Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2016 (2016), Article ID 1972793, 9 pages
http://dx.doi.org/10.1155/2016/1972793
Research Article

Fisetin Modulates Antioxidant Enzymes and Inflammatory Factors to Inhibit Aflatoxin-B1 Induced Hepatocellular Carcinoma in Rats

Biochemistry Section, Department of Zoology, Banaras Hindu University, Varanasi 221005, India

Received 19 June 2015; Accepted 11 August 2015

Academic Editor: Sahdeo Prasad

Copyright © 2016 Brajesh Kumar Maurya and Surendra Kumar Trigun. 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. T. B. Kryston, A. B. Georgiev, P. Pissis, and A. G. Georgakilas, “Role of oxidative stress and DNA damage in human carcinogenesis,” Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, vol. 711, no. 1-2, pp. 193–201, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. M. E. Smela, S. S. Currier, E. A. Bailey, and J. M. Essigmann, “The chemistry and biology of aflatoxin B1: from mutational spectrometry to carcinogenesis,” Carcinogenesis, vol. 22, no. 4, pp. 535–545, 2001. View at Publisher · View at Google Scholar · View at Scopus
  3. Y. Fujimoto, L. L. Hampton, L.-D. Luo, P. J. Wirth, and S. S. Thorgeirsson, “Low frequency of p53 gene mutation in tumors induced by aflatoxin B1 in nonhuman primates,” Cancer Research, vol. 52, no. 4, pp. 1044–1046, 1992. View at Google Scholar · View at Scopus
  4. G. Landskron, M. De La Fuente, P. Thuwajit, C. Thuwajit, and M. A. Hermoso, “Chronic inflammation and cytokines in the tumor microenvironment,” Journal of Immunology Research, vol. 2014, Article ID 149185, 19 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  5. T. Sakurai, G. He, A. Matsuzawa et al., “Hepatocyte necrosis induced by oxidative stress and IL-1α release mediate carcinogen-induced compensatory proliferation and liver tumorigenesis,” Cancer Cell, vol. 14, no. 2, pp. 156–165, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. P. Huang, L. Feng, E. A. Oldham, M. J. Keating, and W. Plunkett, “Superoxide dismutase as a target for the selective killing of cancer cells,” Nature, vol. 407, no. 6802, pp. 390–395, 2000. View at Publisher · View at Google Scholar · View at Scopus
  7. K. A. Conklin, “Cancer chemotherapy and antioxidants,” Journal of Nutrition, vol. 134, pp. 3201S–3204S, 2004. View at Google Scholar
  8. Y. Hasegawa, T. Takano, A. Miyauchi et al., “Decreased expression of glutathione peroxidase mRNA in thyroid anaplastic carcinoma,” Cancer Letters, vol. 182, no. 1, pp. 69–74, 2002. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Pelicano, D. Carney, and P. Huang, “ROS stress in cancer cells and therapeutic implications,” Drug Resistance Updates, vol. 7, no. 2, pp. 97–110, 2004. View at Publisher · View at Google Scholar · View at Scopus
  10. K. Aquilano, P. Vigilanza, G. Rotilio, and M. R. Ciriolo, “Mitochondrial damage due to SOD1 deficiency in SH-SY5Y neuroblastoma cells: a rationale for the redundancy of SOD1,” The FASEB Journal, vol. 20, no. 10, pp. 1683–1685, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. W.-Q. Ding, J. L. Vaught, H. Yamauchi, and S. E. Lind, “Differential sensitivity of cancer cells to docosahexaenoic acid-induced cytotoxicity: the potential importance of down-regulation of superoxide dismutase 1 expression,” Molecular Cancer Therapeutics, vol. 3, no. 9, pp. 1109–1117, 2004. View at Google Scholar · View at Scopus
  12. H.-L. Ha, H.-J. Shin, M. A. Feitelson, and D.-Y. Yu, “Oxidative stress and antioxidants in hepatic pathogenesis,” World Journal of Gastroenterology, vol. 16, no. 48, pp. 6035–6043, 2010. View at Publisher · View at Google Scholar · View at Scopus
  13. A. Naiki-Ito, M. Asamoto, N. Hokaiwado et al., “Gpx2 is an overexpressed gene in rat breast cancers induced by three different chemical carcinogens,” Cancer Research, vol. 67, no. 23, pp. 11353–11358, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. R. Brigelius-Flohé and A. Kipp, “Glutathione peroxidases in different stages of carcinogenesis,” Biochimica et Biophysica Acta, vol. 1790, no. 11, pp. 1555–1568, 2009. View at Publisher · View at Google Scholar · View at Scopus
