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Copper binding to PrPC may inhibit prion disease propagation
Nuha Hijazi1, Yuval Shaked, Hana Rosenmann
1Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Ein Karem, Jerusalem 91120, Israel.
Brain Research
|December 4, 2003
Summary
Copper supplementation reduced prion protein (PrPSc) accumulation in scrapie-infected cells and delayed prion disease onset in hamsters. This suggests copper influences prion disease propagation by affecting cellular interactions with PrPSc.
Area of Science:
- Neuroscience
- Biochemistry
- Molecular Biology
Background:
- The cellular prion protein (PrPC) binds copper, but its role in PrPC function and prion disease pathogenesis is not fully understood.
- Prion diseases are associated with the misfolding and aggregation of PrPC into PrPSc.
Purpose of the Study:
- To investigate the effect of copper on PrPSc accumulation and prion disease progression.
- To explore the potential therapeutic role of copper in prion diseases.
Main Methods:
- Neuroblastoma cells and hamsters were treated with copper.
- PrPSc accumulation was measured in cells and animals.
- Prion disease onset and progression were monitored in hamsters.
Main Results:
- Copper treatment reduced PrPSc accumulation in scrapie-infected neuroblastoma cells.
- Copper-treated normal cells showed reduced binding and internalization of PrPSc.
- Copper administration to hamsters induced cerebellar PrPC accumulation.
- Copper treatment significantly delayed the onset of prion disease in scrapie-infected hamsters.
Conclusions:
- Copper influences PrPC metabolism and PrPSc formation.
- Copper may hinder PrPSc propagation by altering PrPC interactions.
- Copper administration shows therapeutic potential for prion diseases.