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Evidence-Based Complementary and Alternative Medicine
Volume 2012, Article ID 368196, 9 pages
http://dx.doi.org/10.1155/2012/368196
Research Article

Effects of Bee Venom on Glutamate-Induced Toxicity in Neuronal and Glial Cells

Department of Standard Research, Korea Institute of Oriental Medicine, 483 Expo-ro, Yuseong-gu, Daejeon, 305-811, Republic of Korea

Received 21 January 2011; Revised 2 May 2011; Accepted 30 May 2011

Academic Editor: Cheorl-Ho Kim

Copyright © 2012 Sang Min Lee 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. S. P. Butcher and A. Hamberger, “In vivo studies on the extracellular, and veratrine-releasable, pools of endogenous amino acids in the rat striatum: effects of corticostriatal deafferentiation and kainic acid lesion,” Journal of Neurochemistry, vol. 48, no. 3, pp. 713–721, 1987. View at Google Scholar · View at Scopus
  2. K. Abe, Y. Abe, and H. Saito, “Agmatine induces glutamate release and cell death in cultured rat cerebellar granule neurons,” Brain Research, vol. 990, no. 1-2, pp. 165–171, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. T. Kihara, S. Shimohama, H. Sawada et al., “Protective effect of dopamine D2 agonists in cortical neurons via the phosphatidylinositol 3 kinase cascade,” Journal of Neuroscience Research, vol. 70, no. 3, pp. 274–282, 2002. View at Publisher · View at Google Scholar · View at Scopus
  4. M. E. Harris, Y. Wang, N. W. Pedigo, K. Hensley, D. A. Butterfield, and J. M. Carney, “Amyloid β peptide (25–35) inhibits Na+-dependent glutamate uptake in rat hippocampal astrocyte cultures,” Journal of Neurochemistry, vol. 67, no. 1, pp. 277–286, 1996. View at Google Scholar · View at Scopus
  5. T. Kihara, S. Shimohama, H. Sawada et al., “α7 nicotinic receptor transduces signals to phosphatidylinositol 3-Kinase to block A β-amyloid-induced neurotoxicity,” The Journal of Biological Chemistry, vol. 276, no. 17, pp. 13541–13546, 2001. View at Google Scholar
  6. Y. Jin, E. Z. Yan, Y. Fan et al., “Neuroprotection by sodium ferulate against glutamate-induced apoptosis is mediated by ERK and PI3 kinase pathways,” Acta Pharmacologica Sinica, vol. 28, no. 12, pp. 1881–1890, 2007. View at Publisher · View at Google Scholar · View at Scopus
  7. G. Gras, F. Porcheray, B. Samah, and C. Leone, “The glutamate-glutamine cycle as an inducible, protective face of macrophage activation,” Journal of Leukocyte Biology, vol. 80, no. 5, pp. 1067–1075, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. E. Andreadou, E. Kapaki, P. Kokotis et al., “Plasma glutamate and glycine levels in patients with amyotrophic lateral sclerosis,” In Vivo, vol. 22, no. 1, pp. 137–142, 2008. View at Google Scholar · View at Scopus
  9. A. Plaitakis and E. Constantakakis, “Altered metabolism of excitatory amino acids, N-acetyl-aspartate and N- acetyl-aspartyl-glutamate in amyotrophic lateral sclerosis,” Brain Research Bulletin, vol. 30, no. 3-4, pp. 381–386, 1993. View at Google Scholar · View at Scopus
  10. C. Ferrarese, G. Sala, R. Riva et al., “Decreased platelet glutamate uptake in patients with amyotrophic lateral sclerosis,” Neurology, vol. 56, no. 2, pp. 270–272, 2001. View at Google Scholar · View at Scopus
  11. J. D. Rothstein, L. J. Martin, and R. W. Kuncl, “Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis,” The New England Journal of Medicine, vol. 326, no. 22, pp. 1464–1468, 1992. View at Google Scholar · View at Scopus
  12. I. W. M. Bos, G. Hoogland, C. F. Meine Jansen et al., “Increased glutamine synthetase but normal EAAT2 expression in platelets of ALS patients,” Neurochemistry International, vol. 48, no. 4, pp. 306–311, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. S. J. Suh, K. S. Kim, M. J. Kim et al., “Effects of bee venom on protease activities and free radical damages in synovial fluid from type II collagen-induced rheumatoid arthritis rats,” Toxicology in Vitro, vol. 20, no. 8, pp. 1465–1471, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. W. R. Lariviere and R. Melzack, “The bee venom test: a new tonic-pain test,” Pain, vol. 66, no. 2-3, pp. 271–277, 1996. View at Publisher · View at Google Scholar · View at Scopus
