In-situ analysis of cellular poly(ADP-ribose) production in scrapie-infected mouse neuroblastoma cells

The Histochemical Journal
Yonghua ZhangAlexander Bürkle

Abstract

Transmissible spongiform encephalopathies (TSEs), also called prion diseases, are characterized by formation of the disease-associated isoform of prion protein (PrP(Sc)), which arises from a normal isoform termed PrP(c) by a post-translational conversion process occurring in an autocatalytic fashion. Oxidative stress has been proposed as a pathogenetic mechanism in TSEs and increased lipid peroxidation has recently been described in prion-infected cell cultures, suggesting an intrinsic link between the presence of prions and oxidative stress. We investigated if poly(ADP-ribose) formation can be detected in cultured cells upon prion infection, as this NAD+-consuming and DNA strand break-activated nuclear enzymatic reaction has the potential to cause rapid and lethal NAD+ depletion in cells under severe oxidative stress. Poly(ADP-ribose) production was analysed by immunofluorescence in freshly scrapie-infected Neuro2a-D11 mouse neuroblastoma cells, which had been confirmed by immunocytochemistry to produce PrP(Sc), and in uninfected controls. No spontaneous poly(ADP-ribose) specific signals were observed in infected or in uninfected cells, while both cell types readily reacted to H2O2 treatment with poly(ADP-ribose) synthesis in ...Continue Reading

Citations

Jul 18, 2003·The Journal of General Virology·Yonghua ZhangAlexander Bürkle
Aug 13, 2008·Archives of Virology·Stéphanie ChasseigneauxSylvain Lehmann
Oct 7, 2008·European Journal of Cell Biology·Nathalie M VeithAlexander Bürkle

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