Different Patterns of Truncated Prion Protein Fragments Correlate with Distinct Phenotypes in P102L Gerstmann--Straussler--Scheinker Disease

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 95; no. 14; pp. 8322 - 8327
• Main Authors: Parchi, Piero, Chen, Shu G., Brown, Paul, Zou, Wenquan, Capellari, Sabina, Budka, Herbert, Hainfellner, Johannes, Reyes, Patricio F., Golden, Gregory T., Hauw, Jean J., Gajdusek, D. Carleton, Gambetti, Pierluigi
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 07.07.1998; National Acad Sciences; National Academy of Sciences; The National Academy of Sciences
• Subjects: Adult; Aged; Amyloids; Biological Sciences; Codons; Creutzfeldt Jakob syndrome; Disease; Female; Genes; Genetic Markers; Genetic mutation; Gerstmann-Straussler-Scheinker Disease - genetics; Gerstmann-Straussler-Scheinker Disease - metabolism; Gerstmann-Straussler-Scheinker Disease - physiopathology; Heterogeneity; Humans; Male; Mass spectroscopy; Middle Aged; Mutation; Nervous system diseases; Neurology; Pathology; Peptide Fragments - genetics; Peptide Fragments - metabolism; Phenotypes; Prion diseases; Prions; Prions - genetics; Prions - metabolism; Proteins

The clinicopathological phenotype of the Gerstmann--Straussler--Scheinker disease (GSS) variant linked to the codon 102 mutation in the prion protein (PrP) gene (GSS P102L) shows a high heterogeneity. This variability also is observed in subjects with the same prion protein gene PRNP haplotype and i...