Table of Contents Author Guidelines Submit a Manuscript
International Journal of Cell Biology
Volume 2013, Article ID 639401, 16 pages
http://dx.doi.org/10.1155/2013/639401
Review Article

Natural Compounds as Regulators of the Cancer Cell Metabolism

1Laboratoire de Biologie Moléculaire et Cellulaire du Cancer, Hôpital Kirchberg 9, Rue Edward Steichen, 2540 Luxembourg, Luxembourg
2Department of Pharmacy, College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea

Received 20 December 2012; Accepted 22 April 2013

Academic Editor: Young-Joon Surh

Copyright © 2013 Claudia Cerella 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. M. Schumacher, M. Kelkel, M. Dicato, and M. Diederich, “Gold from the sea: marine compounds as inhibitors of the hallmarks of cancer,” Biotechnology Advances, vol. 29, no. 5, pp. 531–547, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. B. Orlikova and M. Diederich, “Power from the garden: plant compounds as inhibitors of the hallmarks of cancer,” Current Medicinal Chemistry, vol. 19, no. 14, pp. 2061–2087, 2012. View at Google Scholar
  3. D. Hanahan and R. A. Weinberg, “Hallmarks of cancer: the next generation,” Cell, vol. 144, no. 5, pp. 646–674, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. F. Chiaradonna, R. M. Moresco, C. Airoldi et al., “From cancer metabolism to new biomarkers and drug targets,” Biotechnology Advances, vol. 30, no. 1, pp. 30–51, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. S. Mazurek, “Pyruvate kinase type M2: a key regulator of the metabolic budget system in tumor cells,” International Journal of Biochemistry and Cell Biology, vol. 43, no. 7, pp. 969–980, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. V. R. Fantin, J. St-Pierre, and P. Leder, “Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance,” Cancer Cell, vol. 9, no. 6, pp. 425–434, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. G. L. Semenza, “Regulation of metabolism by hypoxia-inducible factor 1,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 76, pp. 347–353, 2011. View at Google Scholar
  8. H. R. Christofk, M. G. Vander 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
  9. R. Diaz-Ruiz, M. Rigoulet, and A. Devin, “The Warburg and Crabtree effects: on the origin of cancer cell energy metabolism and of yeast glucose repression,” Biochimica et Biophysica Acta, vol. 1807, no. 6, pp. 568–576, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. L. Zheng, R. G. Roeder, and Y. Luo, “S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component,” Cell, vol. 114, no. 2, pp. 255–266, 2003. View at Publisher · View at Google Scholar · View at Scopus
  11. T. Mitani, R. Yamaji, Y. Higashimura, N. Harada, Y. Nakano, and H. Inui, “Hypoxia enhances transcriptional activity of androgen receptor through hypoxia-inducible factor-1α in a low androgen environment,” Journal of Steroid Biochemistry and Molecular Biology, vol. 123, no. 1-2, pp. 58–64, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. C. Tristan, N. Shahani, T. W. Sedlak, and A. Sawa, “The diverse functions of GAPDH: views from different subcellular compartments,” Cellular Signalling, vol. 23, no. 2, pp. 317–323, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. X. Gao, H. Wang, J. J. Yang, X. Liu, and Z. R. Liu, “Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase,” Molecular Cell, vol. 45, no. 5, pp. 598–609, 2012. View at Google Scholar
  14. M. Tamada, M. Suematsu, and H. Saya, “Pyruvate kinase m2: multiple faces for conferring benefits on cancer cells,” Clinical Cancer Research, vol. 18, no. 20, pp. 5554–5561, 2012. View at Google Scholar
  15. W. Yang, Y. Xia, H. Ji et al., “Nuclear PKM2 regulates beta-catenin transactivation upon EGFR activation,” Nature, vol. 480, no. 7375, pp. 118–122, 2011. View at Google Scholar
  16. B. L. Ebert and H. F. Bunn, “Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein,” Molecular and Cellular Biology, vol. 18, no. 7, pp. 4089–4096, 1998. View at Google Scholar · View at Scopus
  17. M. G. Vander Heiden, J. W. Locasale, K. D. Swanson et al., “Evidence for an alternative glycolytic pathway in rapidly proliferating cells,” Science, vol. 329, no. 5998, pp. 1492–1499, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Fischer, P. Hoffmann, S. Voelkl et al., “Inhibitory effect of tumor cell-derived lactic acid on human T cells,” Blood, vol. 109, no. 9, pp. 3812–3819, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. P. Swietach, R. D. Vaughan-Jones, and A. L. Harris, “Regulation of tumor pH and the role of carbonic anhydrase 9,” Cancer and Metastasis Reviews, vol. 26, no. 2, pp. 299–310, 2007. View at Publisher · View at Google Scholar · View at Scopus
  20. F. Baumann, P. Leukel, A. Doerfelt et al., “Lactate promotes glioma migration by TGF-β2-dependent regulation of matrix metalloproteinase-2,” Neuro-Oncology, vol. 11, no. 4, pp. 368–380, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. K. A. Brand and U. Hermfisse, “Aerobic glycolysis by proliferating cells: a protective strategy against reactive oxygen species,” The FASEB Journal, vol. 11, no. 5, pp. 388–395, 1997. View at Google Scholar · View at Scopus
