Linked Life Data

7562256

Source:http://linkedlifedata.com/resource/pubmed/id/7562256

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1995-11-14
pubmed:abstractText
The prion encephalopathies are characterized by accumulation in the brain of the abnormal form PrPsc of a normal host gene product PrPc. The mechanism and site of formation of PrPsc from PrPc are currently unknown. In this study, ME7 scrapie-infected mouse brain was used to show, both biochemically and by double-labelled immunogold electron microscopy, that proteinase K-resistant PrPsc is enriched in subcellular structures which contain the cation-independent mannose 6-phosphate receptor, ubiquitin-protein conjugates, beta-glucuronidase, and cathepsin B, termed late endosome-like organelles. The glycosylinositol phospholipid membrane-anchored PrPc will enter such compartment for normal degradation and the organelles may therefore act as chambers for the conversion of PrPc into infectious PrPsc in this murine model of scrapie.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-3417
pubmed:author
pubmed:issnType
Print
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
403-11
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain.
pubmed:affiliation
Department of Biochemistry, University of Nottingham Medical School, Queen's Medical Centre, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't