Clin Neuropathol
-
Creutzfeldt-Jakob disease (CJD) is a transmissible neurodegenerative disorder characterized by the accumulation of proteinase-resistant prion protein (PrP) in the brain. Pathological changes in the cerebellum are common and include atrophy of the granular layer, spongiform change in the molecular layer, and astrocytic gliosis of the cerebellar cortex and white matter. In most cases of sporadic CJD immunohistochemistry for PrP shows widespread granular deposits of the scrapie isoform of the prion protein (PrPSc) in the cerebellar cortex. ⋯ No significant difference in allele frequency between the 2 groups was found. Plaques or plaque-like PrPSc deposits were found in 9 cases of CJD and were associated with the presence of valine at codon 129 on at least 1 allele of PRNP. CJD patients homozygous for valine (V/V) were on an average more than 5 years younger than patients with M/M or M/V at codon 129.