Part of the book: Oligomerization of Chemical and Biological Compounds
Prion diseases are progressive neurodegenerative diseases that are associated with the conformational conversion of normal cellular prion protein (PrPC) into abnormal pathogenic prion protein (PrPSc). PrPC is a metal‐binding protein that is located in the synapse and possesses the ability to bind to various metals, including Cu, Zn, Mn and Fe. Moreover, increasing evidence suggests that PrPC plays essential roles in the maintenance of metal homeostasis in the synapse. Trace elements have a crucial influence on the conformational change of PrPC. Given that other disease‐related proteins such as β‐amyloid protein and its precursor protein (APP) in Alzheimer's disease also exist in the synapse and possess a metal‐binding ability, an interaction between PrP and metals and between PrP and APP, may occur in the synapse; the resulting metal homeostasis may lead to the pathogenesis of prion diseases. Here, we review our studies and other new findings that inform the current understanding of the link between trace elements and physiological functions of PrPC and the neurotoxicity of PrPSc.
Part of the book: Prion