Table of Contents Author Guidelines Submit a Manuscript
Evidence-Based Complementary and Alternative Medicine
Volume 2013, Article ID 146142, 8 pages
http://dx.doi.org/10.1155/2013/146142
Research Article

Attenuation of Proinflammatory Responses by S-[6]-Gingerol via Inhibition of ROS/NF-Kappa B/COX2 Activation in HuH7 Cells

1Heart Research Institute, Newtown, NSW 2042, Australia
2Faculty of Pharmacy, University of Sydney, Camperdown, NSW 2006, Australia
3Department of Endocrinology, Dezhou People’s Hospital, Dezhou, Shandong 253014, China
4School of Medical and Molecular Biosciences, University of Technology, P.O. Box 123, Ultimo, NSW 2007, Australia

Received 14 February 2013; Revised 17 May 2013; Accepted 24 May 2013

Academic Editor: Ke Ren

Copyright © 2013 Xiao-Hong 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. G. S. Hotamisligil, “Inflammation and metabolic disorders,” Nature, vol. 444, no. 7121, pp. 860–867, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. P. Marceau, S. Biron, F.-S. Hould et al., “Liver pathology and the metabolic syndrome X in severe obesity,” Journal of Clinical Endocrinology and Metabolism, vol. 84, no. 5, pp. 1513–1517, 1999. View at Google Scholar · View at Scopus
  3. D. Cai, M. Yuan, D. F. Frantz et al., “Local and systemic insulin resistance resulting from hepatic activation of IKK-beta and NF-kappaB,” Nature Medicine, vol. 11, no. 2, pp. 183–190, 2005. View at Google Scholar
  4. S. Ghosh, M. J. May, and E. B. Kopp, “NF-κB and rel proteins: evolutionarily conserved mediators of immune responses,” Annual Review of Immunology, vol. 16, pp. 225–260, 1998. View at Publisher · View at Google Scholar · View at Scopus
  5. J. W. Christman, L. H. Lancaster, and T. S. Blackwell, “Nuclear factor κ B: a pivotal role in the systemic inflammatory response syndrome and new target for therapy,” Intensive Care Medicine, vol. 24, no. 11, pp. 1131–1138, 1998. View at Publisher · View at Google Scholar · View at Scopus
  6. S. A. Abd-El-Aleem, M. W. J. Ferguson, I. Appleton, A. Bhowmick, C. N. McCollum, and G. W. Ireland, “Expression of cyclooxytenase isoforms in normal human skin and chronic venous ulcers,” Journal of Pathology, vol. 195, no. 5, pp. 616–623, 2001. View at Publisher · View at Google Scholar · View at Scopus
  7. M. Afzal, D. Al-Hadidi, M. Menon, J. Pesek, and M. S. I. Dhami, “Ginger: an ethnomedical, chemical and pharmacological review,” Drug Metabolism and Drug Interactions, vol. 18, no. 3-4, pp. 159–190, 2001. View at Google Scholar · View at Scopus
  8. R. Grzanna, L. Lindmark, and C. G. Frondoza, “Ginger—an herbal medicinal product with broad anti-inflammatory actions,” Journal of Medicinal Food, vol. 8, no. 2, pp. 125–132, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. H. W. Jung, C.-H. Yoon, K. M. Park, H. S. Han, and Y.-K. Park, “Hexane fraction of Zingiberis Rhizoma Crudus extract inhibits the production of nitric oxide and proinflammatory cytokines in LPS-stimulated BV2 microglial cells via the NF-kappaB pathway,” Food and Chemical Toxicology, vol. 47, no. 6, pp. 1190–1197, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. C. G. Frondoza, A. Sohrabi, A. Polotsky, P. V. Phan, D. S. Hungerford, and L. Lindmark, “An in vitro screening assay for inhibitors of proinflammatory mediators in herbal extracts using human synoviocyte cultures,” In Vitro Cellular & Developmental Biology, vol. 40, no. 3-4, pp. 95–101, 2004. View at Google Scholar
  11. X.-H. Li, K. C.-Y. McGrath, S. Nammi, A. K. Heather, and B. D. Roufogalis, “Attenuation of liver pro-inflammatory responses by Zingiber officinale via inhibition of NF-kappa B activation in high-fat diet-fed rats,” Basic and Clinical Pharmacology and Toxicology, vol. 110, no. 3, pp. 238–244, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. A. A. Oyagbemi, A. B. Saba, and O. I. Azeez, “Molecular targets of [6]-gingerol: its potential roles in cancer chemoprevention,” BioFactors, vol. 36, no. 3, pp. 169–178, 2010. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Tripathi, K. G. Maier, D. Bruch, and D. S. Kittur, “Effect of 6-gingerol on pro-inflammatory cytokine production and costimulatory molecule expression in murine peritoneal macrophages,” Journal of Surgical Research, vol. 138, no. 2, pp. 209–213, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. C. Lee, G. H. Park, C.-Y. Kim, and J.-H. Jang, “[6]-Gingerol attenuates β-amyloid-induced oxidative cell death via fortifying cellular antioxidant defense system,” Food and Chemical Toxicology, vol. 49, no. 6, pp. 1261–1269, 2011. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Li, V. H. Tran, C. C. Duke, and B. D. Roufogalis, “Gingerols of Zingiber officinale enhance glucose uptake by increasing cell surface GLUT4 in cultured L6 myotubes,” Planta Medica, vol. 78, no. 14, pp. 1549–1555, 2012. View at Google Scholar
