Journal
MOLECULAR MEDICINE
Volume 13, Issue 3-4, Pages 190-198Publisher
SPRINGER
DOI: 10.2119/2006-00073.Karpuj
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Funding
- NCI NIH HHS [P20 CA091471] Funding Source: Medline
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Prions are composed solely of the disease-causing prion protein (PrPsc) that is formed from the cellular isoform PrPC by a post-translational process. Here we report that short phosphorothioate DNA (PS-DNA) oligonucleotides diminished the levels of both PrPC and PrPSc in prion-infected neuroblastoma (ScN2a) cells. The effect of PS-DNA on PrP levels was independent of the nucleotide sequence. The effective concentration (EC50) of PS-DNA required to achieve half-maximal diminution of PrPSc was similar to 70 nM, whereas the EC50 of PS-DNA for PrPc was more than 50-fold greater. This finding indicated that diminished levels of PrPSc after exposure to PS-DNA are unlikely to be due to decreased PrPC levels. Bioassays in transgenic mice demonstrated a substantial diminution in the prion infectivity after ScN2a cells were exposed to PS-DNAs. Whether PS-DNA will be useful in the treatment of prion disease in. people or livestock remains to be established.
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