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Evidence-Based Complementary and Alternative Medicine
Volume 2013, Article ID 163057, 8 pages
http://dx.doi.org/10.1155/2013/163057
Research Article

Isorhynchophylline Protects PC12 Cells Against Beta-Amyloid-Induced Apoptosis via PI3K/Akt Signaling Pathway

1School of Chinese Medicine, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong
2College of Chinese Medicines, Guangzhou University of Chinese Medicine, 510006 Guangzhou, China

Received 3 June 2013; Revised 12 September 2013; Accepted 23 September 2013

Academic Editor: Karl Wah-Keung Tsim

Copyright © 2013 Yan-Fang Xian 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. R. Brookmeyer, E. Johnson, K. Ziegler-Graham, and H. M. Arrighi, “Forecasting the global burden of Alzheimer's disease,” Alzheimer's and Dementia, vol. 3, no. 3, pp. 186–191, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. H. L. Weiner, C. A. Lemere, R. Maron et al., “Nasal administration of amyloid-beta peptide decreases cerebral amyloid burden in a mouse model of Alzheimer’s disease,” Annals of Neurology, vol. 48, no. 4, pp. 567–579, 2000. View at Google Scholar
  3. M. Bothwell and E. Giniger, “Alzheimer's disease: neurodevelopment converges with neurodegeneration,” Cell, vol. 102, no. 3, pp. 271–273, 2000. View at Google Scholar · View at Scopus
  4. D. J. Selkoe, “Alzheimer's disease: genotypes, phenotype, and treatments,” Science, vol. 275, no. 5300, pp. 630–631, 1997. View at Publisher · View at Google Scholar · View at Scopus
  5. E. Hellström-Lindahl, M. Viitanen, and A. Marutle, “Comparison of Aβ levels in the brain of familial and sporadic Alzheimer's disease,” Neurochemistry International, vol. 55, no. 4, pp. 243–252, 2009. View at Publisher · View at Google Scholar · View at Scopus
  6. M. R. Basha, M. Murali, H. K. Siddiqi et al., “Lead (Pb) exposure and its effect on APP proteolysis and Aβ aggregation,” FASEB Journal, vol. 19, no. 14, pp. 2083–2084, 2005. View at Publisher · View at Google Scholar · View at Scopus
  7. Y. Hashimoto, T. Niikura, T. Chiba et al., “The cytoplasmic domain of Alzheimer's amyloid-β protein precursor causes sustained apoptosis signal-regulating kinase 1/c-Jun NH 2-terminal kinase-mediated neurotoxic signal via dimerization,” Journal of Pharmacology and Experimental Therapeutics, vol. 306, no. 3, pp. 889–902, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. D. L. McPhie, R. Coopersmith, A. Hines-Peralta et al., “DNA synthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3,” Journal of Neuroscience, vol. 23, no. 17, pp. 6914–6927, 2003. View at Google Scholar · View at Scopus
  9. T. H. Kang, Y. Murakami, H. Takayama et al., “Protective effect of rhynchophylline and isorhynchophylline on in vitro ischemia-induced neuronal damage in the hippocampus: putative neurotransmitter receptors involved in their action,” Life Sciences, vol. 76, no. 3, pp. 331–343, 2004. View at Publisher · View at Google Scholar · View at Scopus
  10. D. Yuan, B. Ma, J. Y. Yang et al., “Anti-inflammatory effects of rhynchophylline and isorhynchophylline in mouse N9 microglial cells and the molecular mechanism,” International Immunopharmacology, vol. 9, no. 13-14, pp. 1549–1554, 2009. View at Publisher · View at Google Scholar · View at Scopus
  11. Y. Shimada, H. Goto, T. Itoh et al., “Evaluation of the protective effects of alkaloids isolated from the hooks and stems of Uncaria sinensis on glutamate-induced neuronal death in cultured cerebellar granule cells from rats,” Journal of Pharmacy and Pharmacology, vol. 51, no. 6, pp. 715–722, 1999. View at Publisher · View at Google Scholar · View at Scopus
