Linked Life Data

7763249

Source:http://linkedlifedata.com/resource/pubmed/id/7763249

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-6-29
pubmed:abstractText
A major component of the infectious particle causing spongiform encephalopathies or prion diseases is an aberrant isoform (PrPSc) of a glycosyl-phosphatidylinositol (GPI)-anchored cell surface protein, PrPC. The cellular processes involved in the formation of PrPSc are unclear but involve the internalization of PrPC prior to conversion. Here, we demonstrate that PrPC is associated with caveolin, a structural protein component of caveolae. We show that PrPC and caveolin share similar detergent characteristics and copurify in linear sucrose gradients. PrPC was protected from proteinase K digestion in the caveolin fraction but solubilizing the caveolae prior to proteinase K digestion rendered PrPC susceptible to proteinase K digestion. Our results indicate a physical association between PrPC and caveolin in N2a cells. The implication of these results in relation to prion biogenesis is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
210
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
753-9
pubmed:dateRevised
2010-8-25
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The cellular isoform of the prion protein, PrPc, is associated with caveolae in mouse neuroblastoma (N2a) cells.
pubmed:affiliation
Department of Zoology, University College Dublin, Belfield, Ireland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't