  15. J. P. Hye, H. L. Seong, J. S. Dong et al., “Antiarthritic effect of bee venom: inhibition of inflammation mediator generation by suppression of NF-κB through interaction with the p50 subunit,” Arthritis and Rheumatism, vol. 50, no. 11, pp. 3504–3515, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. J. D. Lee, S. Y. Kim, T. W. Kim et al., “Anti-inflammatory effect of bee venom on type II collagen-induced arthritis,” American Journal of Chinese Medicine, vol. 32, no. 3, pp. 361–367, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. H. S. Jang, S. K. Kim, J. B. Han, H. J. Ahn, H. Bae, and B. I. Min, “Effects of bee venom on the pro-inflammatory responses in RAW264.7 macrophage cell line,” Journal of Ethnopharmacology, vol. 99, no. 1, pp. 157–160, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Han, K. Lee, J. Yeo et al., “Effect of honey bee venom on microglial cells nitric oxide and tumor necrosis factor-α production stimulated by LPS,” Journal of Ethnopharmacology, vol. 111, no. 1, pp. 176–181, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. E. J. Yang, J. H. Jiang, S. M. Lee et al., “Bee venom attenuates neuroinflammatory events and extends survival in amyotrophic lateral sclerosis models,” Journal of Neuroinflammation, vol. 7, article 69, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. N. Svoboda and H. H. Kerschbaum, “L-Glutamine-induced apoptosis in microglia is mediated by mitochondrial dysfunction,” European Journal of Neuroscience, vol. 30, no. 2, pp. 196–206, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Subramaniam, U. Zirrgiebel, O. Von Bohlen Und Halbach et al., “ERK activation promotes neuronal degeneration predominantly through plasma membrane damage and independently of caspase-3,” Journal of Cell Biology, vol. 165, no. 3, pp. 357–369, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Cagnol, E. Van Obberghen-Schilling, and J. C. Chambard, “Prolonged activation of ERK1,2 induces FADD-independent caspase 8 activation and cell death,” Apoptosis, vol. 11, no. 3, pp. 337–346, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. R. D. Almeida, B. J. Manadas, C. V. Melo et al., “Neuroprotection by BDNF against glutamate-induced apoptotic cell death is mediated by ERK and PI3-kinase pathways,” Cell Death and Differentiation, vol. 12, no. 10, pp. 1329–1343, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Z. Wu, A. M. Bodles, M. M. Porter, W. S. T. Griffin, A. S. Basile, and S. W. Barger, “Induction of serine racemase expression and D-serine release from microglia by amyloid β-peptide,” Journal of Neuroinflammation, vol. 1, article 2, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. B. J. Turner and K. Talbot, “Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS,” Progress in Neurobiology, vol. 85, no. 1, pp. 94–134, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. Y. Luo and D. B. DeFranco, “Opposing roles for ERK1/2 in neuronal oxidative toxicity: distinct mechanisms of ERK1/2 action at early versus late phases of oxidative stress,” The Journal of Biological Chemistry, vol. 281, no. 24, pp. 16436–16442, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. R. Seger and E. G. Krebs, “The MAPK signaling cascade,” The FASEB Journal, vol. 9, no. 9, pp. 726–735, 1995. View at Google Scholar · View at Scopus
  28. S. S. Grewal, R. D. York, and P. J. S. Stork, “Extracellular-signal-regulated kinase signalling in neurons,” Current Opinion in Neurobiology, vol. 9, no. 5, pp. 544–553, 1999. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Clerk and P. H. Sugden, “Untangling the web: specific signaling from PKC isoforms to MAPK cascades,” Circulation Research, vol. 89, no. 10, pp. 847–849, 2001. View at Google Scholar · View at Scopus
  30. B. C. Chen and W. W. Lin, “PKC- and ERK-dependent activation of IκB kinase by lipopolysaccharide in macrophages: enhancement by P2Y receptor-mediated CaMK activation,” British Journal of Pharmacology, vol. 134, no. 5, pp. 1055–1065, 2001. View at Google Scholar · View at Scopus
  31. I. Nadra, J. C. Mason, P. Philippidis et al., “Proinflammatory activation of macrophages by basic calcium phosphate crystals via protein kinase C and MAP kinase pathways: a vicious cycle of inflammation and arterial calcification?” Circulation Research, vol. 96, no. 12, pp. 1248–1256, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Dehvari, O. Isacsson, B. Winblad, A. Cedazo-Minguez, and R. F. Cowburn, “Presenilin regulates extracellular regulated kinase (Erk) activity by a protein kinase C alpha dependent mechanism,” Neuroscience Letters, vol. 436, no. 1, pp. 77–80, 2008. View at Publisher · View at Google Scholar · View at Scopus
  33. H. J. Park, H. J. Lee, M. S. Choi et al., “JNK pathway is involved in the inhibition of inflammatory target gene expression and NF-kappaB activation by melittin,” Journal of Inflammation, vol. 5, article 7, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. N. Boutahar, E. Reynaud, F. Lassabliere, and J. Borg, “Timing differences of signaling response in neuron cultures activated by glutamate analogue or free radicals,” Brain Research, vol. 1191, pp. 20–29, 2008. View at Publisher · View at Google Scholar · View at Scopus