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KMID : 1007520090180030782
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Food Science and Biotechnology
2009 Volume.18 No. 3 p.782 ~ p.787
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Prion Protein Does Not Interfere with SNARE Complex Formation and Membrane Fusion
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Yang Yoo-Soo
Shin Jae-Il
Shin Jae-Yoon
Oh Jung-Mi
Lee Sang-Ho
Yang Joo-Sung
Kweon Dae-Hyuk
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Abstract
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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.
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KEYWORD
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prion, soluble N-ethylmaleimide sensitive factor attachment receptor (SNARE), membrane fusion, transmissiblespongiform encephalopathy, synaptic transmission
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