  16. A. K. Death, K. C. Y. McGrath, M. A. Sader et al., “Dihydrotestosterone promotes vascular cell adhesion molecule-1 expression in male human endothelial cells via a nuclear factor-κB-dependent pathway,” Endocrinology, vol. 145, no. 4, pp. 1889–1897, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. S. A. Bustin, “Absolute quantification of mrna using real-time reverse transcription polymerase chain reaction assays,” Journal of Molecular Endocrinology, vol. 25, no. 2, pp. 169–193, 2000. View at Google Scholar · View at Scopus
  18. K. C. Y. McGrath, X. H. Li, R. Puranik et al., “Role of 3β-hydroxysteroid-Δ24 reductase in mediating antiinflammatory effects of high-density lipoproteins in endothelial cells,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 29, no. 6, pp. 877–882, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. G. D. Anderson, S. D. Hauser, K. L. McGarity, M. E. Bremer, P. C. Isakson, and S. A. Gregory, “Selective inhibition of cyclooxygenase (COX)-2 reverses inflammation and expression of COX-2 and interleukin 6 in rat adjuvant arthritis,” The Journal of Clinical Investigation, vol. 97, no. 11, pp. 2672–2679, 1996. View at Google Scholar · View at Scopus
  20. J. P. Portanova, Y. Zhang, G. D. Anderson et al., “Selective neutralization of prostaglandin E2 blocks inflammation, hyperalgesia, and interleukin 6 production in vivo,” Journal of Experimental Medicine, vol. 184, no. 3, pp. 883–891, 1996. View at Google Scholar · View at Scopus
  21. K. Seibert, Y. Zhang, K. Leahy et al., “Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 25, pp. 12013–12017, 1994. View at Publisher · View at Google Scholar · View at Scopus
  22. H. K. Cho, K. J. Cheong, H. Y. Kim, and J. Cheong, “Endoplasmic reticulum stress induced by hepatitis B virus X protein enhances cyclo-oxygenase 2 expression via activating transcription factor 4,” Biochemical Journal, vol. 435, no. 2, pp. 431–439, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. C. S. Williams, M. Mann, and R. N. DuBois, “The role of cyclooxygenases in inflammation, cancer, and development,” Oncogene, vol. 18, no. 55, pp. 7908–7916, 1999. View at Google Scholar · View at Scopus
  24. N. S. Buttar and K. K. Wang, “The “aspirin” of the new millennium: cyclooxygenase-2 inhibitors,” Mayo Clinic Proceedings, vol. 75, no. 10, pp. 1027–1038, 2000. View at Google Scholar · View at Scopus
  25. E. Fosslien, “Biochemistry of cyclooxygenase (COX)-2 inhibitors and molecular pathology of COX-2 in neoplasia,” Critical Reviews in Clinical Laboratory Sciences, vol. 37, no. 5, pp. 431–502, 2000. View at Google Scholar · View at Scopus
  26. S. L. Tilley, T. M. Coffman, and B. H. Koller, “Mixed messages: modulation of inflammation and immune responses by prostaglandins and thromboxanes,” The Journal of Clinical Investigation, vol. 108, no. 1, pp. 15–23, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. S. Tsutakawa, D. Kobayashi, M. Kusama, T. Moriya, and N. Nakahata, “Nicotine enhances skin necrosis and expression of inflammatory mediators in a rat pressure ulcer model,” British Journal of Dermatology, vol. 161, no. 5, pp. 1020–1027, 2009. View at Publisher · View at Google Scholar · View at Scopus
  28. C. Yang, Z. Yang, M. Zhang et al., “Hydrogen sulfide protects against chemical hypoxia-induced cytotoxicity and inflammation in hacat cells through inhibition of ROS/NF-κB/COX-2 pathway,” PLoS ONE, vol. 6, no. 7, Article ID e21971, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. J. Vane, “Towards a better aspirin,” Nature, vol. 367, no. 6460, pp. 215–216, 1994. View at Publisher · View at Google Scholar · View at Scopus
  30. P.-C. Tseng, H.-C. Hsu, D. Janmanchi et al., “Helioxanthin inhibits interleukin-1β-induced MIP-1β production by reduction of c-jun expression and binding of the c-jun/CREB1 complex to the AP-1/CRE site of the MIP-1β promoter in Huh7 cells,” Biochemical Pharmacology, vol. 76, no. 9, pp. 1121–1133, 2008. View at Publisher · View at Google Scholar · View at Scopus
