• Food Science and Biotechnology
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• v.18 no.3
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• pp.782-787
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• 2009

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.