Linked Life Data

14593181

Source:http://linkedlifedata.com/resource/pubmed/id/14593181

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5646
pubmed:dateCreated
2003-10-31
pubmed:abstractText
The mechanisms involved in prion neurotoxicity are unclear, and therapies preventing accumulation of PrPSc, the disease-associated form of prion protein (PrP), do not significantly prolong survival in mice with central nervous system prion infection. We found that depleting endogenous neuronal PrPc in mice with established neuroinvasive prion infection reversed early spongiform change and prevented neuronal loss and progression to clinical disease. This occurred despite the accumulation of extraneuronal PrPSc to levels seen in terminally ill wild-type animals. Thus, the propagation of nonneuronal PrPSc is not pathogenic, but arresting the continued conversion of PrPc to PrPSc within neurons during scrapie infection prevents prion neurotoxicity.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
31
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
871-4
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis.
pubmed:affiliation
Medical Research Council Prion Unit and Department of Neurodegenerative Disease, Institute of Neurology, Queen Square, London WC1, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't