  15. K. B. Singh, B. K. Maurya, and S. K. Trigun, “Activation of oxidative stress and inflammatory factors could account for histopathological progression of aflatoxin-B1 induced hepatocarcinogenesis in rat,” Molecular and Cellular Biochemistry, vol. 401, no. 1-2, pp. 185–196, 2015. View at Publisher · View at Google Scholar
  16. A. Bishyee, “The role of inflammation and liver cancer,” Advances in Experimental Medicine and Biology, vol. 816, pp. 401–435, 2014. View at Google Scholar
  17. R. J. Moore, D. M. Owens, G. Stamp et al., “Mice deficient in tumor necrosis factor-α are resistant to skin carcinogenesis,” Nature Medicine, vol. 5, no. 7, pp. 828–831, 1999. View at Publisher · View at Google Scholar
  18. F. Balkwill, “Tumour necrosis factor and cancer,” Nature Reviews Cancer, vol. 9, no. 5, pp. 361–371, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Giavazzi, A. Garofalo, M. R. Bani et al., “Interleukin 1-induced augmentation of experimental metastases from a human melanoma in nude mice,” Cancer Research, vol. 50, no. 15, pp. 4771–4775, 1990. View at Google Scholar · View at Scopus
  20. A. Mantovani, P. Allavena, A. Sica, and F. Balkwill, “Cancer-related inflammation,” Nature, vol. 454, no. 7203, pp. 436–444, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. V. Afonso, G. Santos, P. Collin et al., “Tumor necrosis factor-α down-regulates human Cu/Zn superoxide dismutase 1 promoter via JNK/AP-1 signaling pathway,” Free Radical Biology and Medicine, vol. 41, no. 5, pp. 709–721, 2006. View at Publisher · View at Google Scholar · View at Scopus
  22. Y. Qin, S. Ekmekcioglu, P. Liu et al., “Constitutive aberrant endogenous interleukin-1 facilitates inflammation and growth in human melanoma,” Molecular Cancer Research, vol. 9, no. 11, pp. 1537–1550, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. K. B. Singh and S. K. Trigun, “Apoptosis of Dalton's lymphoma due to in vivo treatment with emodin is associated with modulations of hydrogen peroxide metabolizing antioxidant enzymes,” Cell Biochemistry and Biophysics, vol. 67, no. 2, pp. 439–449, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. M. C. Dias, M. A. M. Rodrigues, M. C. H. Reimberg, and L. F. Barbisan, “Protective effects of Ginkgo biloba against rat liver carcinogenesis,” Chemico-Biological Interactions, vol. 173, no. 1, pp. 32–42, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. V. Ravinayagam, R. Jaganathan, S. Panchanadham, and S. Palanivelu, “Potential antioxidant role of tridham in managing oxidative stress against aflatoxin-B1-induced experimental hepatocellular carcinoma,” International Journal of Hepatology, vol. 2012, Article ID 428373, 9 pages, 2012. View at Publisher · View at Google Scholar
  26. I. Rahman, S. K. Biswas, and P. A. Kirkham, “Regulation of inflammation and redox signaling by dietary polyphenols,” Biochemical Pharmacology, vol. 72, no. 11, pp. 1439–1452, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. K. A. Kang, M. J. Piao, K. C. Kim et al., “Fisetin attenuates hydrogen peroxide-induced cell damage by scavenging reactive oxygen species and activating protective functions of cellular glutathione system,” In Vitro Cellular and Developmental Biology—Animal, vol. 50, no. 1, pp. 66–74, 2014. View at Publisher · View at Google Scholar · View at Scopus
  28. X. Lu, I. J. Jae, J. C. Han et al., “Fisetin inhibits the activities of cyclin-dependent kinases leading to cell cycle arrest in HT-29 human colon cancer cells,” Journal of Nutrition, vol. 135, no. 12, pp. 2884–2890, 2005. View at Google Scholar · View at Scopus
  29. V. M. Adhami, D. N. Syed, N. Khan, and H. Mukhtar, “Dietary flavonoid fisetin: a novel dual inhibitor of PI3K/Akt and mTOR for prostate cancer management,” Biochemical Pharmacology, vol. 84, no. 10, pp. 1277–1281, 2012. View at Publisher · View at Google Scholar · View at Scopus
