Allelic Origin of Protease-Sensitive and Protease-Resistant Prion Protein Isoforms in Gerstmann-Sträussler-Scheinker Disease with the P102L Mutation

• Published in: PloS one Vol. 7; no. 2; p. e32382
• Main Authors: Monaco, Salvatore, Fiorini, Michele, Farinazzo, Alessia, Ferrari, Sergio, Gelati, Matteo, Piccardo, Pedro, Zanusso, Gianluigi, Ghetti, Bernardino
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 23.02.2012; Public Library of Science (PLoS)
• Subjects: Adult; Aged; Alleles; Antibodies; Biology; Centrifugation, Density Gradient; Creutzfeldt-Jakob disease; Degeneration; Dementia; Diagnostic systems; Female; Fragmentation; Gerstmann-Straussler-Scheinker Disease - genetics; Gerstmann-Straussler-Scheinker Disease - metabolism; Humans; Immunohistochemistry; Immunohistochemistry - methods; Insomnia; Isoelectric Focusing; Isoforms; Laboratories; Leucine; Male; Medicine; Middle Aged; Models, Genetic; Morphology; Mutation; Neuropathology; Paraffin; Peptide Hydrolases - metabolism; Peptides; Phenotype; Phenotypes; Point Mutation; Positron-Emission Tomography - methods; Prion protein; Proline; Propagation; Protease; Protein Conformation; Protein purification; Proteinase; Proteins; Proteolysis; PrPSc Proteins - genetics; Separation techniques; Sucrose - chemistry; Transgenic animals; Western blotting; Italy; Indiana; Monaco; United States > US; Indianapolis Indiana

Gerstmann-Sträussler-Scheinker (GSS) disease is a dominantly inherited prion disease associated with point mutations in the Prion Protein gene. The most frequent mutation associated with GSS involves a proline-to-leucine substitution at residue 102 of the prion protein, and is characterized by marke...