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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Removal of the Glycosylation of Prion Protein Provokes Apoptosis in SF126

  • Chen, Lan (National Laboratory of Medical Molecular Biology, Institute of Basic Medical Science, Chinese Academy of Medical Sciences and Peking Union Medical College) ;
  • Yang, Yang (National Laboratory of Medical Molecular Biology, Institute of Basic Medical Science, Chinese Academy of Medical Sciences and Peking Union Medical College) ;
  • Han, Jun (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Zhang, Bao-Yun (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Zhao, Lin (National Laboratory of Medical Molecular Biology, Institute of Basic Medical Science, Chinese Academy of Medical Sciences and Peking Union Medical College) ;
  • Nie, Kai (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Wang, Xiao-Fan (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Li, Feng (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Gao, Chen (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Dong, Xiao-Ping (State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention) ;
  • Xu, Cai-Min (National Laboratory of Medical Molecular Biology, Institute of Basic Medical Science, Chinese Academy of Medical Sciences and Peking Union Medical College)
  • 발행 : 2007.09.30
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초록

Although the function of cellular prion protein (PrP$^C$) and the pathogenesis of prion diseases have been widely described, the mechanisms are not fully clarified. In this study, increases of the portion of non-glycosylated prion protein deposited in the hamster brains infected with scrapie strain 263K were described. To elucidate the pathological role of glycosylation profile of PrP, wild type human PrP (HuPrP) and two genetic engineering generated non-glycosylated PrP mutants (N181Q/N197Q and T183A/T199A) were transiently expressed in human astrocytoma cell line SF126. The results revealed that expressions of non-glycosylated PrP induced significantly more apoptosis cells than that of wild type PrP. It illustrated that Bcl-2 proteins might be involved in the apoptosis pathway of non-glycosylated PrPs. Our data highlights that removal of glycosylation of prion protein provokes cells apoptosis.

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참고문헌

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  2. PrP mutants with different numbers of octarepeat sequences are more susceptible to the oxidative stress vol.51, pp.7, 2008, https://doi.org/10.1007/s11427-008-0062-4
  3. Co-expressions of Casein Kinase 2 (CK2) Subunits Restore the Down-Regulation of Tubulin Levels and Disruption of Microtubule Structures Caused by PrP Mutants vol.50, pp.1, 2013, https://doi.org/10.1007/s12031-012-9845-y
  4. Transient expressions of doppel and its structural analog prionΔ32-121 in SH-SY5Y cells caused cytotoxicity possibly by triggering similar apoptosis pathway vol.37, pp.5, 2010, https://doi.org/10.1007/s11033-009-9772-3
  5. Toward a Mechanism of Prion Misfolding and Structural Models of PrPSc: Current Knowledge and Future Directions vol.74, pp.2-4, 2011, https://doi.org/10.1080/15287394.2011.529065
  6. A Novel PrP Partner HS-1 Associated Protein X-1 (HAX-1) Protected the Cultured Cells Against the Challenge of H2O2 vol.45, pp.2, 2011, https://doi.org/10.1007/s12031-011-9498-2
  7. WITHDRAWN: Transient expressions of doppel and its structural analog PrPΔ32-121 in SH-SY5Y cells caused cytotoxicity by triggering same apoptosis pathway 2009, https://doi.org/10.1016/j.biopha.2009.09.007
  8. Glycosylation modification of human prion protein provokes apoptosis in HeLa cells in vitro vol.42, pp.6, 2009, https://doi.org/10.5483/BMBRep.2009.42.6.331
  9. Resistance against apoptosis by the cellular prion protein is dependent on its glycosylation status in oral HSC-2 and colon LS 174T cancer cells vol.306, pp.1, 2011, https://doi.org/10.1016/j.canlet.2011.02.040
  10. Casein kinase II interacts with prion proteinin vitroand forms complex with native prion proteinin vivo vol.40, pp.12, 2008, https://doi.org/10.1111/j.1745-7270.2008.00486.x
  11. Human Prion Protein Mutants with Deleted and Inserted Octarepeats Undergo Different Pathways to Trigger Cell Apoptosis vol.43, pp.3, 2011, https://doi.org/10.1007/s12031-010-9387-0