Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Prion Protein Does Not Interfere with SNARE Complex Formation and Membrane Fusion

  • Yang, Yoo-Soo (Department of Biotechnology and Bioengineering, Sungkyunkwan University) ;
  • Shin, Jae-Il (Department of Biotechnology and Bioengineering, Sungkyunkwan University) ;
  • Shin, Jae-Yoon (Department of Biotechnology and Bioengineering, Sungkyunkwan University) ;
  • Oh, Jung-Mi (Department of Biotechnology and Bioengineering, Sungkyunkwan University) ;
  • Lee, Sang-Ho (Department of Biological Sciences, Sungkyunkwan University) ;
  • Yang, Joo-Sung (Department of Biotechnology and Bioengineering, Sungkyunkwan University) ;
  • Kweon, Dae-Hyuk (Department of Biotechnology and Bioengineering, Sungkyunkwan University)
  • Published : 2009.06.30
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Abstract

In prion disease, spongiform neurodegeneration is preceded by earlier synaptic dysfunction. There is evidence that soluble N-ethylmaleimide sensitive factor attachment receptor (SNARE) complex formation is reduced in scrapie-infected in vivo models, which might explain this synaptic dysfunction because SNARE complex plays a crucial role in neuroexocytosis. In the present study, however, it is shown that prion protein (PrP) does not interfere with SNARE complex formation of 3 SNARE proteins: syntaxin 1a, SNAP-25, and synaptobrevin. Sodium dodecyl sulfate-resistant complex formation, SNAREdriven membrane fusion, and neuroexocytosis of PC12 cells were not altered by PrP. Thus, PrP does not alter synaptic function by directly interfering with SNARE complex formation.

Keywords

References

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