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Creutzfeldt-Jakob disease.
Creutzfeldt-Jakob disease (CJD), a neurodegenerative disorder that is the commonest form of human prion disease or transmissible spongiform encephalopathies (TSEs). Four types of CJD are known: Sporadic (sCJD), familial or genetic (gCJD); iatrogenic (iCJD) and variant CJD (vCJD). The latter results from transmission of bovine spongiform encephalopathy (BSE) from cattle to humans. The combination of PrP(Sc) peptide (either 21 kDa or 19 kDa) and the status of the codon 129 of the gene (PRNP) encoding for PrP (either Methionine or Valine) is used to classify sCJD into 6 types: MM1 and MV1, the most common; VV2; MV2 (Brownell/Oppenheimer syndrome); MM2; VV1 and sporadic fatal insomnia, in that order of prevalence. Genetic CJD is caused by diverse mutations in the PRNP gene. The neuropathology of CJD consists of spongiform change, astro- and microgliosis and poorly defined neuronal loss. In a proportion of cases, amyloid plaques, like those of kuru, are seen. PrP immunohistochemistry reveals different types of PrP(Sc) deposits - the most common is the synaptic-type, but perivacuolar, perineuronal and plaque-like deposits may be also detected.
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