  22. K. Brand, “Aerobic glycolysis by proliferating cells: protection against oxidative stress at the expense of energy yield,” Journal of Bioenergetics and Biomembranes, vol. 29, no. 4, pp. 355–364, 1997. View at Publisher · View at Google Scholar · View at Scopus
  23. H. Shim, C. Dolde, B. C. Lewis et al., “c-Myc transactivation of LDH-A: implications for tumor metabolism and growth,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 13, pp. 6658–6663, 1997. View at Publisher · View at Google Scholar · View at Scopus
  24. C. V. Dang and G. L. Semenza, “Oncogenic alterations of metabolism,” Trends in Biochemical Sciences, vol. 24, no. 2, pp. 68–72, 1999. View at Publisher · View at Google Scholar · View at Scopus
  25. J. Y. Park, W. Zheng, D. Kim et al., “Candidate tumor suppressor gene SLC5A8 is frequently down-regulated by promoter hypermethylation in prostate tumor,” Cancer Detection and Prevention, vol. 31, no. 5, pp. 359–365, 2007. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Helm, D. Coppola, V. Ganapathy et al., “SLC5A8 nuclear translocation and loss of expression are associated with poor outcome in pancreatic ductal adenocarcinoma,” Pancreas, vol. 41, no. 6, pp. 904–909, 2012. View at Google Scholar
  27. M. Thangaraju, E. Gopal, P. M. Martin et al., “SLC5A8 triggers tumor cell apoptosis through pyruvate-dependent inhibition of histone deacetylases,” Cancer Research, vol. 66, no. 24, pp. 11560–11564, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Thangaraju, K. N. Carswell, P. D. Prasad, and V. Ganapathy, “Colon cancer cells maintain low levels of pyruvate to avoid cell death caused by inhibition of HDAC1/HDAC3,” Biochemical Journal, vol. 417, no. 1, pp. 379–389, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. V. Paroder, S. R. Spencer, M. Paroder et al., “Na+/monocarboxylate transport (SMCT) protein expression correlates with survival in colon cancer: molecular characterization of SMCT,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 19, pp. 7270–7275, 2006. View at Publisher · View at Google Scholar · View at Scopus
  30. R. J. DeBerardinis, A. Mancuso, E. Daikhin et al., “Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 49, pp. 19345–19350, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. Y. Mitsuishi, K. Taguchi, Y. Kawatani et al., “Nrf2 redirects glucose and glutamine into anabolic pathways in metabolic reprogramming,” Cancer Cell, vol. 22, no. 1, pp. 66–79, 2012. View at Google Scholar
  32. D. Chalbos, M. Chambon, G. Ailhaud, and H. Rochefort, “Fatty acid synthetase and its mRNA are induced by progestins in breast cancer cells,” The Journal of Biological Chemistry, vol. 262, no. 21, pp. 9923–9926, 1987. View at Google Scholar · View at Scopus
  33. J. V. Swinnen, M. Esquenet, K. Goossens, W. Heyns, and G. Verhoeven, “Androgens stimulate fatty acid synthase in the human prostate cancer cell line LNCaP,” Cancer Research, vol. 57, no. 6, pp. 1086–1090, 1997. View at Google Scholar · View at Scopus
  34. T. S. Ho, Y. P. Ho, W. Y. Wong, L. Chi-Ming Chiu, Y. S. Wong, and V. Eng-Choon Ooi, “Fatty acid synthase inhibitors cerulenin and C75 retard growth and induce caspase-dependent apoptosis in human melanoma A-375 cells,” Biomedicine & Pharmacotherapy, vol. 61, no. 9, pp. 578–587, 2007. View at Publisher · View at Google Scholar · View at Scopus
  35. Z. L. Liu, G. Wang, A. F. Peng et al., “Fatty acid synthase expression in osteosarcoma and its correlation with pulmonary metastasis,” Oncology Letters, vol. 4, no. 5, pp. 878–882, 2012. View at Google Scholar
  36. J. N. Li, M. A. Mahmoud, W. F. Han, M. Ripple, and E. S. Pizer, “Sterol regulatory element-binding protein-1 participates in the regulation of fatty acid synthase expression in colorectal neoplasia,” Experimental Cell Research, vol. 261, no. 1, pp. 159–165, 2000. View at Publisher · View at Google Scholar · View at Scopus
  37. Y. Zhan, N. Ginanni, M. R. Tota et al., “Control of cell growth and survival by enzymes of the fatty acid synthesis pathway in HCT-116 colon cancer cells,” Clinical Cancer Research, vol. 14, no. 18, pp. 5735–5742, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. H. Orita, J. Coulter, E. Tully, F. P. Kuhajda, and E. Gabrielson, “Inhibiting fatty acid synthase for chemoprevention of chemically induced lung tumors,” Clinical Cancer Research, vol. 14, no. 8, pp. 2458–2464, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. E. S. Pizer, F. D. Wood, G. R. Pasternack, and F. P. Kuhajda, “Fatty acid synthase (FAS): a target for cytotoxic antimetabolites in HL60 promyelocytic leukemia cells,” Cancer Research, vol. 56, no. 4, pp. 745–751, 1996. View at Google Scholar · View at Scopus
  40. A. P. Bhatt, S. R. Jacobs, A. J. Freemerman et al., “Dysregulation of fatty acid synthesis and glycolysis in non-Hodgkin lymphoma,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 29, pp. 11818–11823.
