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Oxidative Medicine and Cellular Longevity
Volume 2016, Article ID 4768541, 10 pages
http://dx.doi.org/10.1155/2016/4768541
Research Article

Weaning Induced Hepatic Oxidative Stress, Apoptosis, and Aminotransferases through MAPK Signaling Pathways in Piglets

School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai Key Laboratory of Veterinary Biotechnology, Shanghai 200240, China

Received 2 June 2016; Revised 7 August 2016; Accepted 25 August 2016

Academic Editor: Claudio Cabello-Verrugio

Copyright © 2016 Zhen Luo 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. J. M. Campbell, J. D. Crenshaw, and J. Polo, “The biological stress of early weaned piglets,” Journal of Animal Science and Biotechnology, vol. 4, no. 1, article 19, 2013. View at Publisher · View at Google Scholar · View at Scopus
  2. G. Boudry, V. Péron, I. Le Huërou-Luron, J. P. Lallès, and B. Sève, “Weaning induces both transient and long-lasting modifications of absorptive, secretory, and barrier properties of piglet intestine,” The Journal of Nutrition, vol. 134, no. 9, pp. 2256–2262, 2004. View at Google Scholar · View at Scopus
  3. S. Pié, J. P. Lallès, F. Blazy, J. Laffitte, B. Sève, and I. P. Oswald, “Weaning is associated with an upregulation of expression of inflamatory cytokines in the intestine of piglets,” Journal of Nutrition, vol. 134, no. 3, pp. 641–647, 2004. View at Google Scholar · View at Scopus
  4. A. J. Moeser, C. Vander Klok, K. A. Ryan et al., “Stress signaling pathways activated by weaning mediate intestinal dysfunction in the pig,” American Journal of Physiology—Gastrointestinal and Liver Physiology, vol. 292, no. 1, pp. G173–G181, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. C. H. Hu, K. Xiao, Z. S. Luan, and J. Song, “Early weaning increases intestinal permeability, alters expression of cytokine and tight junction proteins, and activates mitogen-activated protein kinases in pigs,” Journal of Animal Science, vol. 91, no. 3, pp. 1094–1101, 2013. View at Publisher · View at Google Scholar · View at Scopus
  6. L. H. Zhu, K. L. Zhao, X. L. Chen, and J. X. Xu, “Impact of weaning and an antioxidant blend on intestinal barrier function and antioxidant status in pigs,” Journal of Animal Science, vol. 90, no. 8, pp. 2581–2589, 2012. View at Publisher · View at Google Scholar · View at Scopus
  7. L. Zhu, X. Cai, Q. Guo, X. Chen, S. Zhu, and J. Xu, “Effect of N-acetyl cysteine on enterocyte apoptosis and intracellular signalling pathways' response to oxidative stress in weaned piglets,” British Journal of Nutrition, vol. 110, no. 11, pp. 1938–1947, 2013. View at Publisher · View at Google Scholar · View at Scopus
  8. E. Seki and B. Schnabl, “Role of innate immunity and the microbiota in liver fibrosis: crosstalk between the liver and gut,” The Journal of Physiology, vol. 590, no. 3, pp. 447–458, 2012. View at Publisher · View at Google Scholar · View at Scopus
  9. G. K. Michalopoulos, “Liver regeneration,” Journal of Cellular Physiology, vol. 213, no. 2, pp. 286–300, 2007. View at Publisher · View at Google Scholar · View at Scopus
  10. Y. Ying, J. Yun, W. Guoyao, S. Kaiji, D. Zhaolai, and W. Zhenlong, “Dietary l-methionine restriction decreases oxidative stress in porcine liver mitochondria,” Experimental Gerontology, vol. 65, pp. 35–41, 2015. View at Publisher · View at Google Scholar · View at Scopus
  11. J. F. Turrens, “Mitochondrial formation of reactive oxygen species,” The Journal of Physiology, vol. 552, no. 2, pp. 335–344, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. H. Assaad, K. Yao, C. D. Tekwe et al., “Analysis of energy expenditure in diet-induced obese rats,” Frontiers in Bioscience, vol. 19, pp. 967–985, 2014. View at Google Scholar
