Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2017, Article ID 9718615, 6 pages
https://doi.org/10.1155/2017/9718615
Research Article

The Role of Oxidative Stress in Decreased Acetylcholinesterase Activity at the Neuromuscular Junction of the Diaphragm during Sepsis

1Department of Anesthesiology, Shanghai General Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200080, China
2Department of Anesthesiology, The Ninth People’s Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China

Correspondence should be addressed to Shi-tong Li; moc.oohay@sgnotihsil

Received 13 July 2017; Accepted 17 October 2017; Published 5 November 2017

Academic Editor: Paola Venditti

Copyright © 2017 Hua Liu 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. Singer, C. S. Deutschman, and C. W. Seymour, “The third international consensus definitions for sepsis and septic shock (sepsis-3),” JAMA, vol. 315, no. 8, pp. 801–810, 2016. View at Publisher · View at Google Scholar · View at Scopus
  2. A. Demoule, B. Jung, H. Prodanovic et al., “Diaphragm dysfunction on admission to ICU: prevalence, risk factors and prognostic impact - a prospective study,” American Journal of Respiratory and Critical Care Medicine, vol. 88, no. 2, pp. 213–219, 2013. View at Publisher · View at Google Scholar · View at Scopus
  3. J. Wu, T. Jin, H. Wang, and S.-T. Li, “Sepsis strengthens antagonistic actions of neostigmine on rocuronium in a rat model of cecal ligation and puncture,” Chinese Medical Journal, vol. 129, no. 12, pp. 1477–1482, 2016. View at Publisher · View at Google Scholar · View at Scopus
  4. R. C. Bone, C. J. Grodzin, and R. A. Balk, “Sepsis: a new hypothesis for pathogenesis of the disease process,” Chest, vol. 112, no. 1, pp. 235–243, 1997. View at Publisher · View at Google Scholar
  5. R. C. Bone, R. A. Balk, F. B. Cerra, R. P. Dellinger, A. M. Fein, and W. A. Knaus, “Definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis,” Chest, vol. 101, no. 6, pp. 1644–1655, 1992. View at Publisher · View at Google Scholar
  6. D. Rittirsch, M. A. Flierl, and P. A. Ward, “Harmful molecular mechanisms in sepsis,” Nature Reviews Immunology, vol. 8, no. 10, pp. 776–787, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. J. Duran-Bedolla, M. A. Montes de Oca-Sandoval, and V. Saldaña-Navor, “Sepsis, mitochondrial failure and multiple organ dysfunction,” Clinical and Investigative Medicine, vol. 37, no. 2, pp. E58–E69, 2014. View at Publisher · View at Google Scholar
  8. M. P. Fink, “Role of reactive oxygen and nitrogen species in acute respiratory distress syndrome,” Current Opinion in Critical Care, vol. 8, no. 1, pp. 6–11, 2002. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Bayir, “Reactive oxygen species,” Critical Care Medicine, vol. 33, no. 12, pp. S498–S501, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. C. A. Prauchner, “Oxidative stress in sepsis: pathophysiological implications justifying antioxidant co-therapy,” Burns, vol. 43, no. 3, pp. 471–485, 2017. View at Publisher · View at Google Scholar
  11. B. W. O’Malley, C. E. Mengel, and W. D. Meriwether, “Inhibition of erythrocyte acetylcholinesterase by peroxides,” Biochemistry, vol. 5, no. 1, pp. 40–44, 1966. View at Publisher · View at Google Scholar
  12. D. IuV, “Hydrogen peroxide inhibits acetylcholinesterase of myometrium sarcolemma,” UkrBiokhim Zh, vol. 81, no. 4, pp. 32–38, 2009. View at Google Scholar
  13. K. U. Schallreuter, S. M. Elwary, and N. C. Gibbons, “Activation/deactivation of acetylcholinesterase by H2O2: more evidence for oxidative stress in vitiligo,” Biochemical and Biophysical Research, vol. 315, no. 2, pp. 502–508, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. K. U. Schallreuter and S. Elwary, “Hydrogen peroxide regulates the cholinergic signal in a concentration dependent manner,” Life Sciences, vol. 80, no. 24-25, pp. 2221–2226, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. S. Tsakiris, P. Angelogianni, K. H. Schulpis, and J. C. Stavridis, “Protective effect of L phenylalanine on rat brain acetylcholinesterase inhibition induced by free radicals,” Clinical Biochemistry, vol. 33, no. 2, pp. 103–106, 2000. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Méndez-Garrido, M. Hernández-Rodríguez, R. Zamorano-Ulloa et al., “In vitro effect of H2O2, some transition metals and hydroxyl radical produced via Fenton and Fenton-like reactions, on the catalytic activity of AChE and the hydrolysis of ACh,” Neurochemical Research, vol. 39, no. 11, pp. 2093–2104, 2014. View at Publisher · View at Google Scholar · View at Scopus
