Virologica Sinica

, Volume 25, Issue 6, pp 440–444

PrP 106-126 Altered PrP mRNA gene expression in mouse microglia BV-2 Cells

  • Yu Bai
  • Yu-rong Li
  • Gui-hua Wang
  • Xiang-mei Zhou
  • De-ming Zhao


Prion diseases are infectious and fatal neurodegenerative diseases. The pathogenic agent is an abnormal prion protein aggregate. Microglial activation in the centre nervous system is a characteristic feature of prion disease. In this study, we examined the effect of PrP 106–126 on PrP mRNA gene expression in Mouse microglia cells BV-2 by real-time quantitative PCR. PrP mRNA expression level was found to be significantly increased after 18 h exposure of BV-2 cells to PrP 106–126, with 3-fold increase after 18 h and 4.5-fold increase after 24 h and BV-2 cells proliferating occurred correspondingly. Our results provide the first in vitro evidence of the increase of PrP mRNA levels in microglial cells exposed to PrP 106–126, and indicate that microglial cells might play a critical role in prion pathogenesis.

Key words

Prion PrP106-126 PrP mRNA Mouse microglia BV-2 Cells 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Aguzzi A, Heikenwalder M. 2006. Pathogenesis of prion diseases: current status and future outlook. Nature, 4: 765–775.Google Scholar
  2. 2.
    Baker C A, Lu Z Y, Zaitsev I,et al. 1999. Microglial Activation Varies in Different Models of Creutzfeldt-Jakob Disease. J Virol, 73(6): 5089–5097.PubMedGoogle Scholar
  3. 3.
    Bai Y, Li Q, Yang J,et al. 2008. p75NTR activation of NF-κB is involved in PrP106-126-induced apoptosis in mouse neuroblastoma cells. Neuroscience Res, 662: 9–14.CrossRefGoogle Scholar
  4. 4.
    Barcikowska M, Liberski P P, Boellaard J W,et al. 1993. Microglia is a component of the prion protein amyloid plaque in the Gerstmann-Sträussler-Scheinker syndrome. Acta Neuropathol, 85: 623–627.CrossRefPubMedGoogle Scholar
  5. 5.
    Biieler H, Aguzzi A, Sailer A,et al. 1993. Mice Devoid of PrP Are Resistant to Scrapie. Cell, 73: 1339–1347.CrossRefGoogle Scholar
  6. 6.
    Brandenburg L-O, Koch T, Sievers J,et al. 2007. Internalization of PrP106-126 by the formyl-peptidereceptorlike- 1 in glial cells. J Neurochem, 101: 718–728.CrossRefPubMedGoogle Scholar
  7. 7.
    Brown D R, Schmidt B, Kretzschmar, H.A., 1996. Role of microglia and host protein in neurotoxicity of a prion protein fragment. Nature, 380: 345–347.CrossRefPubMedGoogle Scholar
  8. 8.
    Brown H R, Goller N L, Rudelli RD,et al. 1990. The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells. Acta Neuropathol, 80: 1–6.CrossRefPubMedGoogle Scholar
  9. 9.
    Combs C K, Johnson D E, Cannady S B,et al. 1999. Identification of Microglial Signal Transduction Pathways Mediating a Neurotoxic Response to Amyloidogenic Fragments of b-Amyloid and Prion Proteins. J Neuroscience, 19: 928–939.Google Scholar
  10. 10.
    Forloni G, Angeretti N, Chiesa R,et al. 1993. Neurotoxicity of a prion protein fragment. Nature, 362: 543–546.CrossRefPubMedGoogle Scholar
  11. 11.
    Giese A, Brown D R, Groschup M H,et al. 2006. Role of Microglia in Neuronal Cell Death in Prion Disease. Brain Pathol, 8(3): 449–457.CrossRefGoogle Scholar
  12. 12.
    Mchattie S J, Brown D R, Bird M M, 2004. Uptake of the prion protein fragment PrP106-126 in vitro. J Neurocytol, 28: 149–159.CrossRefGoogle Scholar
  13. 13.
    Moser M, Colello R J, Pott U,et al. 1995. Developmental Expression of the Prion Protein Gene in Glial Cells. Neuron, 14: 509–517.CrossRefPubMedGoogle Scholar
  14. 14.
    Muhleisen H, Gehrmann J, Meyermann R. 1995. Reactive microgIia in Creutzfeldt-Jakob disease. Neuropathol Appl Neurobiol, 21(6): 505–517.CrossRefPubMedGoogle Scholar
  15. 15.
    Sileia V, Fabrizia C, Venturini G,et al. 1999. Activation of microglial cells by PrP and β-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels. Brain Res, 8818: 168–170.CrossRefGoogle Scholar
  16. 16.
    Tagliavini F, Prelli F, Verga L,et al. 1993. Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. Proc Natl Acad Sci USA, 90: 9678–9682.CrossRefPubMedGoogle Scholar
  17. 17.
    Prusiner S B. 1997. Prion Diseases and the BSE Crisis. Science, 278: 245–251.CrossRefPubMedGoogle Scholar
  18. 18.
    Prusiner S B. 1998. Prions. Proc. Natl. Acad. Sci USA, 95: 13363–13383.CrossRefPubMedGoogle Scholar
  19. 19.
    Prusiner S B. 2001. Neurodegenerative Diseases and Prions. N Engl J Med, 344(20): 1516–1526.CrossRefPubMedGoogle Scholar
  20. 20.
    Prusiner S B, Groth D, Serban A,et al. 1993. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc Natl Acad Sci USA, 90: 10608–10612.CrossRefPubMedGoogle Scholar
  21. 21.
    Williamsa A, Lucassenc P J, Ritchiea D,et al. 1997. PrP Deposition, Microglial Activation, and Neuronal Apoptosis in Murine Scrapie. Exp Neurol, 144: 433–438.CrossRefGoogle Scholar

Copyright information

© Wuhan Institute of Virology, CAS and Springer-Verlag Berlin Heidelberg 2010

Authors and Affiliations

  • Yu Bai
    • 1
  • Yu-rong Li
    • 2
  • Gui-hua Wang
    • 3
  • Xiang-mei Zhou
    • 1
  • De-ming Zhao
    • 1
  1. 1.The state key Lab of Agrobiotechnology National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary MedicineChina Agricultural UniversityBeijingChina
  2. 2.Department of Animal Science and TechnologyAgricultural University of HebeiBaodingChina
  3. 3.Department of Animal Science and TechnologyAgricultural University of ShandongTaianChina

Personalised recommendations