  41. Y. A. Yang, W. F. Han, P. J. Morin, F. J. Chrest, and E. S. Pizer, “Activation of fatty acid synthesis during neoplastic transformation: role of mitogen-activated protein kinase and phosphatidylinositol 3-kinase,” Experimental Cell Research, vol. 279, no. 1, pp. 80–90, 2002. View at Publisher · View at Google Scholar · View at Scopus
  42. N. Li, X. Bu, X. Tian et al., “Fatty acid synthase regulates proliferation and migration of colorectal cancer cells via HER2-PI3K/Akt signaling pathway,” Nutrition and Cancer, vol. 64, no. 6, pp. 864–870, 2012. View at Google Scholar
  43. Z. Luo, M. Zang, and W. Guo, “AMPK as a metabolic tumor suppressor: control of metabolism and cell growth,” Future Oncology, vol. 6, no. 3, pp. 457–470, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. W. Shao and P. J. Espenshade, “Expanding roles for SREBP in metabolism,” Cell Metabolism, vol. 16, no. 4, pp. 414–419, 2012. View at Google Scholar
  45. J. R. Cantor and D. M. Sabatini, “Cancer cell metabolism: one hallmark, many faces,” Cancer Discovery, vol. 2, no. 10, pp. 881–898, 2012. View at Google Scholar
  46. R. J. DeBerardinis, N. Sayed, D. Ditsworth, and C. B. Thompson, “Brick by brick: metabolism and tumor cell growth,” Current Opinion in Genetics and Development, vol. 18, no. 1, pp. 54–61, 2008. View at Publisher · View at Google Scholar · View at Scopus
  47. S. Bandyopadhyay, S. K. Pai, M. Watabe et al., “FAS expression inversely correlates with PTEN level in prostate cancer and a PI 3-kinase inhibitor synergizes with FAS siRNA to induce apoptosis,” Oncogene, vol. 24, no. 34, pp. 5389–5395, 2005. View at Publisher · View at Google Scholar · View at Scopus
  48. K. Walter, S. M. Hong, S. Nyhan et al., “Serum fatty acid synthase as a marker of pancreatic neoplasia,” Cancer Epidemiology Biomarkers and Prevention, vol. 18, no. 9, pp. 2380–2385, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. F. P. Kuhajda, “Fatty acid synthase and cancer: new application of an old pathway,” Cancer Research, vol. 66, no. 12, pp. 5977–5980, 2006. View at Publisher · View at Google Scholar · View at Scopus
  50. S. Lu and M. C. Archer, “Fatty acid synthase is a potential molecular target for the chemoprevention of breast cancer,” Carcinogenesis, vol. 26, no. 1, pp. 153–157, 2005. View at Publisher · View at Google Scholar · View at Scopus
  51. S. Bandyopadhyay, R. Zhan, Y. Wang et al., “Mechanism of apoptosis induced by the inhibition of fatty acid synthase in breast cancer cells,” Cancer Research, vol. 66, no. 11, pp. 5934–5940, 2006. View at Publisher · View at Google Scholar · View at Scopus
  52. J. L. Little, F. B. Wheeler, D. R. Fels, C. Koumenis, and S. J. Kridel, “Inhibition of fatty acid synthase induces endoplasmic reticulum stress in tumor cells,” Cancer Research, vol. 67, no. 3, pp. 1262–1269, 2007. View at Publisher · View at Google Scholar · View at Scopus
  53. I. Samudio, R. Harmancey, M. Fiegl et al., “Pharmacologic inhibition of fatty acid oxidation sensitizes human leukemia cells to apoptosis induction,” Journal of Clinical Investigation, vol. 120, no. 1, pp. 142–156, 2010. View at Publisher · View at Google Scholar · View at Scopus
  54. T. M. Loftus, D. E. Jaworsky, C. L. Frehywot et al., “Reduced food intake and body weight in mice treated with fatty acid synthase inhibitors,” Science, vol. 288, no. 5475, pp. 2379–2381, 2000. View at Publisher · View at Google Scholar · View at Scopus
  55. J. A. Menendez, L. Vellon, and R. Lupu, “Targeting fatty acid synthase-driven lipid rafts: a novel strategy to overcome trastuzumab resistance in breast cancer cells,” Medical Hypotheses, vol. 64, no. 5, pp. 997–1001, 2005. View at Publisher · View at Google Scholar · View at Scopus
  56. C. J. Piyathilake, A. R. Frost, U. Manne et al., “The expression of fatty acid synthase (FASE) is an early event in the development and progression of squamous cell carcinoma of the lung,” Human Pathology, vol. 31, no. 9, pp. 1068–1073, 2000. View at Publisher · View at Google Scholar · View at Scopus
  57. J. V. Swinnen, T. Roskams, S. Joniau et al., “Overexpression of fatty acid synthase is an early and common event in the development of prostate cancer,” International Journal of Cancer, vol. 98, no. 1, pp. 19–22, 2002. View at Publisher · View at Google Scholar · View at Scopus
  58. A. Baron, T. Migita, D. Tang, and M. Loda, “Fatty acid synthase: a metabolic oncogene in prostate cancer?” Journal of Cellular Biochemistry, vol. 91, no. 1, pp. 47–53, 2004. View at Publisher · View at Google Scholar · View at Scopus