  31. R. Kleemann, L. Verschuren, B.-J. De Rooij et al., “Evidence for anti-inflammatory activity of statins and PPARα activators in human C-reactive protein transgenic mice in vivo and in cultured human hepatocytes in vitro,” Blood, vol. 103, no. 11, pp. 4188–4194, 2004. View at Publisher · View at Google Scholar · View at Scopus
  32. R. Kleemann, P. P. Gervois, L. Verschuren, B. Staels, H. M. G. Princen, and T. Kooistra, “Fibrates down-regulate IL-1-stimulated C-reactive protein gene expression in hepatocytes by reducing nuclear p50-NFκB-C/EBP-β complex formation,” Blood, vol. 101, no. 2, pp. 545–551, 2003. View at Publisher · View at Google Scholar · View at Scopus
  33. S. F. El-Tayeh, T. D. Hussein, M. E. El-Houseini, M. A. Amer, M. El-Sherbini, and W. M. Elshemey, “Serological biomarkers of hepatocellular carcinoma in Egyptian patients,” Disease Markers, vol. 32, no. 4, pp. 255–263, 2012. View at Publisher · View at Google Scholar · View at Scopus
  34. T. A. Pearson, G. A. Mensah, R. W. Alexander et al., “Markers of inflammation and cardiovascular disease: application to clinical and public health practice: a statement for healthcare professionals from the centers for disease control and prevention and the American Heart Association,” Circulation, vol. 107, no. 3, pp. 499–511, 2003. View at Publisher · View at Google Scholar · View at Scopus
  35. G. S. Hotamisligil, “Inflammatory pathways and insulin action,” International Journal of Obesity, vol. 27, supplement 3, pp. S53–S55, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. M. C. Arkan, A. L. Hevener, F. R. Greten et al., “IKK-beta links inflammation to obesity-induced insulin resistance,” Nature Medicine, vol. 11, no. 2, pp. 191–198, 2005. View at Google Scholar
  37. K. A. Roebuck, “Oxidant stress regulation of IL-8 and ICAM-1 gene expression: differential activation and binding of the transcription factors AP-1 and NF-kappaB (Review),” International Journal of Molecular Medicine, vol. 4, no. 3, pp. 223–230, 1999. View at Google Scholar · View at Scopus
  38. S. W. Kang, H. Z. Chae, M. S. Seo, K. Kim, I. C. Baines, and S. G. Rhee, “Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generatedin response to growth factors and tumor necrosis factor-α,” The Journal of Biological Chemistry, vol. 273, no. 11, pp. 6297–6302, 1998. View at Publisher · View at Google Scholar · View at Scopus
  39. H. Schenk, M. Klein, W. Erdbrügger, W. Dröge, and K. Schulze-Osthoff, “Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 5, pp. 1672–1676, 1994. View at Google Scholar
  40. R. Brigelius-Flohé, B. Friedrichs, S. Maurer, M. Schultz, and R. Streicher, “Interleukin-1-induced nuclear factor κB activation is inhibited by overexpression of phospholipid hydroperoxide glutathione peroxidase in a human endothelial cell line,” Biochemical Journal, vol. 328, no. 1, pp. 199–203, 1997. View at Google Scholar · View at Scopus
  41. S. K. Manna, H. J. Zhang, T. Yan, L. W. Oberley, and B. B. Aggarwal, “Overexpression of manganese superoxide dismutase suppresses tumor necrosis factor-induced apoptosis and activation of nuclear transcription factor-κB and activated protein-1,” The Journal of Biological Chemistry, vol. 273, no. 21, pp. 13245–13254, 1998. View at Publisher · View at Google Scholar · View at Scopus
  42. C. Kretz-Remy, P. Mehlen, M.-E. Mirault, and A.-P. Arrigo, “Inhibition of IκB-α phosphorylation and degradation and subsequent NF-κB activation by glutathione peroxidase overexpression,” Journal of Cell Biology, vol. 133, no. 5, pp. 1083–1093, 1996. View at Google Scholar · View at Scopus
  43. R. Lee, P. Beauparlant, H. Elford, P. Ponka, and J. Hiscott, “Selective inhibition of IκBα phosphorylation and HIV-1 LTR-directed gene expression by novel antioxidant compounds,” Virology, vol. 234, no. 2, pp. 277–290, 1997. View at Publisher · View at Google Scholar · View at Scopus
  44. X. Lu, F. Kambe, X. Cao et al., “3β-hydroxysteroid-Δ24 reductase is a hydrogen peroxide scavenger, protecting cells from oxidative stress-induced apoptosis,” Endocrinology, vol. 149, no. 7, pp. 3267–3273, 2008. View at Publisher · View at Google Scholar · View at Scopus