  13. L. Zhao, The nutritional regulation of endoplasmic reticulum stress induced by early weaning stress in liver of piglets [M.S. thesis], 2014.
  14. T. Wada and J. M. Penninger, “Mitogen-activated protein kinases in apoptosis regulation,” Oncogene, vol. 23, no. 16, pp. 2838–2849, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. D. E. Shifflett, S. L. Jones, A. J. Moeser, and A. T. Blikslager, “Mitogen-activated protein kinases regulate COX-2 and mucosal recovery in ischemic-injured porcine ileum,” American Journal of Physiology—Gastrointestinal and Liver Physiology, vol. 286, no. 6, pp. G906–G913, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. J. R. Pluske, D. J. Hampson, and I. H. Williams, “Factors influencing the structure and function of the small intestine in the weaned pig: a review,” Livestock Production Science, vol. 51, no. 1–3, pp. 215–236, 1997. View at Publisher · View at Google Scholar · View at Scopus
  17. A. Fernández-Sánchez, E. Madrigal-Santillán, M. Bautista et al., “Inflammation, oxidative stress, and obesity,” International Journal of Molecular Sciences, vol. 12, no. 5, pp. 3117–3132, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. D. Armstrong, Oxidative Stress in Applied Basic Research and Clinical Practice, 2010.
  19. E. Schulz, T. Jansen, P. Wenzel, A. Daiber, and T. Münzel, “Nitric oxide, tetrahydrobiopterin, oxidative stress, and endothelial dysfunction in hypertension,” Antioxidants & Redox Signaling, vol. 10, no. 6, pp. 1115–1126, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. C. C. Xu, S. F. Yang, L. H. Zhu et al., “Regulation of N-acetyl cysteine on gut redox status and major microbiota in weaned piglets,” Journal of Animal Science, vol. 92, no. 4, pp. 1504–1511, 2014. View at Publisher · View at Google Scholar · View at Scopus
  21. D. Del Rio, A. J. Stewart, and N. Pellegrini, “A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress,” Nutrition, Metabolism and Cardiovascular Diseases, vol. 15, no. 4, pp. 316–328, 2005. View at Publisher · View at Google Scholar · View at Scopus
  22. E. N. Frankel and W. E. Neff, “Formation of malonaldehyde from lipid oxidation products,” Biochimica et Biophysica Acta (BBA)—Lipids and Lipid Metabolism, vol. 754, no. 3, pp. 264–270, 1983. View at Publisher · View at Google Scholar · View at Scopus
  23. S. Kawanishi and Y. Hiraku, “Oxidative and nitrative DNA damage as biomarker for carcinogenesis with special reference to inflammation,” Antioxidants & Redox Signaling, vol. 8, no. 5-6, pp. 1047–1058, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. A. G. Georgakilas, “Oxidative stress, DNA damage and repair in carcinogenesis: have we established a connection?” Cancer Letters, vol. 327, no. 1-2, pp. 3–4, 2012. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Dizdaroglu, R. Olinski, J. H. Doroshow, and S. A. Akman, “Modification of DNA bases in chromatin of intact target human cells by activated human polymorphonuclear leukocytes,” Cancer Research, vol. 53, no. 6, pp. 1269–1272, 1993. View at Google Scholar · View at Scopus
  26. H. Zhang, K. J. Davies, and H. J. Forman, “Oxidative stress response and Nrf2 signaling in aging,” Free Radical Biology and Medicine, vol. 88, pp. 314–336, 2015. View at Publisher · View at Google Scholar
  27. J. Yin, M. M. Wu, H. Xiao et al., “Development of an antioxidant system after early weaning in piglets,” Journal of Animal Science, vol. 92, no. 2, pp. 612–619, 2014. View at Publisher · View at Google Scholar · View at Scopus