  59. J. A. Menendez, J. P. Decker, and R. Lupu, “In support of Fatty Acid Synthase (FAS) as a metabolic oncogene: extracellular acidosis acts in an epigenetic fashion activating FAS gene expression in cancer cells,” Journal of Cellular Biochemistry, vol. 94, no. 1, pp. 1–4, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. T. Migita, S. Ruiz, A. Fornari et al., “Fatty acid synthase: a metabolic enzyme and candidate oncogene in prostate cancer,” Journal of the National Cancer Institute, vol. 101, no. 7, pp. 519–532, 2009. View at Publisher · View at Google Scholar · View at Scopus
  61. G. B. Mills and W. H. Moolenaar, “The emerging role of lysophosphatidic acid in cancer,” Nature Reviews Cancer, vol. 3, no. 8, pp. 582–591, 2003. View at Publisher · View at Google Scholar · View at Scopus
  62. C. Sobolewski, C. Cerella, M. Dicato, L. Ghibelli, and M. Diederich, “The role of cyclooxygenase-2 in cell proliferation and cell death in human malignancies,” International Journal of Cell Biology, vol. 2010, Article ID 215158, 21 pages, 2010. View at Publisher · View at Google Scholar · View at Scopus
  63. C. Cerella, C. Sobolewski, M. Dicato, and M. Diederich, “Targeting COX-2 expression by natural compounds: a promising alternative strategy to synthetic COX-2 inhibitors for cancer chemoprevention and therapy,” Biochemical Pharmacology, vol. 80, no. 12, pp. 1801–1815, 2010. View at Publisher · View at Google Scholar · View at Scopus
  64. D. K. Nomura, J. Z. Long, S. Niessen, H. S. Hoover, S. W. Ng, and B. F. Cravatt, “Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis,” Cell, vol. 140, no. 1, pp. 49–61, 2010. View at Publisher · View at Google Scholar · View at Scopus
  65. A. Vila, A. Rosengarth, D. Piomelli, B. Cravatt, and L. J. Marnett, “Hydrolysis of prostaglandin glycerol esters by the endocannabinoid-hydrolyzing enzymes, monoacylglycerol lipase and fatty acid amide hydrolase,” Biochemistry, vol. 46, no. 33, pp. 9578–9585, 2007. View at Publisher · View at Google Scholar · View at Scopus
  66. P. Carmeliet and R. K. Jain, “Angiogenesis in cancer and other diseases,” Nature, vol. 407, no. 6801, pp. 249–257, 2000. View at Publisher · View at Google Scholar · View at Scopus
  67. J. D. Rabinowitz and E. White, “Autophagy and metabolism,” Science, vol. 330, no. 6009, pp. 1344–1348, 2010. View at Publisher · View at Google Scholar · View at Scopus
  68. L. T. Jia, S. Y. Chen, and A. G. Yang, “Cancer gene therapy targeting cellular apoptosis machinery,” Cancer Treatment Reviews, vol. 38, no. 7, pp. 868–876, 2012. View at Google Scholar
  69. G. Sutendra, P. Dromparis, A. Kinnaird et al., “Mitochondrial activation by inhibition of PDKII suppresses HIF1a signaling and angiogenesis in cancer,” Oncogene, vol. 32, no. 13, pp. 1638–1650, 2012. View at Publisher · View at Google Scholar
  70. D. C. Wallace, “Mitochondria and cancer,” Nature Reviews Cancer, vol. 12, no. 10, pp. 685–698, 2012. View at Google Scholar
  71. T. N. Milovanova, V. M. Bhopale, E. M. Sorokina et al., “Lactate stimulates vasculogenic stem cells via the thioredoxin system and engages an autocrine activation loop involving hypoxia-inducible factor 1,” Molecular and Cellular Biology, vol. 28, no. 20, pp. 6248–6261, 2008. View at Publisher · View at Google Scholar · View at Scopus
  72. R. T. Marquez and L. Xu, “Bcl-2:Beclin 1 complex: multiple, mechanisms regulating autophagy/apoptosis toggle switch,” American Journal of Cancer Research, vol. 2, no. 2, pp. 214–221, 2012. View at Google Scholar
  73. A. J. Levine and A. M. Puzio-Kuter, “The control of the metabolic switch in cancers by oncogenes and tumor suppressor genes,” Science, vol. 330, no. 6009, pp. 1340–1344, 2010. View at Publisher · View at Google Scholar · View at Scopus
  74. D. C. Wallace, “Mitochondria and cancer: Warburg addressed,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 70, pp. 363–374, 2005. View at Publisher · View at Google Scholar · View at Scopus
  75. N. C. Denko, “Hypoxia, HIF1 and glucose metabolism in the solid tumour,” Nature Reviews Cancer, vol. 8, no. 9, pp. 705–713, 2008. View at Publisher · View at Google Scholar · View at Scopus
  76. G. L. Semenza, “Hypoxia-inducible factors in physiology and medicine,” Cell, vol. 148, no. 3, pp. 399–408, 2012. View at Google Scholar
  77. G. L. Wang, B. H. Jiang, and G. L. Semenza, “Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1,” Biochemical and Biophysical Research Communications, vol. 212, no. 2, pp. 550–556, 1995. View at Publisher · View at Google Scholar · View at Scopus
  78. L. E. Huang, Z. Arany, D. M. Livingston, and H. Franklin Bunn, “Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its α subunit,” The Journal of Biological Chemistry, vol. 271, no. 50, pp. 32253–32259, 1996. View at Publisher · View at Google Scholar · View at Scopus
  79. S. Salceda and J. Caro, “Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes,” The Journal of Biological Chemistry, vol. 272, no. 36, pp. 22642–22647, 1997. View at Publisher · View at Google Scholar · View at Scopus
