Inherited human prion diseases, such as fatal familial insomnia (FFI) and familial Creutzfeldt-Jakob disease (fCJD), are associated with autosomal dominant mutations in the human prion protein gene and accumulation of PrP, an abnormal isomer of the normal host protein PrP, in the brain of affected individuals. PrP is the principal component of the transmissible neurotoxic prion agent. It is important to identify molecular pathways and cellular processes that regulate prion formation and prion-induced neurotoxicity.
View Article and Find Full Text PDFThe prion protein (PrP) can be structurally shifted to its PrP isoform causing a wide range of neurodegenerative diseases, which are currently incurable. There is an evidence that metallothioneins (MTs), and especially MT-3, are associated with neurodegenerative diseases. PrP and MTs play pivotal roles in maintaining metal homeostasis; therefore, it is conceivable that each of them has its own significance in prion diseases.
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