Linked Life Data

12867662

Source:http://linkedlifedata.com/resource/pubmed/id/12867662

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 8
pubmed:dateCreated
2003-7-17
pubmed:abstractText
Prion diseases are characterized by the accumulation of an abnormal, proteinase K-resistant isoform of the prion protein, PrP(Sc), which is generated by a post-translational conversion of the protease-sensitive normal cell-surface glycoprotein PrP(c) involving major conformational changes. The conversion is thought to occur at the plasma membrane or along the endocytic pathway towards the lysosome. PrP(Sc) aggregates have been found to accumulate in secondary lysosomes. In our study, the activities of two major lysosomal cysteine proteases, cathepsins B and L, were found to be significantly increased in scrapie-infected Neuro2a cells compared with uninfected cells using biochemical and cytochemical methods. We hypothesize that lysosomal proteases may be involved in a 'second autocatalytic loop' of PrP(Sc) formation, acting in concert with the well-known autocatalytic enhancement of PrP conversion in the presence of PrP(Sc).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2279-83
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Up-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells.
pubmed:affiliation
Department of Gerontology, Institute for Ageing and Health, University of Newcastle upon Tyne, Newcastle upon Tyne, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't