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Trace elements and prion diseases: a review of the interactions of copper, manganese and zinc with the prion protein

Published online by Cambridge University Press:  28 March 2007

Scott P. Leach ,
M. D. Salman  and
Dwayne Hamar
Scott P. Leach
Affiliation:
Colorado Department of Agriculture, Division of Animal Industry, 700 Kipling Street, Suite 4000, Lakewood, CO 80215-8000, USA
M. D. Salman
Affiliation:
Animal Population Health Institute of Colorado State University, Fort Collins, CO 80523-1681, USA
Dwayne Hamar
Affiliation:
Veterinary Diagnostic Laboratory, Colorado State University, Fort Collins, CO 80523-1681, USA
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Abstract

Transmissible spongiform encephalopathies (TSEs) are a family of neurodegenerative diseases characterized by their long incubation periods, progressive neurological changes, and spongiform appearance in the brain. There is much evidence to show that TSEs are caused by an isoform of the normal cellular surface prion protein PrPC. The normal function of PrPC is still unknown, but it exhibits properties of a cupro-protein, capable of binding up to six copper ions. There are two differing views on copper's role in prion diseases. While one view looks at the PrPC copper-binding as the trigger for conversion to PrPSc, the opposing viewpoint sees a lack of PrPC copper-binding resulting in the conformational change into the disease causing isoform. Manganese and zinc have been shown to interact with PrPC as well and have been found in abnormal levels in prion diseases. This review addresses the interaction between select trace elements and the PrPC.

Keywords

transmissible spongiform encephalopathyprioncoppermanganesezinctrace elements
Type
Research Article
Information
Animal Health Research Reviews , Volume 7 , Issue 1-2 , June 2006 , pp. 97 - 105
Copyright
Cambridge University Press

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