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Prion diseases are progressive and transmissive neurodegenerative diseases. The conformational conversion of normal cellular prion protein (PrP^C) into abnormal pathogenic prion protein (PrP^Sc) is critical for its infection and pathogenesis. PrP^C possesses the ability to bind to various neurometals, including copper, zinc, iron, and manganese. Moreover, increasing evidence suggests that PrP^C plays essential roles in the maintenance of homeostasis of these neurometals in the synapse. In addition, trace metals are critical determinants of the conformational change and toxicity of PrP^C. Here, we review our studies and other new findings that inform the current understanding of the links between trace elements and physiological functions of PrP^C and the neurotoxicity of PrP^Sc.