Molecular & Cellular Toxicology

The Korean Society of Toxicogenomics and Toxicoproteomics (대한독성유전 단백체학회)
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Genome Wide Expression Profile of Asiasarum sieboldi in LPS-stimulated BV-2 Microglial Cells

  • Sohn, Sung-Hwa (Department of Physiology, College of Oriental Medicine, KyungHee University) ;
  • Ko, Eun-Jung (Department of Physiology, College of Oriental Medicine, KyungHee University) ;
  • Kim, Yang-Seok (Department of Physiology, College of Oriental Medicine, KyungHee University) ;
  • Shin, Min-Kyu (Department of Physiology, College of Oriental Medicine, KyungHee University) ;
  • Hong, Moo-Chang (Department of Physiology, College of Oriental Medicine, KyungHee University) ;
  • Bae, Hyun-Su (Department of Physiology, College of Oriental Medicine, KyungHee University)
  • Published : 2008.09.30
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Abstract

Recent studies suggest that activated microglial cells play an essential role in the inflammatory responses and neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease. This study was conducted to evaluate the protective mechanisms of Asiasarum sieboldi (AS) on LPS-induced activation of BV-2 microglial cells. The effects of AS on gene expression profiles in activated BV-2 microglial cells were evaluated using microarray analysis. BV-2 microglial cells were cultured in a 100 mm dish ($1{\times}10^7$/mL) for 24 h and then pretreated with 1 ${\mu}g$/mL AS or left untreated for 30 min. Next, 1 ${\mu}g$/mL LPS was added to the samples and the cells were reincubated at $37^{\circ}C$ for 30 min and 1 hr. The gene expression profiles of the BV-2 microglial cells varied depending on the AS. The microarray analysis revealed that MAPK signaling pathway-related genes were downregulated in AS-treated BV-2 microglial cells. AS can affect the neuroinflammatory-related pathway such as MAPK signaling pathway in activated BV-2 microglial cells.

