Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Kocisko, D.A. et al.

Kocisko, Engel, Harbuck, Arnold, Olsen, Raymond, Vilette, Caughey,

Comparison of protease-resistant prion protein inhibitors in cell cultures infected with two strains of mouse and sheep scrapie.

The transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases. A primary therapeutic target for TSE intervention has been a protease-resistant form of prion protein known as PrP(Sc) or PrP-res. In vitro testing of mouse scrapie-infected cell cultures has identified many PrP-res inhibitors that also have activity in vivo. Here we identify 32 new inhibitors of two strains of mouse scrapie PrP-res. Furthermore, to investigate the species-specificity of these and other PrP-res inhibitors, we have developed a high-throughput cell culture assay based on Rov9 cells chronically-infected with sheep scrapie. Of 32 inhibitors of murine PrP-res that were also tested in the Rov9 cells, only six showed inhibitory activity against sheep PrP-res. The three most potent inhibitors of both murine and ovine PrP-res formation (with 50% inhibition at < or =5 microM) were tannic acid, pentosan polysulfate and Fe(III) deuteroporphyrin 2,4-bisethyleneglycol. The latter two have anti-mouse scrapie activity in vivo. These results identify new inhibitors of murine and ovine PrP-res formation and reinforce the idea that compounds effective against PrP-res from one species or strain cannot be assumed to be active against others.[1]

References

Comparison of protease-resistant prion protein inhibitors in cell cultures infected with two strains of mouse and sheep scrapie. Kocisko, D.A., Engel, A.L., Harbuck, K., Arnold, K.M., Olsen, E.A., Raymond, L.D., Vilette, D., Caughey, B. Neurosci. Lett. (2005) [Pubmed]

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