. Sen et al., “Oxidative damage targets complexes containing DNA methyltransferases, SIRT1, and polycomb members to promoter CpG islands,” Cancer Cell, vol. 20, no. 5, pp. 606–619, 2011. View at Publisher · View at Google Scholar · View at Scopus