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Influence of PrP conversion on ion metabolism 2

In collaboration with Partner 4 we looked also at the metal ion metabolism in prion infected cells. Using radioactive copper (64Cu) at physiological concentration, we showed that prion infected cells display a marked reduction in copper binding. The level of full-length prion protein known to bind the metal ion was not modified in infected cells, but a fraction of this protein was not releasable from the membrane by phosphatidylinositol-specific phospholipase C. Our results suggest therefore that prion infection modulates copper content at a cellular level and that modification of copper homeostasis plays a determinant role in the neuropathology of TSEs.

Ref: Rachidi W., Mangé A., Senator A, Guiraud P., Riondel J., Benboubetra M., Favier A.& Lehmann S. (2003) Prion infection impairs copper binding of infected cells. J. Biol. Chem. 278, 14595-8.

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