  12. H. Kanatani, H. Kohda, and K. Yamasaki, “The active principles of the branchlet and hood of Uncaria sinensis Oliv. examined with a 5-hydroxytryptamine receptor binding assay,” Journal of Pharmacy and Pharmacology, vol. 37, no. 6, pp. 401–404, 1985. View at Google Scholar · View at Scopus
  13. K. Matsumoto, R. Morishige, Y. Murakami et al., “Suppressive effects of isorhynchophylline on 5-HT2A receptor function in the brain: behavioural and electrophysiological studies,” European Journal of Pharmacology, vol. 517, no. 3, pp. 191–199, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. F. Xian, Z. X. Lin, Q. Q. Mao, S. P. Ip, Z. R. Su, and X. P. Lai, “Protective effect of isorhynchophylline against β-amyloid-induced neurotoxicity in PC12 cells,” Cellular and Molecular Neurobiology, vol. 32, no. 3, pp. 353–360, 2012. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. F. Xian, Z. X. Lin, Q. Q. Mao, M. Zhao, Z. Hu, and S. P. Ip, “Bioassay-guided isolation of neuroprotective compounds from uncaria rhynchophylla against beta-amyloid-induced neurotoxicity in PC12 cells,” Evidence-Based Complementary and Alternative Medicine, vol. 2012, Article ID 802625, 8 pages, 2012. View at Publisher · View at Google Scholar
  16. J. Haginiwa, S. Sakai, and N. Aimi, “Studies of plants containing indole alkaloids. (II). The alkaloids of Uncaria rhynchophylla Miq,” Yakugaku Zasshi, vol. 93, no. 4, pp. 448–452, 1973. View at Google Scholar · View at Scopus
  17. K. W. Zeng, H. Ko, H. O. Yang, and X. M. Wang, “Icariin attenuates β-amyloid-induced neurotoxicity by inhibition of tau protein hyperphosphorylation in PC12 cells,” Neuropharmacology, vol. 59, no. 6, pp. 542–550, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. Z. Zhang, R. Zhao, J. Qi, S. Wen, Y. Tang, and D. Wang, “Inhibition of glycogen synthase kinase-3β by Angelica sinensis extract decreases β-amyloid-induced neurotoxicity and tau phosphorylation in cultured cortical neurons,” Journal of Neuroscience Research, vol. 89, no. 3, pp. 437–447, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. L. Sun, C. Guo, D. Liu et al., “Protective effects of bone morphogenetic protein 7 against amyloid-beta induced neurotoxicity in PC12 cells,” Neuroscience, vol. 184, pp. 151–163, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Pap and G. M. Cooper, “Role of glycogen synthase kinase-3 in the phosphatidylinositol 3- kinase/Akt cell survival pathway,” Journal of Biological Chemistry, vol. 273, no. 32, pp. 19929–19932, 1998. View at Publisher · View at Google Scholar · View at Scopus
  21. G. Alvarez, J. R. Muñoz-Montaño, J. Satrústegui, J. Avila, E. Bogónez, and J. Díaz-Nido, “Regulation of tau phosphorylation and protection against beta-amyloid-induced neurodegeneration by lithium. Possible implications for Alzheimer’s disease,” Bipolar Disorders, vol. 4, no. 3, pp. 153–165, 2002. View at Google Scholar
  22. F. Plattner, M. Angelo, and K. P. Giese, “The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation,” Journal of Biological Chemistry, vol. 281, no. 35, pp. 25457–25465, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. D. H. Geschwind and B. L. Miller, “Molecular approaches to cerebral laterality: development and neurodegeneration,” American Journal of Medical Genetics, vol. 101, no. 4, pp. 370–381, 2001. View at Google Scholar
  24. C. Tackenberg and R. Brandt, “Divergent pathways mediate spine alterations and cell death induced by amyloid-β, wild-type tau, and R406W tau,” Journal of Neuroscience, vol. 29, no. 46, pp. 14439–14450, 2009. View at Publisher · View at Google Scholar · View at Scopus
  25. J. J. Pei, E. Braak, H. Braak et al., “Distribution of active glycogen synthase kinase 3β (GSK-3β) in brains staged for Alzheimer disease neurofibrillary changes,” Journal of Neuropathology and Experimental Neurology, vol. 58, no. 9, pp. 1010–1019, 1999. View at Google Scholar · View at Scopus
