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Evidence-Based Complementary and Alternative Medicine
Volume 2016 (2016), Article ID 7481323, 7 pages
http://dx.doi.org/10.1155/2016/7481323
Research Article

Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor

1Department of Pharmacy, School of Medicine, Hunan Normal University, Changsha, Hunan 410013, China
2The First Affiliated Hospital, Hunan Normal University, 61 West Jiefang Road, Changsha, Hunan 410005, China

Received 29 May 2016; Revised 9 July 2016; Accepted 13 July 2016

Academic Editor: Hyunsu Bae

Copyright © 2016 Yong-Chao Xie 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. Z. Li, C. Mu, B. Wang, and J. Jin, “Graveoline analogs exhibiting selective acetylcholinesterase inhibitory activity as potential lead compounds for the treatment of Alzheimer's disease,” Molecules, vol. 21, no. 2, p. 132, 2016. View at Publisher · View at Google Scholar
  2. T. Zhou, G. Zu, X. Zhang et al., “Neuroprotective effects of ginsenoside Rg1 through the Wnt/β-catenin signaling pathway in both in vivo and in vitro models of Parkinson's disease,” Neuropharmacology, vol. 101, no. 5, pp. 480–489, 2016. View at Publisher · View at Google Scholar · View at Scopus
  3. B. DaRocha-Souto, M. Coma, B. G. Pérez-Nievas et al., “Activation of glycogen synthase kinase-3 beta mediates β-amyloid induced neuritic damage in Alzheimer's disease,” Neurobiology of Disease, vol. 45, no. 1, pp. 425–437, 2012. View at Publisher · View at Google Scholar · View at Scopus
  4. W. Wang, Y. Yang, C. Ying et al., “Inhibition of glycogen synthase kinase-3β protects dopaminergic neurons from MPTP toxicity,” Neuropharmacology, vol. 52, no. 8, pp. 1678–1684, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Du, Y. Wei, L. Liu et al., “A kinesin signaling complex mediates the ability of GSK-3β to affect mood-associated behaviors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 25, pp. 11573–11578, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. T. D. King, G. N. Bijur, and R. S. Jope, “Caspase-3 activation induced by inhibition of mitochondrial complex I is facilitated by glycogen synthase kinase-3β and attenuated by lithium,” Brain Research, vol. 919, no. 1, pp. 106–114, 2001. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Jing, Q. Jin, J. Wu, and X.-J. Zhang, “GSK3β mediates the induced expression of synaptic acetylcholinesterase during apoptosis,” Journal of Neurochemistry, vol. 104, no. 2, pp. 409–419, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. T. S. Anekonda and P. H. Reddy, “Can herbs provide a new generation of drugs for treating Alzheimer's disease?” Brain Research Reviews, vol. 50, no. 2, pp. 361–376, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Pu, Z. Wang, Q. Huang et al., “Biatractylolide of guinea pigs in vitro atrial muscle function,” Chinese Pharmacological Bulletin, vol. 16, no. 5, pp. 60–62, 2000. View at Google Scholar
  10. X. Feng, Z. L. Wang, Y.-C. Lin et al., “Biatractylolide's effect on Aβ1–40-induced dementia model rats,” Chinese Pharmacological Bulletin, vol. 25, no. 7, pp. 949–951, 2009. View at Google Scholar
  11. G. L. Ellman, K. D. Courtney, V. Andres Jr., and R. M. Featherstone, “A new and rapid colorimetric determination of acetylcholinesterase activity,” Biochemical Pharmacology, vol. 7, no. 2, pp. 88–95, 1961. View at Publisher · View at Google Scholar · View at Scopus
  12. K. Hostettmann, A. Borloz, A. Urbain, and A. Marston, “Natural product inhibitors of acetylcholinesterase,” Current Organic Chemistry, vol. 10, no. 8, pp. 825–847, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. Z.-D. Yang, X. Zhang, J. Du et al., “An aporphine alkaloid from Nelumbo nucifera as an acetylcholinesterase inhibitor and the primary investigation for structure-activity correlations,” Natural Product Research, vol. 26, no. 5, pp. 387–392, 2012. View at Publisher · View at Google Scholar · View at Scopus
  14. H. A. Jung, B.-S. Min, T. Yokozawa, J.-H. Lee, Y. S. Kim, and J. S. Choi, “Anti-Alzheimer and antioxidant activities of coptidis rhizoma alkaloids,” Biological and Pharmaceutical Bulletin, vol. 32, no. 8, pp. 1433–1438, 2009. View at Publisher · View at Google Scholar · View at Scopus
  15. M. T. H. Khan, I. Orhan, F. S. Şenol et al., “Cholinesterase inhibitory activities of some flavonoid derivatives and chosen xanthone and their molecular docking studies,” Chemico-Biological Interactions, vol. 181, no. 3, pp. 383–389, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. V. Sepsova, J. Z. Karasova, J. Korabecny et al., “Oximes: inhibitors of human recombinant acetylcholinesterase. A structure-activity relationship (SAR) study,” International Journal of Molecular Sciences, vol. 14, no. 8, pp. 16882–16900, 2013. View at Publisher · View at Google Scholar · View at Scopus
  17. D. Barak, C. Kronman, A. Ordentlich et al., “Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core,” Journal of Biological Chemistry, vol. 269, no. 9, pp. 6296–6305, 1994. View at Google Scholar · View at Scopus
  18. L. Berg, C. D. Da Andersson, E. Artursson et al., “Targeting acetylcholinesterase: identification of chemical leads by high throughput screening, structure determination and molecular modeling,” PLoS ONE, vol. 6, no. 11, Article ID e26039, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Zimmermann, “Neuronal AChE splice variants and their non-hydrolytic functions: redefining a target of AChE inhibitors?” British Journal of Pharmacology, vol. 170, no. 5, pp. 953–967, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. J. E. Cohen, G. Zimmerman, N. Melamed-Book, A. Friedman, A. Dori, and H. Soreq, “Transgenic inactivation of acetylcholinesterase impairs homeostasis in mouse hippocampal granule cells,” Hippocampus, vol. 18, no. 2, pp. 182–192, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. C. B. Moore and I. C. Allen, “Primary ear fibroblast derivation from mice,” Methods in Molecular Biology, vol. 1031, no. 5, pp. 65–70, 2013. View at Publisher · View at Google Scholar · View at Scopus
  22. Y. Lei, “Generation and culture of mouse embryonic fibroblasts,” Methods in Molecular Biology, vol. 1031, no. 15, pp. 59–64, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. D. Toiber, A. Berson, D. Greenberg, N. Melamed-Book, S. Diamant, and H. Soreq, “N-acetylcholinesterase-induced apoptosis in Alzheimer's disease,” PLoS ONE, vol. 3, no. 9, Article ID e3108, 2008. View at Publisher · View at Google Scholar · View at Scopus
  24. I. Orhan, B. Şener, M. I. Choudhary, and A. Khalid, “Acetylcholinesterase and butyrylcholinesterase inhibitory activity of some Turkish medicinal plants,” Journal of Ethnopharmacology, vol. 91, no. 1, pp. 57–60, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Sternfeld, G.-L. Ming, H.-J. Song et al., “Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini,” The Journal of Neuroscience, vol. 18, no. 4, pp. 1240–1249, 1998. View at Google Scholar · View at Scopus
  26. X. Tang, J.-S. Gao, Y.-J. Guan et al., “Acetylation-dependent signal transduction for type I interferon receptor,” Cell, vol. 131, no. 1, pp. 93–105, 2007. View at Publisher · View at Google Scholar · View at Scopus