Linked Life Data

18328261

Source:http://linkedlifedata.com/resource/pubmed/id/18328261

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-3-31
pubmed:abstractText
The conversion of cellular prion protein to the disease-associated isoform (PrP(Sc)) has been suggested to follow a mechanism of seeded aggregation. Here, we show that fragmentation of PrP(Sc) aggregates by sonication increases converting activity in cell culture in a way similar to in vitro conversion assays. In contrast, under the same conditions the infectious titer of sonicated samples in vivo was reduced. We modified the size distribution of PrP(Sc) by adsorption to nitrocellulose, which resulted in a reduction of the infectious titer in non-sonicated samples and an increase in sonicated samples. Our results indicate that NC-adsorption can (i) block some active sites of PrP(Sc) aggregates and (ii) reduce the rate of clearance from the brain. For large particles with low clearance the effect of NC-particles on the number of available active sites may dominate, whereas for smaller particles (i.e. sonicated samples) the effect of NC-adsorption on clearance dominates resulting in increased infectivity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
369
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
924-8
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Differential effects of prion particle size on infectivity in vivo and in vitro.
pubmed:affiliation
Center for Neuropathology and Prion Research, Ludwig Maximilians University of Munich, Feodor-Lynen-Strasse 23, 81377 Munich, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't