  26. M. D. Kaytor and H. T. Orr, “The GSK3β signaling cascade and neurodegenerative disease,” Current Opinion in Neurobiology, vol. 12, no. 3, pp. 275–278, 2002. View at Publisher · View at Google Scholar · View at Scopus
  27. I. Tato, R. Bartrons, F. Ventura, and J. L. Rosa, “Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via PI3K/Akt signaling,” Journal of Biological Chemistry, vol. 286, no. 8, pp. 6128–6142, 2011. View at Publisher · View at Google Scholar · View at Scopus
  28. R. Zhao, Z. Zhang, Y. Song, D. Wang, J. Qi, and S. Wen, “Implication of phosphatidylinositol-3 kinase/Akt/glycogen synthase kinase-3β pathway in ginsenoside Rb1's attenuation of beta-amyloid-induced neurotoxicity and tau phosphorylation,” Journal of Ethnopharmacology, vol. 133, no. 3, pp. 1109–1116, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. L. Baki, J. Shioi, P. Wen et al., “PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations,” EMBO Journal, vol. 23, no. 13, pp. 2586–2596, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. S. F. Moore, R. W. Hunter, and I. Hers, “mTORC2 protein-mediated protein kinase B (Akt) serine 473 phosphorylation is not required for Akt1 activity in human platelets,” Journal of Biological Chemistry, vol. 286, no. 28, pp. 24553–24560, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. H. Koide, T. Asai, K. Furuya et al., “Inhibition of Akt (ser473) phosphorylation and rapamycin-resistant cell growth by knockdown of mammalian target of rapamycin with small interfering RNA in vascular endothelial growth factor receptor-1-targeting vector,” Biological and Pharmaceutical Bulletin, vol. 34, no. 5, pp. 602–608, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. J. M. Beaulieu, R. R. Gainetdinov, and M. G. Caron, “Akt/GSK3 signaling in the action of psychotropic drugs,” Annual Review of Pharmacology and Toxicology, vol. 49, pp. 327–347, 2009. View at Publisher · View at Google Scholar · View at Scopus
  33. C. A. Grimes and R. S. Jope, “The multifaceted roles of glycogen synthase kinase 3β in cellular signaling,” Progress in Neurobiology, vol. 65, no. 4, pp. 391–426, 2001. View at Publisher · View at Google Scholar · View at Scopus
  34. K. Du and M. Montminy, “CREB is a regulatory target for the protein kinase Akt/PKB,” Journal of Biological Chemistry, vol. 273, no. 49, pp. 32377–32379, 1998. View at Publisher · View at Google Scholar · View at Scopus
  35. T. R. Salas, S. A. Reddy, J. L. Clifford et al., “Alleviating the suppression of glycogen synthase kinase-3β by Akt leads to the phosphorylation of cAMP-response element-binding protein and its transactivation in intact cell nuclei,” Journal of Biological Chemistry, vol. 278, no. 42, pp. 41338–41346, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. D. W. Kim, J. H. Lee, S. K. Park et al., “Astrocytic expressions of phosphorylated Akt, GSK3β and CREB following an excitotoxic lesion in the mouse hippocampus,” Neurochemical Research, vol. 32, no. 9, pp. 1460–1468, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. L. Ji, E. Mochon, M. Arcinas, and L. M. Boxer, “CREB proteins function as positive regulators of the translocated bcl-2 allele in t(14;18) lymphomas,” Journal of Biological Chemistry, vol. 271, no. 37, pp. 22687–22691, 1996. View at Publisher · View at Google Scholar · View at Scopus
  38. Y. Takada-Takatori, T. Kume, M. Sugimoto, H. Katsuki, H. Sugimoto, and A. Akaike, “Acetylcholinesterase inhibitors used in treatment of Alzheimer's disease prevent glutamate neurotoxicity via nicotinic acetylcholine receptors and phosphatidylinositol 3-kinase cascade,” Neuropharmacology, vol. 51, no. 3, pp. 474–486, 2006. View at Publisher · View at Google Scholar · View at Scopus