  80. S. Krishna, I. C. C. Low, and S. Pervaiz, “Regulation of mitochondrial metabolism: yet another facet in the biology of the oncoprotein Bcl-2,” Biochemical Journal, vol. 435, no. 3, pp. 545–551, 2011. View at Publisher · View at Google Scholar · View at Scopus
  81. S. Cristofanon, S. Nuccitelli, M. D'Alessio, M. Dicato, M. Diederich, and L. Ghibelli, “Oxidation-dependent maturation and survival of explanted blood monocytes via Bcl-2 up-regulation,” Biochemical Pharmacology, vol. 76, no. 11, pp. 1533–1543, 2008. View at Publisher · View at Google Scholar · View at Scopus
  82. B. R. You and W. H. Park, “Trichostatin A induces apoptotic cell death of HeLa cells in a Bcl-2 and oxidative stress-dependent manner,” International Journal of Oncology, vol. 42, no. 1, pp. 359–366, 2013. View at Google Scholar
  83. B. J. Altman and J. C. Rathmell, “Autophagy: not good or bad, but good and bad,” Autophagy, vol. 5, no. 4, pp. 569–570, 2009. View at Publisher · View at Google Scholar · View at Scopus
  84. J. Y. Guo, H. Y. Chen, R. Mathew et al., “Activated Ras requires autophagy to maintain oxidative metabolism and tumorigenesis,” Genes and Development, vol. 25, no. 5, pp. 460–470, 2011. View at Publisher · View at Google Scholar · View at Scopus
  85. J. Lee, S. Giordano, and J. Zhang, “Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling,” The Biochemical Journal, vol. 441, no. 2, pp. 523–540, 2012. View at Google Scholar
  86. L. Liu, D. Feng, G. Chen et al., “Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells,” Nature Cell Biology, vol. 14, no. 2, pp. 177–185, 2012. View at Google Scholar
  87. A. Y. Andreyev, Y. E. Kushnareva, and A. A. Starkov, “Mitochondrial metabolism of reactive oxygen species,” Biochemistry, vol. 70, no. 2, pp. 200–214, 2005. View at Publisher · View at Google Scholar · View at Scopus
  88. A. Apel, I. Herr, H. Schwarz, H. P. Rodemann, and A. Mayer, “Blocked autophagy sensitizes resistant carcinoma cells to radiation therapy,” Cancer Research, vol. 68, no. 5, pp. 1485–1494, 2008. View at Publisher · View at Google Scholar · View at Scopus
  89. Y. Yu, S. M. Fan, J. K. Song et al., “Hydroxyl radical (·OH) played a pivotal Role in oridonin-induced apoptosis and autophagy in human epidermoid carcinoma A431 cells,” Biological & Pharmaceutical Bulletin, vol. 35, no. 12, pp. 2148–2159, 2012. View at Google Scholar
  90. V. Ganapathy, M. Thangaraju, and P. D. Prasad, “Nutrient transporters in cancer: relevance to Warburg hypothesis and beyond,” Pharmacology and Therapeutics, vol. 121, no. 1, pp. 29–40, 2009. View at Publisher · View at Google Scholar · View at Scopus
  91. M. P. Torres, S. Rachagani, V. Purohit et al., “Graviola: a novel promising natural-derived drug that inhibits tumorigenicity and metastasis of pancreatic cancer cells in vitro and in vivo through altering cell metabolism,” Cancer Letters, vol. 323, no. 1, pp. 29–40, 2012. View at Google Scholar
  92. M. Kitagawa, S. Ikeda, E. Tashiro, T. Soga, and M. Imoto, “Metabolomic identification of the target of the filopodia protrusion inhibitor glucopiericidin A,” Chemistry & Biology, vol. 17, no. 9, pp. 989–998, 2010. View at Publisher · View at Google Scholar · View at Scopus
  93. J. B. Park, “Flavonoids are potential inhibitors of glucose uptake in U937 cells,” Biochemical and Biophysical Research Communications, vol. 260, no. 2, pp. 568–574, 1999. View at Publisher · View at Google Scholar · View at Scopus
  94. P. Strobel, C. Allard, T. Perez-Acle, R. Calderon, R. Aldunate, and F. Leighton, “Myricetin, quercetin and catechin-gallate inhibit glucose uptake in isolated rat adipocytes,” Biochemical Journal, vol. 386, no. 3, pp. 471–478, 2005. View at Publisher · View at Google Scholar · View at Scopus
  95. A. Perez, P. Ojeda, L. Ojeda et al., “Hexose transporter GLUT1 harbors several distinct regulatory binding sites for flavones and tyrphostins,” Biochemistry, vol. 50, no. 41, pp. 8834–8845, 2011. View at Google Scholar
  96. A. Wolf, S. Agnihotri, J. Micallef et al., “Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme,” The Journal of Experimental Medicine, vol. 208, no. 2, pp. 313–326, 2011. View at Publisher · View at Google Scholar · View at Scopus
  97. N. Shulga, R. Wilson-Smith, and J. G. Pastorino, “Hexokinase II detachment from the mitochondria potentiates cisplatin induced cytotoxicity through a caspase-2 dependent mechanism,” Cell Cycle, vol. 8, no. 20, pp. 3355–3364, 2009. View at Google Scholar · View at Scopus
  98. S. Cohen and E. Flescher, “Methyl jasmonate: a plant stress hormone as an anti-cancer drug,” Phytochemistry, vol. 70, no. 13-14, pp. 1600–1609, 2009. View at Publisher · View at Google Scholar · View at Scopus
