Molecular Pathology of Human Prion Diseases
AbstractPrion diseases are fatal neurodegenerative conditions in humans and animals. In this review, we summarize the molecular background of phenotypic variability, relation of prion protein (PrP) to other proteins associated with neurodegenerative diseases, and pathogenesis of neuronal vulnerability. PrP exists in different forms that may be present in both diseased and non-diseased brain, however, abundant disease-associated PrP together with tissue pathology characterizes prion diseases and associates with transmissibility. Prion diseases have different etiological background with distinct pathogenesis and phenotype. Mutations of the prion protein gene are associated with genetic forms. The codon 129 polymorphism in combination with the Western blot pattern of PrP after proteinase K digestion serves as a basis for molecular subtyping of sporadic Creutzfeldt-Jakob disease. Tissue damage may result from several parallel, interacting or subsequent pathways that involve cellular systems associated with synapses, protein processing, oxidative stress, autophagy, and apoptosis.
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Kovacs, G.G.; Budka, H. Molecular Pathology of Human Prion Diseases. Int. J. Mol. Sci. 2009, 10, 976-999.
Kovacs GG, Budka H. Molecular Pathology of Human Prion Diseases. International Journal of Molecular Sciences. 2009; 10(3):976-999.Chicago/Turabian Style
Kovacs, Gabor G.; Budka, Herbert. 2009. "Molecular Pathology of Human Prion Diseases." Int. J. Mol. Sci. 10, no. 3: 976-999.