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000015094 0247_ $$2DOI$$a10.1515/BC.2011.048
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000015094 084__ $$2WoS$$aBiochemistry & Molecular Biology
000015094 1001_ $$0P:(DE-HGF)0$$aStöhr, J.$$b0
000015094 245__ $$aIn vitro conversion and seeded fibrillization of posttranslationally modified prion protein
000015094 260__ $$aBerlin [u.a.]$$bde Gruyter$$c2011
000015094 300__ $$a415 - 421
000015094 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000015094 440_0 $$09042$$aBiological Chemistry$$v392$$x1431-6730$$y5
000015094 500__ $$aThis work was supported by grants from the Deutsche Forschungsgemeinschaft (DFG), EUNetwork of Excellence (NeuroPrion) and the Praesidentenfond of the Helmholtzgemeinschaft (HGF, Virtual Institute of Structural Biology). Jan Stohr is supported by postdoctoral fellowship of the Deutsche Forschungsgemeinschaft (DFG). We thank S.B. Prusiner for critical reading and helpful discussion for this manuscript. The authors thank Ilka Ostermann for her assistance in the purification of CHO-PrP<SUP>C</SUP>.
000015094 520__ $$aThe conversion of the cellular isoform of the prion protein (PrP(C)) into the pathologic isoform (PrP(Sc)) is the key event in prion diseases. To study the conversion process, an in vitro system based on varying the concentration of low amounts of sodium dodecyl sulfate (SDS) has been employed. In the present study, the conversion of full-length PrP(C) isolated from Chinese hamster ovary cells (CHO-PrP(C)) was examined. CHO-PrP(C) harbors native, posttranslational modifications, including the GPI anchor and two N-linked glyco-sylation sites. The properties of CHO-PrP(C) were compared with those of full-length and N-terminally truncated recombinant PrP. As shown earlier with recombinant PrP (recPrP90-231), transition from a soluble α-helical state as known for native PrP(C) into an aggregated, β-sheet-rich PrP(Sc)-like state could be induced by dilution of SDS. The aggregated state is partially proteinase K (PK)-resistant, exhibiting a cleavage site similar to that found with PrP(Sc). Compared to recPrP (90-231), fibril formation with CHO-PrP(C) requires lower SDS concentrations (0.0075%), and can be drastically accelerated by seeding with PrP(Sc) purified from brain homogenates of terminally sick hamsters. Our results show that recPrP 90-231 and CHO-PrPC behave qualitatively similar but quantitatively different. The in vivo situation can be simulated closer with CHO-PrP(C) because the specific PK cleave site could be shown and the seed-assisted fibrillization was much more efficient.
000015094 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000015094 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000015094 588__ $$aDataset connected to Web of Science, Pubmed
000015094 650_2 $$2MeSH$$aAnimals
000015094 650_2 $$2MeSH$$aBlotting, Western
000015094 650_2 $$2MeSH$$aCHO Cells
000015094 650_2 $$2MeSH$$aCircular Dichroism
000015094 650_2 $$2MeSH$$aCricetinae
000015094 650_2 $$2MeSH$$aCricetulus
000015094 650_2 $$2MeSH$$aElectrophoresis, Polyacrylamide Gel
000015094 650_2 $$2MeSH$$aMicroscopy, Electron
000015094 650_2 $$2MeSH$$aPrPC Proteins: chemistry
000015094 650_2 $$2MeSH$$aPrPC Proteins: drug effects
000015094 650_2 $$2MeSH$$aPrPC Proteins: metabolism
000015094 650_2 $$2MeSH$$aPrPSc Proteins: chemistry
000015094 650_2 $$2MeSH$$aPrPSc Proteins: drug effects
000015094 650_2 $$2MeSH$$aPrPSc Proteins: metabolism
000015094 650_2 $$2MeSH$$aProtein Processing, Post-Translational
000015094 650_2 $$2MeSH$$aProtein Structure, Secondary
000015094 650_2 $$2MeSH$$aSodium Dodecyl Sulfate: pharmacology
000015094 650_7 $$00$$2NLM Chemicals$$aPrPC Proteins
000015094 650_7 $$00$$2NLM Chemicals$$aPrPSc Proteins
000015094 650_7 $$0151-21-3$$2NLM Chemicals$$aSodium Dodecyl Sulfate
000015094 650_7 $$2WoSType$$aJ
000015094 65320 $$2Author$$aaggregation
000015094 65320 $$2Author$$aconversion
000015094 65320 $$2Author$$afibrillization
000015094 65320 $$2Author$$aglycosylation
000015094 65320 $$2Author$$aGPI anchor
000015094 65320 $$2Author$$aprion protein
000015094 65320 $$2Author$$aseeding
000015094 7001_ $$0P:(DE-HGF)0$$aElfrink, K.$$b1
000015094 7001_ $$0P:(DE-HGF)0$$aWeinmann, N.$$b2
000015094 7001_ $$0P:(DE-HGF)0$$aWille, H.$$b3
000015094 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000015094 7001_ $$0P:(DE-Juel1)VDB65870$$aBirkmann, E.$$b5$$uFZJ
000015094 7001_ $$0P:(DE-HGF)0$$aRiesner, D.$$b6
000015094 773__ $$0PERI:(DE-600)1466062-3$$a10.1515/bc.2011.048$$gVol. 392, p. 415 - 421$$p415 - 421$$q392<415 - 421$$tBiological chemistry$$v392$$x1431-6730$$y2011
000015094 8567_ $$uhttp://dx.doi.org/10.1515/BC.2011.048
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