1887

Abstract

Expression of the cellular prion protein PrP is for the development of transmissible spongiform encephalopathy and thus for the accumulation of the illness-associated conformer PrP. Therefore, the tissue distribution of PrP at the protein level in both quantitative and qualitative terms was investigated. PrP was quantified using a two-site enzyme immunometric assay which was calibrated with purified ovine recombinant prion protein (rPrP). The most PrP-rich tissue was the brain, followed by the lungs, skeletal muscle, heart, uterus, thymus and tongue, which contained between 20- and 50-fold less PrP than the brain. The PrP content of these tissues seems to be comparable between sheep. Other organs, however, showed different, but low, levels of the protein depending on the animal examined. This was also the case for tissues from the gastrointestinal tract. The tissue containing the lowest concentration of PrP was shown to be the liver, where PrP was found to be between 564- and 16000-fold less abundant than in the brain. PrP was concentrated from crude cellular extracts by immunoprecipitation using several monoclonal and polyclonal anti-ovine PrP antibodies. Interestingly, it was observed that the isoform profile of PrP was tissue-specific. The most atypical electrophoretic profile of PrP was found in the skeletal muscle, where two polypeptides of 32 and 35 kDa were detected.

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2001-08-01
2019-10-15
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