![]() ![]() ![]() PrP C is encoded by the PRNP gene and is most highly expressed in the central nervous system. Accumulation of PrP Sc occurs by a mechanism of seeded conversion of PrP C which can result in PrP Sc aggregates ranging from discrete fibrils to diffuse amyloid plaques. Prion diseases are marked by the accumulation of protease-resistant isoforms of the prion protein, designated PrP Sc, in the central nervous system. Prion diseases include Creutzfeldt–Jakob disease (CJD) in man, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle and scrapie in sheep and goats. The presence of K 222 or S 146 alleles demonstrated significantly different relative levels of C1 compared to that observed in wild type goats, which suggests that the genotype association with C1 is neither unique to sheep nor exclusive to the ovine Q171R dimorphism.Įxpression of the cellular form of the prion protein (PrP C) is essential for the pathogenesis of a group of disorders called prion diseases, also known as transmissible spongiform encephalopathies (TSE). Brain tissue homogenates from scrapie-free goats with wild type PRNP or polymorphisms (I142M, H143R, N146S, or Q222K) were deglycosylated prior to immunoblot for assessment of the relative abundance of the C1 fragment of PrP C. In this study, we assessed PrP C in goats for the existence of similar associations between PrP C fragments and genotype. Goats are another small ruminant where classical scrapie susceptibility is under strong genetic control. The relative abundance of C1, a natural α-cleavage fragment of PrP C, was previously found to be associated with a resistant PRNP genotype in sheep. Amino acid changes in PrP C or a reduced amount of PrP C may modulate disease resistance. Expression of the cellular prion protein (PrP C) is crucial for the development of prion diseases. ![]()
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