  17. G. J. den Hartog, E. Vegt, and W. J. van der Vijgh, “Hypochlorous acid is a potent inhibitor of acetylcholinesterase,” Toxicology and Applied Pharmacology, vol. 181, no. 3, pp. 228–232, 2002. View at Publisher · View at Google Scholar · View at Scopus
  18. D. Rittirsch, M. S. Huber-Lang, M. A. Flierl, and P. AWard, “Immunodesign of experimental sepsis by cecal ligation and puncture,” Nature Protocols, vol. 4, no. 1, pp. 31–36, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Ruiz, F. Vardon-Bounes, V. Merlet-Dupuy, J.-M. Conil, M. Buléon, and O. Fourcade, “Sepsis modeling in mice: ligation length is a major severity factor in cecal ligation and puncture,” Intensive Care Medicine Experimental, vol. 4, no. 1, p. 22, 2016. View at Publisher · View at Google Scholar
  20. M. J. Karnovsky and L. Roots, “A “direct-coloring” thiocholine method for cholinesterases,” The Journal of Histochemistry and Cytochemistry, vol. 12, no. 3, pp. 219–221, 1964. View at Publisher · View at Google Scholar
  21. S. Ma, S. Xu, B. Liu et al., “Long-term treatment of l-3-n-butylphthalide attenuated neurodegenerative changes in aged rats,” Naunyn-Schmiedeberg's Archives of Pharmacology, vol. 379, no. 6, pp. 565–574, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. H. H. Draper and M. Hadley, “Malondialdehyde determination as index of lipid peroxidation,” Methods in Enzymology, vol. 186, pp. 421–431, 1990. View at Google Scholar
  23. R. L. Levine, D. Garland, and C. N. Oliver, “Determination of carbonyl content in oxidatively modified proteins,” Methods in Enzymology, vol. 186, pp. 464–478, 1990. View at Google Scholar
  24. D. E. Taylor, A. J. Ghio, and C. A. Piantadosi, “Reactive oxygen species produced by liver mitochondria of rats in sepsis,” Archives of Biochemistry and Biophysics, vol. 316, no. 1, pp. 70–76, 1995. View at Publisher · View at Google Scholar · View at Scopus
  25. Y. V. Lerman and M. Kim, “Neutrophil migration under normal and sepsis conditions,” Cardiovascular & Hematological Disorders Drug Targets, vol. 15, no. 1, pp. 19–28, 2015. View at Publisher · View at Google Scholar · View at Scopus
  26. J. P. Gaut, G. C. Yeh, and H. D. Tran, “Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 21, pp. 11961–11966, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. C. Ritter, M. E. Andrades, A. Reinke, S. Menna-Barreto, J. C. Moreira, and F. Dal-Pizzol, “Treatment with N-acetylcysteine plus deferoxamine protects rats against oxidative stress and improves survival in sepsis,” Critical Care Medicine, vol. 32, no. 2, pp. 342–349, 2004. View at Publisher · View at Google Scholar · View at Scopus
  28. C. Ritter, M. Andrades, and M. L. Frota Júnior, “Oxidative parameters and mortality in sepsis induced by cecal ligation and perforation,” Intensive Care Medicine, vol. 29, pp. 1782–1789, 2003. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Masuda, D. L. Longo, and Y. Kobayashi, “Induction of mitochondrial manganese superoxide dismutase by interleukin 1,” The FASEB Journal, vol. 2, pp. 3087–3091, 1988. View at Google Scholar
  30. G. A. Visner, W. C. Douglas, J. M. Wilson, I. A. Burr, and H. S. Nick, “Regulation of manganese superoxide dismutase by lipopolysaccaride, interleukin-1, and tumor necrosis factor,” The Journal of Biological Chemistry, vol. 265, pp. 2856–2286, 1990. View at Google Scholar
  31. T. G. Gantchev and J. E. van Lier, “Catalase inactivation following photosensitization with tetrasulfonated metallophthalocyanines,” Photochemistry and Photobiology, vol. 62, pp. 123–134, 1995. View at Publisher · View at Google Scholar · View at Scopus
  32. C. A. Prauchner, S. Prestes Ade, and J. B. da Rocha, “Effects of diphenyl diselenide on oxidative stress induced by sepsis in rats,” Pathology, Research and Practice, vol. 207, pp. 554–558, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. M. Faith, A. Sukumaran, A. B. Pulimood, and M. Jacob, “How reliable an indicator of inflammation is myeloperoxidase activity?” Clinica Chimica Acta, vol. 396, pp. 23–25, 2008. View at Publisher · View at Google Scholar · View at Scopus