  99. C. Xing, J. R. LaPorte, J. K. Barbay, and A. G. Myers, “Identification of GAPDH as a protein target of the saframycin antiproliferative agents,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 16, pp. 5862–5866, 2004. View at Publisher · View at Google Scholar · View at Scopus
  100. M. G. Vander Heiden, H. R. Christofk, E. Schuman et al., “Identification of small molecule inhibitors of pyruvate kinase M2,” Biochemical Pharmacology, vol. 79, no. 8, pp. 1118–1124, 2010. View at Publisher · View at Google Scholar · View at Scopus
  101. J. Chen, J. Xie, Z. Jiang et al., “Shikonin and its analogs inhibit cancer cell glycolysis by targeting tumor pyruvate kinase-M2,” Oncogene, vol. 30, no. 42, pp. 4297–4306, 2011. View at Google Scholar
  102. W. Han, L. Li, S. Qiu et al., “Shikonin circumvents cancer drug resistance by induction of a necroptotic death,” Molecular Cancer Therapeutics, vol. 6, no. 5, pp. 1641–1649, 2007. View at Publisher · View at Google Scholar · View at Scopus
  103. D. Anastasiou, Y. Yu, W. J. Israelsen et al., “Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis,” Nature Chemical Biology, vol. 8, no. 12, p. 1008, 2012. View at Google Scholar
  104. T. W. Hodges, C. F. Hossain, Y. P. Kim, Y. D. Zhou, and D. G. Nagle, “Molecular-targeted antitumor agents: the Saururus cernuus dineolignans manassantin B and 4-O-demethylmanassantin B are potent inhibitors of hypoxia-activated HIF-1,” Journal of Natural Products, vol. 67, no. 5, pp. 767–771, 2004. View at Publisher · View at Google Scholar · View at Scopus
  105. Y. Liu, C. K. Venna, J. B. Morgan et al., “Methylalpinumisoflavone inhibits hypoxia-inducible factor-1 (HIF-1) activation by simultaneously targeting multiple pathways,” The Journal of Biological Chemistry, vol. 284, no. 9, pp. 5859–5868, 2009. View at Publisher · View at Google Scholar · View at Scopus
  106. H. Hattori, K. Okuda, T. Murase et al., “Isolation, identification, and biological evaluation of HIF-1-modulating compounds from Brazilian green propolis,” Bioorganic & Medicinal Chemistry, vol. 19, no. 18, pp. 5392–5401, 2011. View at Google Scholar
  107. M. H. Teiten, S. Eifes, M. Dicato, and M. Diederich, “Curcumin-the paradigm of a multi-target natural compound with applications in cancer prevention and treatment,” Toxins, vol. 2, no. 1, pp. 128–162, 2010. View at Publisher · View at Google Scholar · View at Scopus
  108. L. D. Guo, X. J. Chen, Y. H. Hu et al., “Curcumin inhibits proliferation and induces apoptosis of human colorectal cancer cells by activating the mitochondria apoptotic pathway,” Phytotherapy Research, vol. 27, no. 3, pp. 422–430, 2012. View at Publisher · View at Google Scholar
  109. A. Kunwar, S. Jayakumar, A. K. Srivastava, and K. I. Priyadarsini, “Dimethoxycurcumin-induced cell death in human breast carcinoma MCF7 cells: evidence for pro-oxidant activity, mitochondrial dysfunction, and apoptosis,” Archives of Toxicology, vol. 86, no. 4, pp. 603–614, 2012. View at Google Scholar
  110. Q. Y. Chen, J. G. Shi, Q. H. Yao et al., “Lysosomal membrane permeabilization is involved in curcumin-induced apoptosis of A549 lung carcinoma cells,” Molecular and Cellular Biochemistry, vol. 359, no. 1-2, pp. 389–398, 2012. View at Google Scholar
  111. C. L. Kuo, S. Y. Wu, S. W. Ip et al., “Apoptotic death in curcumin-treated NPC-TW 076 human nasopharyngeal carcinoma cells is mediated through the ROS, mitochondrial depolarization and caspase-3-dependent signaling responses,” International Journal of Oncology, vol. 39, no. 2, pp. 319–328, 2011. View at Publisher · View at Google Scholar · View at Scopus
  112. C. L. Yang, Y. G. Ma, Y. X. Xue et al., “Curcumin induces small cell lung cancer NCI-H446 cell apoptosis via the reactive oxygen species-mediated mitochondrial pathway and not the cell death receptor pathway,” DNA and Cell Biology, vol. 31, no. 2, pp. 139–150, 2012. View at Google Scholar
  113. K. H. Jung and J. W. Park, “Suppression of mitochondrial NADP+-dependent isocitrate dehydrogenase activity enhances curcumin-induced apoptosis in HCT116 cells,” Free Radical Research, vol. 45, no. 4, pp. 431–438, 2011. View at Publisher · View at Google Scholar · View at Scopus
  114. A. McLachlan, N. Kekre, J. McNulty, and S. Pandey, “Pancratistatin: a natural anti-cancer compound that targets mitochondria specifically in cancer cells to induce apoptosis,” Apoptosis, vol. 10, no. 3, pp. 619–630, 2005. View at Publisher · View at Google Scholar · View at Scopus
  115. M. Y. Kim, L. J. Trudel, and G. N. Wogan, “Apoptosis induced by capsaicin and resveratrol in colon carcinoma cells requires nitric oxide production and caspase activation,” Anticancer Research, vol. 29, no. 10, pp. 3733–3740, 2009. View at Google Scholar · View at Scopus
