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Oxidative Medicine and Cellular Longevity
Volume 2016 (2016), Article ID 3123294, 12 pages
http://dx.doi.org/10.1155/2016/3123294
Research Article

24-Week Exposure to Oxidized Tyrosine Induces Hepatic Fibrosis Involving Activation of the MAPK/TGF-β1 Signaling Pathway in Sprague-Dawley Rats Model

1The Laboratory of Food Nutrition and Functional Factors, Food Science and Technology, Jiangnan University, Wuxi 214122, China
2The State Key Laboratory of Food Science and Technology, Food Science and Technology, Jiangnan University, Wuxi 214122, China

Received 29 July 2015; Accepted 9 September 2015

Academic Editor: Tilman Grune

Copyright © 2016 Zhuqing Leslie 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. E. R. Stadtman and R. L. Levine, “Protein oxidation,” Annals of the New York Academy of Sciences, vol. 899, pp. 191–208, 2000. View at Google Scholar · View at Scopus
  2. T. K. Dalsgaard, J. H. Nielsen, B. E. Brown, N. Stadler, and M. J. Davies, “Dityrosine, 3,4-dihydroxyphenylalanine (DOPA), and radical formation from tyrosine residues on milk proteins with globular and flexible structures as a result of riboflavin-mediated photo-oxidation,” Journal of Agricultural and Food Chemistry, vol. 59, no. 14, pp. 7939–7947, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. H. J. Kim and N. D. Vaziri, “Contribution of impaired Nrf2-Keap1 pathway to oxidative stress and inflammation in chronic renal failure,” American Journal of Physiology: Renal Physiology, vol. 298, no. 3, pp. F662–F671, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. J. Meltretter, C.-M. Becker, and M. Pischetsrieder, “Identification and site-specific relative quantification of β-lactoglobulin modifications in heated milk and dairy products,” Journal of Agricultural and Food Chemistry, vol. 56, no. 13, pp. 5165–5171, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. E. R. Stadtman, “Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions,” Annual Review of Biochemistry, vol. 62, pp. 797–821, 1993. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Utrera and M. Estévez, “Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway,” Journal of Agricultural and Food Chemistry, vol. 60, no. 32, pp. 8002–8011, 2012. View at Publisher · View at Google Scholar · View at Scopus
  7. Y. L. Xiong, S. P. Blanchard, T. Ooizumi, and Y. Ma, “Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein,” Journal of Food Science, vol. 75, no. 2, pp. C215–C221, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. M. Tong, L. Longato, and S. M. de la Monte, “Early limited nitrosamine exposures exacerbate high fat diet-mediated type 2 diabetes and neurodegeneration,” BMC Endocrine Disorders, vol. 10, article 4, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. P. Voss and T. Grune, Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases, I. Dalle-Donne, A. Scaloni, D. A. Butterfield, Eds., John Wiley & Sons, Hoboken, NJ, USA, 2006.
  10. F. Xie, S. Sun, A. Xu et al., “Advanced oxidation protein products induce intestine epithelial cell death through a redox-dependent, c-jun N-terminal kinase and poly (ADP-ribose) polymerase-1-mediated pathway,” Cell Death & Disease, vol. 5, article 542, 2014. View at Publisher · View at Google Scholar · View at Scopus
  11. W. Fang, J. Sun, Z. L. Li, G. Le, and Y. Shi, “Effect of oxidated food protein on mice gut floraand redox state,” Chinese Journal of Microecology, vol. 24, pp. 193–196, 2012. View at Google Scholar
  12. Z. L. Li, L. Wu, G. Le, and Y. Shi, “Effect of oxidized casein on the oxidative damage of blood and digestive organs in mice,” Acta Nutrimenta Sinica, vol. 35, no. 1, pp. 39–43, 2013. View at Google Scholar
  13. Z. L. Li, L. Mo, G. Le, and Y. Shi, “Oxidized casein impairs antioxidant defense system and induces hepatic and renal injury in mice,” Food and Chemical Toxicology, vol. 64, pp. 86–93, 2014. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. Fukuchi, Y. Miura, Y. Nabeno, Y. Kato, T. Osawa, and M. Naito, “Immunohistochemical detection of oxidative stress biomarkers, dityrosine and Nε-(hexanoyl)lysine, and C-reactive protein in rabbit atherosclerotic lesions,” Journal of Atherosclerosis and Thrombosis, vol. 15, no. 4, pp. 185–192, 2008. View at Publisher · View at Google Scholar · View at Scopus
  15. D. A. Malencik and S. R. Anderson, “Dityrosine as a product of oxidative stress and fluorescent probe,” Amino Acids, vol. 25, no. 3-4, pp. 233–247, 2003. View at Publisher · View at Google Scholar · View at Scopus
  16. T. Kurahashi, A. Miyazaki, S. Suwan, and M. Isobe, “Extensive investigations on oxidized amino acid residues in H2O2-treated Cu,Zn-SOD protein with LC-ESI-Q-TOF-MS, MS/MS for the determination of the copper-binding site,” Journal of the American Chemical Society, vol. 123, no. 38, pp. 9268–9278, 2001. View at Publisher · View at Google Scholar · View at Scopus
  17. C. N. Oliver, B.-W. Ahn, E. J. Moerman, S. Goldstein, and E. R. Stadtman, “Age-related changes in oxidized proteins,” The Journal of Biological Chemistry, vol. 262, no. 12, pp. 5488–5491, 1987. View at Google Scholar · View at Scopus