Keywords

References

  1. Wang, P., Rothwell, N. J., Pinteaux, E. & Brough, D. Neuronal injury induces the release of pro-interleukin- 1beta from activated microglia in vitro. Brain Res (2008). (in press)
  2. Kim, W. K. et al. A new anti-inflammatory agent KL -1037 represses proinflammatory cytokine and inducible nitric oxide synthase (iNOS) gene expression in activated microglia. Neuropharmacology 47:243-252 (2004) https://doi.org/10.1016/j.neuropharm.2004.03.019
  3. Nagai, A. et al. Immortalized human microglial cell line: phenotypic expression. J Neurosci Res 81:342-348 (2005) https://doi.org/10.1002/jnr.20478
  4. Woo, M. S. et al. Selective modulation of lipopolysaccharide- stimulated cytokine expression and mitogen- activated protein kinase pathways by dibutyrylcAMP in BV2 microglial cells. Brain Res Mol Brain Res 113:86-96 (2003) https://doi.org/10.1016/S0169-328X(03)00095-0
  5. Seo, W. G. et al. Inhibitory effect of ethyl acetate fraction from Cudrania tricuspidata on the expression of nitric oxide synthase gene in RAW 264.7 macrophages stimulated with interferon-gamma and lipopolysaccharide. Gen Pharmacol 35:21-28 (2000) https://doi.org/10.1016/S0306-3623(01)00086-6
  6. Kim, Y. J. et al. Neuroprotective effects of human mesenchymal stem cells on dopaminergic neurons through anti-inflammatory action. Glia (2008). (in press)
  7. Reynolds, A. D. et al. Nitrated Alpha-synuclein and microglial neuroregulatory activities. J Neuroimmune Pharmacol (2008). (in press)
  8. Skaper, S. D. The Brain as a target for inflammatory processes and neuroprotective strategies. Ann N Y Acad Sci 1122:23-34 (2007) https://doi.org/10.1196/annals.1403.002
  9. Hou, R. C., Chen, H. L., Tzen, J. T. & Jeng, K. C. Effect of sesame antioxidants on LPS-induced NO production by BV2 microglial cells. Neuroreport 14: 1815-1819 (2003) https://doi.org/10.1097/00001756-200310060-00011
  10. Hashimoto, K. et al. Studies on anti-allergic components in the roots of Asiasarum sieboldi. Planta Med 60:124-127 (1994) https://doi.org/10.1055/s-2006-959432
  11. Lamar, J. M., Iyer, V. & DiPersio, C. M. Integrin alpha3beta1 potentiates TGFbeta-mediated induction of MMP-9 in immortalized keratinocytes. J Invest Dermatol 128:575-586 (2008) https://doi.org/10.1038/sj.jid.5701042
  12. Raines, K. W. et al. Nitric oxide inhibition of ERK1/2 activity in cells expressing neuronal nitric-oxide synthase. J Biol Chem 279:3933-3940 (2004) https://doi.org/10.1074/jbc.M304813200
  13. Sim, S. et al. NADPH oxidase-derived reactive oxygen species-mediated activation of ERK1/2 is required for apoptosis of human neutrophils induced by Entamoeba histolytica. J Immunol 174:4279-4288 (2005) https://doi.org/10.4049/jimmunol.174.7.4279
  14. Akundi, R. S. et al. Signal transduction pathways regulating cyclooxygenase-2 in lipopolysaccharide-activated primary rat microglia. Glia 51:199-208 (2005) https://doi.org/10.1002/glia.20198
  15. Zaragoza, C. et al . Activation of the mitogen activated protein kinase extracellular signal-regulated kinase 1 and 2 by the nitric oxide-cGMP-cGMP-dependent protein kinase axis regulates the expression of matrix metalloproteinase 13 in vascular endothelial cells. Mol Pharmacol 62:927-935 (2002) https://doi.org/10.1124/mol.62.4.927
  16. Kimoto, M. et al. Purification, cDNA cloning and expression of human NG,NG-dimethylarginine dimethylaminohydrolase. Eur J Biochem 258:863-868 (1998) https://doi.org/10.1046/j.1432-1327.1998.2580863.x
  17. Leiper, J. et al. Disruption of methylarginine metabo-lism impairs vascular homeostasis. Nat Med 13:198-203 (2007) https://doi.org/10.1038/nm1543
  18. Lee, K. S., Jin, S. M., Kim, H. J. & Lee, Y. C. Matrix metalloproteinase inhibitor regulates inflammatory cell migration by reducing ICAM-1 and VCAM-1 expression in a murine model of toluene diisocyanateinduced asthma. J Allergy Clin Immunol 111:1278-1284 (2003) https://doi.org/10.1067/mai.2003.1501
  19. Sabatini, F. et al. Fibroblast-eosinophil interaction: modulation of adhesion molecules expression and chemokine release by human fetal lung fibroblasts in response to IL-4 and TNF-alpha. Immunol Lett 84:173-178 (2002) https://doi.org/10.1016/S0165-2478(02)00183-9
  20. Zhu, G. D. et al. Selective inhibition of ICAM-1 and E-selectin expression in human endothelial cells. 2. Aryl modifications of 4-(aryloxy)thieno[2,3-c]pyridines with fine-tuning at C-2 carbamides. J Med Chem 44:3469-3487 (2001) https://doi.org/10.1021/jm0101702
  21. Zerfaoui, M. et al. Nuclear translocation of p65 NFkappaB is sufficient for VCAM-1, but not ICAM-1, expression in TNF-stimulated smooth muscle cells: Differential requirement for PARP-1 expression and interaction. Cell Signal 20:186-194 (2008) https://doi.org/10.1016/j.cellsig.2007.10.007
  22. Heijink, I. H. et al. Down-regulation of E-cadherin in human bronchial epithelial cells leads to epidermal growth factor receptor-dependent Th2 cell-promoting activity. J Immunol 178:7678-7685 (2007) https://doi.org/10.4049/jimmunol.178.12.7678