  116. J. Z. Boyer, J. Jandova, J. Janda et al., “Resveratrol-sensitized UVA induced apoptosis in human keratinocytes through mitochondrial oxidative stress and pore opening,” Journal of Photochemistry and Photobiology B, vol. 113, pp. 42–50, 2012. View at Google Scholar
  117. E. C. Filippi-Chiela, E. S. Villodre, L. L. Zamin, and G. Lenz, “Autophagy interplay with apoptosis and cell cycle regulation in the growth inhibiting effect of resveratrol in glioma cells,” PLoS ONE, vol. 6, no. 6, Article ID e20849, 2011. View at Publisher · View at Google Scholar · View at Scopus
  118. X. Wang, A. W. Leung, J. Luo, and C. Xu, “TEM observation of ultrasound-induced mitophagy in nasopharyngeal carcinoma cells in the presence of curcumin,” Experimental and Therapeutic Medicine, vol. 3, no. 1, pp. 146–148, 2012. View at Google Scholar
  119. H. Qian, Y. Yang, and X. Wang, “Curcumin enhanced adriamycin-induced human liver-derived Hepatoma G2 cell death through activation of mitochondria-mediated apoptosis and autophagy,” European Journal of Pharmaceutical Sciences, vol. 43, no. 3, pp. 125–131, 2011. View at Publisher · View at Google Scholar · View at Scopus
  120. M. Strofer, W. Jelkmann, and R. Depping, “Curcumin decreases survival of Hep3B liver and MCF-7 breast cancer cells: the role of HIF,” Strahlentherapie und Onkologie, vol. 187, no. 7, pp. 393–400, 2011. View at Google Scholar
  121. M. Nepal, H. J. Choi, B. Y. Choi et al., “Anti-angiogenic and anti-tumor activity of Bavachinin by targeting hypoxia-inducible factor-1alpha,” European Journal of Pharmacology, vol. 691, no. 1–3, pp. 28–37, 2012. View at Google Scholar
  122. C. Yang, J. Sudderth, T. Dang, R. M. Bachoo, J. G. McDonald, and R. J. DeBerardinis, “Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling,” Cancer Research, vol. 69, no. 20, pp. 7986–7993, 2009. View at Publisher · View at Google Scholar · View at Scopus
  123. C. Li, A. Allen, J. Kwagh et al., “Green tea polyphenols modulate insulin secretion by inhibiting glutamate dehydrogenase,” The Journal of Biological Chemistry, vol. 281, no. 15, pp. 10214–10221, 2006. View at Publisher · View at Google Scholar · View at Scopus
  124. C. Li, M. Li, P. Chen et al., “Green tea polyphenols control dysregulated glutamate dehydrogenase in transgenic mice by hijacking the ADP activation site,” The Journal of Biological Chemistry, vol. 286, no. 39, pp. 34164–34174, 2011. View at Google Scholar
  125. S. Smith, “The animal fatty acid synthase: one gene, one polypeptide, seven enzymes,” The FASEB Journal, vol. 8, no. 15, pp. 1248–1259, 1994. View at Google Scholar · View at Scopus
  126. H. Liu, J. Y. Liu, X. Wu, and J. T. Zhang, “Biochemistry, molecular biology, and pharmacology of fatty acid synthase, an emerging therapeutic target and diagnosis/prognosis marker,” International Journal of Biochemistry and Molecular Biology, vol. 1, no. 1, pp. 69–89, 2010. View at Google Scholar · View at Scopus
  127. D. Vance, I. Goldberg, O. Mitsuhashi, and K. Bloch, “Inhibition of fatty acid synthetases by the antibiotic cerulenin,” Biochemical and Biophysical Research Communications, vol. 48, no. 3, pp. 649–656, 1972. View at Google Scholar · View at Scopus
  128. S. J. Kridel, F. Axelrod, N. Rozenkrantz, and J. W. Smith, “Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity,” Cancer Research, vol. 64, no. 6, pp. 2070–2075, 2004. View at Publisher · View at Google Scholar · View at Scopus
  129. B. Liu, Y. Wang, K. L. Fillgrove, and V. E. Anderson, “Triclosan inhibits enoyl-reductase of type I fatty acid synthase in vitro and is cytotoxic to MCF-7 and SKBr-3 breast cancer cells,” Cancer Chemotherapy and Pharmacology, vol. 49, no. 3, pp. 187–193, 2002. View at Publisher · View at Google Scholar · View at Scopus
  130. Y. J. Jin, S. Z. Li, Z. S. Zhao et al., “Carnitine palmitoyltransferase-1 (CPT-1) activity stimulation by cerulenin via sympathetic nervous system activation overrides cerulenin's peripheral effect,” Endocrinology, vol. 145, no. 7, pp. 3197–3204, 2004. View at Publisher · View at Google Scholar · View at Scopus
  131. S. H. Cha, Z. Hu, S. Chohnan, and M. D. Lane, “Inhibition of hypothalamic fatty acid synthase triggers rapid activation of fatty acid oxidation in skeletal muscle,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 41, pp. 14557–14562, 2005. View at Publisher · View at Google Scholar · View at Scopus
  132. A. R. Rendina and D. Cheng, “Characterization of the inactivation of rat fatty acid synthase by C75: inhibition of partial reactions and protection by substrates,” Biochemical Journal, vol. 388, no. 3, pp. 895–903, 2005. View at Publisher · View at Google Scholar · View at Scopus