  18. W. L. Boatright and N. S. Hettiarachchy, “Effect of lipids on soy protein isolate solubility,” Journal of the American Oil Chemists' Society, vol. 72, no. 12, pp. 1439–1444, 1995. View at Publisher · View at Google Scholar · View at Scopus
  19. H. Kobayashi, E. Gil-Guzman, A. M. Mahran et al., “Quality control of reactive oxygen species measurement by luminol-dependent chemiluminescence assay,” Journal of Andrology, vol. 22, no. 4, pp. 568–574, 2001. View at Google Scholar · View at Scopus
  20. P. J. Hissin and R. Hilf, “A fluorometric method for determination of oxidized and reduced glutathione in tissues,” Analytical Biochemistry, vol. 74, no. 1, pp. 214–226, 1976. View at Publisher · View at Google Scholar · View at Scopus
  21. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951. View at Google Scholar · View at Scopus
  22. F. Fenaille, V. Parisod, J. Vuichoud, J.-C. Tabet, and P. A. Guy, “Quantitative determination of dityrosine in milk powders by liquid chromatography coupled to tandem mass spectrometry using isotope dilution,” Journal of Chromatography A, vol. 1052, no. 1-2, pp. 77–84, 2004. View at Publisher · View at Google Scholar · View at Scopus
  23. S. M. Abdel-Fattah, M. I. Sanad, M. A. Safaa, and F. F. Ragaa, “The protective effect of white ginseng against biochemical and pathological changes induced by aflatoxins in rats,” The Journal of American Science, vol. 6, no. 12, pp. 461–472, 2010. View at Google Scholar
  24. J. S. Ozer, R. Chetty, G. Kenna et al., “Enhancing the utility of alanine aminotransferase as a reference standard biomarker for drug-induced liver injury,” Regulatory Toxicology and Pharmacology, vol. 56, no. 3, pp. 237–246, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. T. A. Woreta and S. A. Alqahtani, “Evaluation of abnormal liver tests,” Medical Clinics of North America, vol. 98, no. 1, pp. 1–16, 2014. View at Publisher · View at Google Scholar · View at Scopus
  26. K. H. Cheeseman and T. F. Slater, “An introduction to free radical biochemistry,” British Medical Bulletin, vol. 49, no. 3, pp. 481–493, 1993. View at Google Scholar · View at Scopus
  27. A. Rezaie, R. D. Parker, and M. Abdollahi, “Oxidative stress and pathogenesis of inflammatory bowel disease: an epiphenomenon or the cause?” Digestive Diseases and Sciences, vol. 52, no. 9, pp. 2015–2021, 2007. View at Publisher · View at Google Scholar · View at Scopus
  28. D. M. Bissell, “Hepatic fibrosis as wound repair: a progress report,” Journal of Gastroenterology, vol. 33, no. 2, pp. 295–302, 1998. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Gabriel, R. H. Kuddus, A. S. Rao, and C. R. Gandhi, “Down-regulation of endothelin receptors by transforming growth factor β1 in hepatic stellate cells,” Journal of Hepatology, vol. 30, no. 3, pp. 440–450, 1999. View at Publisher · View at Google Scholar · View at Scopus
  30. V. Witko-Sarsat, T. Nguyen-Khoa, P. Jungers, T. B. Drüeke, and B. Descamps-Latscha, “Advanced oxidation protein products as a novel molecular basis of oxidative stress in uraemia,” Nephrology Dialysis Transplantation, vol. 14, no. 1, pp. 76–78, 1999. View at Google Scholar · View at Scopus
  31. V. J. Desmet, M. Gerber, J. H. Hoofnagle, M. Manns, and P. J. Scheuer, “Classification of chronic hepatitis: diagnosis, grading and staging,” Hepatology, vol. 19, no. 6, pp. 1513–1520, 1994. View at Publisher · View at Google Scholar · View at Scopus
  32. J.-H. Lee, H. Lee, Y. K. Joung et al., “The use of low molecular weight heparin-pluronic nanogels to impede liver fibrosis by inhibition the TGF-β/Smad signaling pathway,” Biomaterials, vol. 32, no. 5, pp. 1438–1445, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. A. Pellicoro, P. Ramachandran, and J. P. Iredale, “Reversibility of liver fibrosis,” Fibrogenesis & Tissue Repair, vol. 5, supplement 1, article S26, pp. 281–289, 2012. View at Google Scholar
  34. A. J. Czaja, “The prevention and reversal of hepatic fibrosis in autoimmune hepatitis,” Alimentary Pharmacology & Therapeutics, vol. 39, no. 4, pp. 385–406, 2014. View at Publisher · View at Google Scholar · View at Scopus
  35. X. Zhai, K. Yan, Y. Zhou et al., “The β-catenin pathway contributes to the effects of leptin on SREBP-1c expression in rat hepatic stellate cells and liver fibrosis,” British Journal of Pharmacology, vol. 169, no. 1, pp. 197–212, 2013. View at Publisher · View at Google Scholar · View at Scopus
  36. A. Boye, “Compound Astragalus and Salvia miltiorrhiza extracts modulate MAPK-regulated TGF-β/Smad signaling in hepatocellular carcinoma by multi-target mechanism,” Journal of Ethnopharmacology, vol. 169, pp. 219–228, 2015. View at Publisher · View at Google Scholar
  37. X. Wang, J. Z. Liu, J. X. Hu et al., “ROS-activated p38 MAPK/ERK-Akt cascade plays a central role in palmitic acid-stimulated hepatocyte proliferation,” Free Radical Biology and Medicine, vol. 51, no. 2, pp. 539–551, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. X.-L. Liang and J.-Y. Yuan, “Effect of Chinese herbal compound on liver fibrosis in rabbits with schistosomiasis by B-ultrasound,” Asian Pacific Journal of Tropical Medicine, vol. 6, no. 8, pp. 658–662, 2013. View at Publisher · View at Google Scholar · View at Scopus