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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Am+J+Pathol
2014 ; 184
(12
): 3299-307
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Uptake and degradation of protease-sensitive and -resistant forms of abnormal
human prion protein aggregates by human astrocytes
#MMPMID25280631
Choi YP
; Head MW
; Ironside JW
; Priola SA
Am J Pathol
2014[Dec]; 184
(12
): 3299-307
PMID25280631
show ga
Sporadic Creutzfeldt-Jakob disease is the most common of the human prion
diseases, a group of rare, transmissible, and fatal neurologic diseases
associated with the accumulation of an abnormal form (PrP(Sc)) of the host prion
protein. In sporadic Creutzfeldt-Jakob disease, disease-associated PrP(Sc) is
present not only as an aggregated, protease-resistant form but also as an
aggregated protease-sensitive form (sPrP(Sc)). Although evidence suggests that
sPrP(Sc) may play a role in prion pathogenesis, little is known about how it
interacts with cells during prion infection. Here, we show that
protease-sensitive abnormal PrP aggregates derived from patients with sporadic
Creutzfeldt-Jakob disease are taken up and degraded by immortalized human
astrocytes similarly to abnormal PrP aggregates that are resistant to proteases.
Our data suggest that relative proteinase K resistance does not significantly
influence the astrocyte's ability to degrade PrP(Sc). Furthermore, the cell does
not appear to distinguish between sPrP(Sc) and protease-resistant PrP(Sc),
suggesting that sPrP(Sc) could contribute to prion infection.