  30. T. A. Bhat, D. Nambiar, A. Pal, R. Agarwal, and R. P. Singh, “Fisetin inhibits various attributes of angiogenesis in vitro and in vivo-implications for angioprevention,” Carcinogenesis, vol. 33, no. 2, pp. 385–393, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. J. Y. Kim, Y. K. Jeon, W. Jeon, and M. J. Nam, “Fisetin induces apoptosis in Huh-7 cells via downregulation of BIRC8 and Bcl2L2,” Food and Chemical Toxicology, vol. 48, no. 8-9, pp. 2259–2264, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Ravichandran, G. Suresh, B. Ramesh, and G. Vijaiyan Siva, “Fisetin, a novel flavonol attenuates benzo(a)pyrene-induced lung carcinogenesis in Swiss albino mice,” Food and Chemical Toxicology, vol. 49, no. 5, pp. 1141–1147, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. A. Mookerjee, J. M. Basu, S. Majumder et al., “A novel copper complex induces ROS generation in doxorubicin resistant Ehrlich ascitis carcinoma cells and increases activity of antioxidant enzymes in vital organs in vivo,” BMC Cancer, vol. 6, article 267, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. O. H. Lowry, N. J. Rosbrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951. View at Google Scholar · View at Scopus
  35. P. T. Schumacker, “Reactive oxygen species in cancer cells: live by the sword, die by the sword,” Cancer Cell, vol. 10, no. 3, pp. 175–176, 2006. View at Publisher · View at Google Scholar · View at Scopus
  36. G. Liou and P. Storz, “Reactive oxygen species in cancer,” Free Radical Research, vol. 44, no. 5, pp. 479–496, 2010. View at Publisher · View at Google Scholar
  37. R. K. Koiri, S. K. Trigun, and L. Mishra, “Activation of p53 mediated glycolytic inhibition-oxidative stress-apoptosis pathway in Dalton's lymphoma by a ruthenium (II)-complex containing 4-carboxy N-ethylbenzamide,” Biochimie, vol. 110, pp. 52–61, 2015. View at Publisher · View at Google Scholar · View at Scopus
  38. G. Ramakrishnan, H. R. B. Raghavendran, R. Vinodhkumar, and T. Devaki, “Suppression of N-nitrosodiethylamine induced hepatocarcinogenesis by silymarin in rats,” Chemico-Biological Interactions, vol. 161, no. 2, pp. 104–114, 2006. View at Publisher · View at Google Scholar · View at Scopus
  39. S. Higa, T. Hirano, M. Kotani et al., “Fisetin a flavonol, inhibits TH2-type cytokine production by activated human basophils,” Journal of Allergy and Clinical Immunology, vol. 111, pp. 1299–1306, 2003. View at Google Scholar
  40. N. Li, T. D. Oberley, L. W. Oberley, and W. Zhong, “Overexpression of manganese superoxide dismutase in DU145 human prostate carcinoma cells has multiple effects on cell phenotype,” Prostate, vol. 35, no. 3, pp. 221–233, 1998. View at Google Scholar · View at Scopus
  41. Y. Zhang, W. Zhao, H. J. Zhang, F. E. Domann, and L. W. Oberley, “Overexpression of copper zinc superoxide dismutase suppresses human glioma cell growth,” Cancer Research, vol. 62, no. 4, pp. 1205–1212, 2002. View at Google Scholar · View at Scopus
  42. 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
  43. P. Amstad, A. Peskin, G. Shah et al., “The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress,” Biochemistry, vol. 30, no. 38, pp. 9305–9313, 1991. View at Publisher · View at Google Scholar · View at Scopus
  44. P. Amstad, R. Moret, and P. Cerutti, “Glutathione peroxidase compensates for the hypersensitivity of Cu–Zn-superoxide dismutase overproducers to oxidant stress,” The Journal of Biological Chemistry, vol. 269, no. 3, pp. 1606–1609, 1994. View at Google Scholar · View at Scopus
  45. E. O. Farombi, B. I. Olowu, and G. O. Emerole, “Effect of three structurally related antimalarial drugs on liver microsomal components and lipid peroxidation in rats,” Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, vol. 126, no. 3, pp. 217–224, 2000. View at Publisher · View at Google Scholar · View at Scopus
  46. H. U. Nwanjo and G. O. Oze, “Oxidative imbalance and non-enzymic antioxidant status in pulmonary tuberculosis infected subjects: carcinogenic potential,” Pakistan Journal of Nutrition, vol. 6, no. 6, pp. 590–592, 2007. View at Publisher · View at Google Scholar · View at Scopus
  47. X. G. Lei, “In vivo antioxidant role of glutathione peroxidase: evidence from knockout mice,” Methods in Enzymology, vol. 347, pp. 213–225, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. J. L. Schwartz and G. Shklar, “Glutathione inhibits experimental oral carcinogenesis, p53 expression, and angiogenesis,” Nutrition and Cancer, vol. 26, no. 2, pp. 229–236, 1996. View at Publisher · View at Google Scholar · View at Scopus
  49. S. Nowsheen, K. Aziz, T. B. Kryston, N. F. Ferguson, and A. Georgakilas, “The interplay between inflammation and oxidative stress in carcinogenesis,” Current Molecular Medicine, vol. 12, no. 6, pp. 672–680, 2012. View at Publisher · View at Google Scholar · View at Scopus