  28. G. J. Burton and E. Jauniaux, “Oxidative stress,” Best Practice & Research: Clinical Obstetrics & Gynaecology, vol. 25, no. 3, pp. 287–299, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. S. J. Riedl and Y. Shi, “Molecular mechanisms of caspase regulation during apoptosis,” Nature Reviews Molecular Cell Biology, vol. 5, no. 11, pp. 897–907, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. J. C. Reed, “Bcl-2 and the regulation of programmed cell death,” The Journal of Cell Biology, vol. 124, no. 1, pp. 1–6, 1994. View at Publisher · View at Google Scholar
  31. I. Budihardjo, H. Oliver, M. Lutter, X. Luo, and X. Wang, “Biochemical pathways of caspase activation during apoptosis,” Annual Review of Cell and Developmental Biology, vol. 15, no. 1, pp. 269–290, 1999. View at Publisher · View at Google Scholar · View at Scopus
  32. S. Elmore, “Apoptosis: a review of programmed cell death,” Toxicologic Pathology, vol. 35, no. 4, pp. 495–516, 2007. View at Publisher · View at Google Scholar · View at Scopus
  33. M. Raisova, A. M. Hossini, J. Eberle et al., “The Bax/Bcl-2 ratio determines the susceptibility of human melanoma cells to CD95/Fas-mediated apoptosis,” Journal of Investigative Dermatology, vol. 117, no. 2, pp. 333–340, 2001. View at Publisher · View at Google Scholar · View at Scopus
  34. B. San-Miguel, M. Alvarez, J. M. Culebras, J. González-Gallego, and M. J. Tuñón, “N-acetyl-cysteine protects liver from apoptotic death in an animal model of fulminant hepatic failure,” Apoptosis, vol. 11, no. 11, pp. 1945–1957, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. A. R. Knudsen, K. J. Andersen, S. Hamilton-Dutoit, J. R. Nyengaard, and F. V. Mortensen, “Correlation between liver cell necrosis and circulating alanine aminotransferase after ischaemia/reperfusion injuries in the rat liver,” International Journal of Experimental Pathology, vol. 97, no. 2, pp. 133–138, 2016. View at Publisher · View at Google Scholar
  36. M. A. Hyder, M. Hasan, and A. H. Mohieldein, “Comparative levels of ALT, AST, ALP and GGT in liver associated diseases,” European Journal of Experimental Biology, vol. 3, no. 2, pp. 280–284, 2013. View at Google Scholar
  37. M.-J. Kang and J.-I. Kim, “Protective effect of Hedyotis diffusa on lipopolysaccharide (LPS)-induced liver damage,” The FASEB Journal, vol. 27, no. 1, supplement, p. 1155.5, 2013. View at Google Scholar
  38. J. S. Campbell, G. M. Argast, S. Y. Yuen, B. Hayes, and N. Fausto, “Inactivation of p38 MAPK during liver regeneration,” The International Journal of Biochemistry & Cell Biology, vol. 43, no. 2, pp. 180–188, 2011. View at Publisher · View at Google Scholar · View at Scopus
  39. J. A. McCubrey, M. M. LaHair, and R. A. Franklin, “Reactive oxygen species-induced activation of the MAP kinase signaling pathways,” Antioxidants & Redox Signaling, vol. 8, no. 9-10, pp. 1775–1789, 2006. View at Publisher · View at Google Scholar · View at Scopus
  40. S.-F. Wang, J.-C. Yen, P.-H. Yin, C.-W. Chi, and H.-C. Lee, “Involvement of oxidative stress-activated JNK signaling in the methamphetamine-induced cell death of human SH-SY5Y cells,” Toxicology, vol. 246, no. 2-3, pp. 234–241, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. A. Van Laethem, S. Van Kelst, S. Lippens et al., “Activation of p38 MAPK is required for Bax translocation to mitochondria, cytochrome c release and apoptosis induced by UVB irradiation in human keratinocytes,” The FASEB Journal, vol. 18, no. 15, pp. 1946–1948, 2004. View at Publisher · View at Google Scholar · View at Scopus