Earticle

초록

영어

In prion disease, spongiform neurodegeneration is preceded by earlier synaptic dysfunction. There is evidence thatsoluble N-ethylmaleimide sensitive factor attachment receptor (SNARE) complex formation is reduced in scrapie-infected invivo 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 3SNARE proteins: syntaxin 1a, SNAP-25, and synaptobrevin. Sodium dodecyl sulfate-resistant complex formation, SNARE-driven membrane fusion, and neuroexocytosis of PC12 cells were not altered by PrP. Thus, PrP does not alter synapticfunction by directly interfering with SNARE complex formation.

목차

Abstract
 Introduction
 Materials and Methods
 Results and Discussion
 References

키워드

저자

• Yoo-Soo Yang [ Department of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ]
• Jae-Il Shin [ Department of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ]
• Jae-Yoon Shin [ Department of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ]
• Jung-Mi Oh [ Department of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ]
• Sang Ho Lee [ Department of Biological Sciences, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ]
• Joo-Sung Yang [ Department of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ]
• Dae-Hyuk Kweon [ Department of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi 440-746, Korea ] Corresponding author

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  Food Science and Biotechnology

• 간기

  격월간

• pISSN

  1226-7708

• 수록기간

  1992~2009

• 십진분류

  KDC 574 DDC 664