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Prion Protein Does Not Interfere with SNARE Complex Formation and Membrane Fusion
- Authors
- Yang, YS[Yang, Yoo-Soo]; Shin, JI[Shin, Jae-Il]; Shin, JY[Shin, Jae-Yoon]; Oh, JM[Oh, Jung-Mi]; Lee, SH[Lee, Sang Ho]; Yang, JS[Yang, Joo-Sung]; Kweon, DH[Kweon, Dae-Hyuk]
- Issue Date
- Jun-2009
- Publisher
- KOREAN SOC FOOD SCIENCE TECHNOLOGY
- Keywords
- prion; soluble N-ethylmaleimide sensitive factor attachment receptor (SNARE); membrane fusion; transmissible spongiform encephalopathy; synaptic transmission
- Citation
- FOOD SCIENCE AND BIOTECHNOLOGY, v.18, no.3, pp.782 - 787
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- FOOD SCIENCE AND BIOTECHNOLOGY
- Volume
- 18
- Number
- 3
- Start Page
- 782
- End Page
- 787
- ISSN
- 1226-7708
- 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 fort-nation of 3 SNARE proteins: syntaxin la, 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 synaptic function by directly interfering with SNARE complex formation.
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Related Researcher
- KWEON, DAE HYUK
- Biotechnology and Bioengineering (Integrative Biotechnology)