  133. W. X. Tian, “Inhibition of fatty acid synthase by polyphenols,” Current Medicinal Chemistry, vol. 13, no. 8, pp. 967–977, 2006. View at Publisher · View at Google Scholar · View at Scopus
  134. X. Wang, K. S. Song, Q. X. Guo, and W. X. Tian, “The galloyl moiety of green tea catechins is the critical structural feature to inhibit fatty-acid synthase,” Biochemical Pharmacology, vol. 66, no. 10, pp. 2039–2047, 2003. View at Publisher · View at Google Scholar · View at Scopus
  135. R. Zhang, W. Xiao, X. Wang, X. Wu, and W. Tian, “Novel inhibitors of fatty-acid synthase from green tea (Camellia sinensis Xihu Longjing) with high activity and a new reacting site,” Biotechnology and Applied Biochemistry, vol. 43, no. 1, pp. 1–7, 2006. View at Publisher · View at Google Scholar · View at Scopus
  136. B. H. Li and W. X. Tian, “Inhibitory effects of flavonoids on animal fatty acid synthase,” Journal of Biochemistry, vol. 135, no. 1, pp. 85–91, 2004. View at Publisher · View at Google Scholar · View at Scopus
  137. K. Brusselmans, R. Vrolix, G. Verhoeven, and J. V. Swinnen, “Induction of cancer cell apoptosis by flavonoids is associated with their ability to inhibit fatty acid synthase activity,” The Journal of Biological Chemistry, vol. 280, no. 7, pp. 5636–5645, 2005. View at Publisher · View at Google Scholar · View at Scopus
  138. B. H. Li, X. F. Ma, Y. Wang, and W. X. Tian, “Structure-activity relationship of polyphenols that inhibit fatty acid synthase,” Journal of Biochemistry, vol. 138, no. 6, pp. 679–685, 2005. View at Publisher · View at Google Scholar · View at Scopus
  139. J. Zhao, X. B. Sun, F. Ye, and W. X. Tian, “Suppression of fatty acid synthase, differentiation and lipid accumulation in adipocytes by curcumin,” Molecular and Cellular Biochemistry, vol. 351, no. 1-2, pp. 19–28, 2011. View at Publisher · View at Google Scholar · View at Scopus
  140. A. A. Nanji, K. Jokelainen, G. L. Tipoe, A. Rahemtulla, P. Thomas, and A. J. Dannenberg, “Curcumin prevents alcohol-induced liver disease in rats by inhibiting the expression of NF-κB-dependent genes,” American Journal of Physiology, vol. 284, no. 2, pp. G321–G327, 2003. View at Google Scholar · View at Scopus
  141. C. M. Hung, Y. H. Su, H. Y. Lin et al., “Demethoxycurcumin Modulates Prostate Cancer Cell Proliferation via AMPK-Induced Down-regulation of HSP70 and EGFR,” Journal of Agricultural and Food Chemistry, vol. 60, no. 34, pp. 8427–8434, 2012. View at Publisher · View at Google Scholar
  142. V. Soetikno, F. R. Sari, V. Sukumaran et al., “Curcumin decreases renal triglyceride accumulation through AMPK-SREBP signaling pathway in streptozotocin-induced type 1 diabetic rats,” The Journal of Nutritional Biochemistry, vol. 24, no. 5, pp. 796–802, 2012. View at Publisher · View at Google Scholar
  143. C. W. Yeh, W. J. Chen, C. T. Chiang, S. Y. Lin-Shiau, and J. K. Lin, “Suppression of fatty acid synthase in MCF-7 breast cancer cells by tea and tea polyphenols: a possible mechanism for their hypolipidemic effects,” The Pharmacogenomics Journal, vol. 3, no. 5, pp. 267–276, 2003. View at Google Scholar · View at Scopus
  144. X. Hou, S. Xu, K. A. Maitland-Toolan et al., “SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase,” The Journal of Biological Chemistry, vol. 283, no. 29, pp. 20015–20026, 2008. View at Publisher · View at Google Scholar · View at Scopus
  145. S. M. Shin, I. J. Cho, and S. G. Kim, “Resveratrol protects mitochondria against oxidative stress through AMP-activated protein kinase-mediated glycogen synthase kinase-3β inhibition downstream of poly(ADP-ribose) polymerase-LKB1 pathway,” Molecular Pharmacology, vol. 76, no. 4, pp. 884–895, 2009. View at Publisher · View at Google Scholar · View at Scopus
  146. M. Y. Yang, C. H. Peng, K. C. Chan, Y. I. S. Yang, C. N. Huang, and C. J. Wang, “The hypolipidemic effect of Hibiscus sabdariffa polyphenols via inhibiting lipogenesis and promoting hepatic lipid clearance,” Journal of Agricultural and Food Chemistry, vol. 58, no. 2, pp. 850–859, 2010. View at Publisher · View at Google Scholar · View at Scopus
  147. J. A. Menendez, A. Vazquez-Martin, C. Oliveras-Ferraros et al., “Analyzing effects of extra-virgin olive polyphenols on breast cancer-associated fatty acid synthase protein expression using reverse-phase protein microarrays,” International Journal of Molecular Medicine, vol. 22, no. 4, pp. 433–439, 2008. View at Publisher · View at Google Scholar · View at Scopus
  148. M. Notarnicola, S. Pisanti, V. Tutino et al., “Effects of olive oil polyphenols on fatty acid synthase gene expression and activity in human colorectal cancer cells,” Genes and Nutrition, vol. 6, no. 1, pp. 63–69, 2011. View at Publisher · View at Google Scholar · View at Scopus