caa a22 4500 378866478 CHVBK 20180305123359.0 cr unu---uuuuu 161128e20030101xx s 000 0 eng 10.1351/pac200375020317 doi (NATIONALLICENCE)gruyter-10.1351/pac200375020317 Prion protein allotype profiling by mass spectrometry [Elektronische Daten] [M. E. Schininà, Bruno Maras, Franco Cardone, Carmine Mancone, S. Principe, M. A. Di Bari, P. Parchi, M. Pocchiari] Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative pathologies characterized by the formation in the central nervous system of the amyloid protein PrPSc, which derives from a cellular precursor called PrPc. Epidemiological and laboratory studies have shown that in species where the PrPc gene is polymorphic, the genotype composition is an important factor for the development of the disease. Identification of PrPSc allotypes accumulated in the brain during the disease proved valuable to investigate whether these polymorphisms are critical for the pathological conversion. These analyses are complicated by the heterogeneity and the insolubility of the prion amyloid extracted from affected brains, which have been obviated by extensive digestion of extracted fractions and analysis of peptide fragment composition. We have developed an optimized protocol of liquid chromatography/mass spectrometry (LC/MS) that can reliably map PrP peptides in digested fractions with a low PrPSc/contaminants ratio. This approach has been successfully applied to the analysis of amyloidogenesis in experimentally infected PrP-heterozygous laboratory animals. © 2013 Walter de Gruyter GmbH, Berlin/Boston Schininà M. E. Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, Roma, Italy aut Maras Bruno Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, Roma, Italy aut Cardone Franco Laboratorio di Virologia, Istituto Superiore di Sanità, Roma, Italy aut Mancone Carmine Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, Roma, Italy aut Principe S. Laboratorio di Virologia, Istituto Superiore di Sanità, Roma, Italy aut Di Bari M. A. Laboratorio di Medicina Veterinaria, Istituto Superiore di Sanità, Roma, Italy aut Parchi P. Dipartimento di Scienze Neurologiche, Università di Bologna, Italy aut Pocchiari M. Laboratorio di Virologia, Istituto Superiore di Sanità, Roma, Italy aut Pure and Applied Chemistry De Gruyter 75/2-3(2003-01-01), 317-323 0033-4545 75:2-3<317 2003 75 pac https://doi.org/10.1351/pac200375020317 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1351/pac200375020317 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Schininà M. E. Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, Roma, Italy aut NATIONALLICENCE 700 1- Maras Bruno Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, Roma, Italy aut NATIONALLICENCE 700 1- Cardone Franco Laboratorio di Virologia, Istituto Superiore di Sanità, Roma, Italy aut NATIONALLICENCE 700 1- Mancone Carmine Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, Roma, Italy aut NATIONALLICENCE 700 1- Principe S. Laboratorio di Virologia, Istituto Superiore di Sanità, Roma, Italy aut NATIONALLICENCE 700 1- Di Bari M. A. Laboratorio di Medicina Veterinaria, Istituto Superiore di Sanità, Roma, Italy aut NATIONALLICENCE 700 1- Parchi P. Dipartimento di Scienze Neurologiche, Università di Bologna, Italy aut NATIONALLICENCE 700 1- Pocchiari M. Laboratorio di Virologia, Istituto Superiore di Sanità, Roma, Italy aut NATIONALLICENCE 773 0- Pure and Applied Chemistry De Gruyter 75/2-3(2003-01-01), 317-323 0033-4545 75:2-3<317 2003 75 pac CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter