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      Prion Protein Does Not Interfere with SNARE Complex Formation and Membrane Fusion

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      https://www.riss.kr/link?id=A82730841

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      다국어 초록 (Multilingual 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.
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      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, w...

      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.

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      목차 (Table of Contents)

      • Abstract
      • Introduction
      • Materials and Methods
      • Results and Discussion
      • Acknowledgments
      • Abstract
      • Introduction
      • Materials and Methods
      • Results and Discussion
      • Acknowledgments
      • References
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      참고문헌 (Reference)

      1 Asuni AA, "Unaltered SNARE complex formation in an in vivo model of prion disease" 1233 : 1-7, 2008

      2 Requena JR, "Thioredoxin converts the Syrian hamster (29-231) recombinant prion protein to an insoluble form" 30 : 141-147, 2001

      3 Poirier MA, "The synaptic SNARE complex is a parallel four-stranded helical bundle" 5 : 765-769, 1998

      4 Kitamoto T, "The primary structure of the prion protein influences the distribution of abnormal prion protein in the central nervous system" 141 : 271-277, 1992

      5 Hay DW, "The effects of calcium channel inhibitors and other procedures affecting calcium translocation on drug-induced rhythmic contractions in the rat vas deferens" 79 : 347-362, 1983

      6 Legname G, "Synthetic mammalian prions" 305 : 673-676, 2004

      7 Clinton J, "Synaptic degeneration is the primary neuropathological feature in prion disease: A preliminary study" 4 : 65-68, 1993

      8 Cunningham C, "Synaptic changes characterize early behavioural signs in the ME7 model of murine prion disease" 17 : 2147-2155, 2003

      9 Jeffrey M, "Synapse loss associated with abnormal PrP precedes neuronal degeneration in the scrapie-infected murine hippocampus" 26 : 41-54, 2000

      10 Brunger AT, "Structure of proteins involved in synaptic vesicle fusion in neurons" 30 : 157-171, 2001

      1 Asuni AA, "Unaltered SNARE complex formation in an in vivo model of prion disease" 1233 : 1-7, 2008

      2 Requena JR, "Thioredoxin converts the Syrian hamster (29-231) recombinant prion protein to an insoluble form" 30 : 141-147, 2001

      3 Poirier MA, "The synaptic SNARE complex is a parallel four-stranded helical bundle" 5 : 765-769, 1998

      4 Kitamoto T, "The primary structure of the prion protein influences the distribution of abnormal prion protein in the central nervous system" 141 : 271-277, 1992

      5 Hay DW, "The effects of calcium channel inhibitors and other procedures affecting calcium translocation on drug-induced rhythmic contractions in the rat vas deferens" 79 : 347-362, 1983

      6 Legname G, "Synthetic mammalian prions" 305 : 673-676, 2004

      7 Clinton J, "Synaptic degeneration is the primary neuropathological feature in prion disease: A preliminary study" 4 : 65-68, 1993

      8 Cunningham C, "Synaptic changes characterize early behavioural signs in the ME7 model of murine prion disease" 17 : 2147-2155, 2003

      9 Jeffrey M, "Synapse loss associated with abnormal PrP precedes neuronal degeneration in the scrapie-infected murine hippocampus" 26 : 41-54, 2000

      10 Brunger AT, "Structure of proteins involved in synaptic vesicle fusion in neurons" 30 : 157-171, 2001

      11 Sorensen JB, "Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles" 25 : 955-966, 2006

      12 Jahn R, "SNAREs-engines for membrane fusion" 7 : 631-643, 2006

      13 Chen YA, "SNARE-mediated membrane fusion" 2 : 98-106, 2001

      14 Weber T, "SNARE pins: Minimal machinery for membrane fusion" 92 : 759-772, 1998

      15 Melia TJ Jr, "Putting the clamps on membrane fusion: How complexin sets the stage for calcium-mediated exocytosis" 581 : 2131-2139, 2007

      16 Prusiner SB, "Prions" 95 : 13363-13383, 1998

      17 Russelakis-Carneiro M, "Prion replication alters the distribution of synaptophysin and caveolin 1 in neuronal lipid rafts" 165 : 1839-1848, 2004

      18 Ferrer I, "Prion protein deposition and abnormal synaptic protein expression in the cerebellum in Creutzfeldt-Jakob disease" 97 : 715-726, 2000

      19 Kocisko DA, "New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products" 77 : 10288-10294, 2003

      20 Pobbati AV, "N- to C-terminal SNARE complex assembly promotes rapid membrane fusion" 313 : 673-676, 2006

      21 Aguzzi A, "Mammalian prion biology: One century of evolving concepts" 116 : 313-327, 2004

      22 Porat Y, "Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism" 67 : 27-37, 2006

      23 Richardson CM, "Inhibition of acetylcholine release from presynaptic terminals of skate electric organ by calcium channel antagonists: a detailed pharmacological study" 35 : 1537-1546, 1996

      24 Jung CH, "Inhibition of SNARE-driven neuroexocytosis by plant extracts" 2008

      25 Castilla J, "In vitro generation of infectious scrapie prions" 121 : 195-206, 2005

      26 Mehlhorn I, "High-level expression and characterization of a purified 142-residue polypeptide of the prion protein" 35 : 5528-5537, 1996

      27 Xu Y, "Hemifusion in SNARE-mediated membrane fusion" 12 : 417-422, 2005

      28 Ferrer I, "Expression of proteins linked to exocytosis and neurotransmission in patients with Creutzfeldt-Jakob disease" 6 : 92-100, 1999

      29 Jeffrey M, "Early unsuspected neuron and axon terminal loss in scrapie­infected mice revealed by morphometry and immunocytochemistry" 21 : 41-49, 1995

      30 Hayashi T, "Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro" 14 : 2317-2325, 1995

      31 Shin JI, "Deep membrane insertion of prion protein upon reduction of disulfide bond" 377 : 995-1000, 2008

      32 Sutton RB, "Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution" 395 : 347-353, 1998

      33 Ma J, "Conversion of PrP to a self-perpetuating PrPSc­like conformation in the cytosol" 298 : 17-85, 2002

      34 Chen Y, "Constitutive versus regulated SNARE assembly: A structural basis" 23 : 681-689, 2004

      35 Kocisko DA, "Cell-free formation of protease-resistant prion protein" 370 : 471-474, 1994

      36 Ishida H, "Botulinum toxin type A targets RhoB to inhibit lysophosphatidic acid-stimulated actin reorganization and acetylcholine release in nerve growth factor-treated PC12 cells" 310 : 881-889, 2004

      37 Ray P, "Botulinum toxin inhibits arachidonic acid release associated with acetylcholine release from PC12 cells" 268 : 11057-11064, 1993

      38 Sandberg MK, "Altered interaction and expression of proteins involved in neurosecretion in scrapie-infected GT1-1 cells" 280 : 1264-1271, 2005

      39 Siso S, "Abnormal synaptic protein expression and cell death in murine scrapie" 103 : 615-626, 2002

      40 Jung CH, "A search for synthetic peptides that inhibit soluble N-ethylmaleimide sensitive-factor attachment receptor-mediated membrane fusion" 275 : 3051-3063, 2008

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      1999-01-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.75 0.17 0.56
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.49 0.43 0.364 0.06
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