Linked Life Data

12713659

Source:http://linkedlifedata.com/resource/pubmed/id/12713659

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-4-25
pubmed:abstractText
N-linked glycans with complex structure have a major role in the biological activity of a wide variety of cell surface and secreted glycoproteins. Here, we show that geldanamycin, an inhibitor of Hsp90, interferes with the formation of complex glycosylated mammalian prion protein (PrPC). Similarly to inhibitors of alpha-mannosidases, geldanamycin stabilized a high mannose PrPC glycoform and prevented the subsequent processing into complex structures. Moreover, a PrP/Grp94 complex could be isolated from geldanamycin-treated cells, suggesting that Grp94 might play a role in the processing of PrPC in the endoplasmic reticulum. Inhibition of complex glycosylation did not interfere with the glycosylphosphatidylinositol (GPI) anchor attachment and cellular trafficking of high mannose PrPC to the outer leaflet of the plasma membrane. In scrapie-infected neuroblastoma cells, however, high mannose PrPC glycoforms were preferred substrates for the formation of PrP-scrapie (PrPSc). Our study reveals that complex glycosylation is dispensable for the cellular trafficking of PrPC, but modulates the formation of PrPSc.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1398-9219
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
313-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Inhibition of complex glycosylation increases the formation of PrPsc.
pubmed:affiliation
Department of Cellular Biochemistry, Max-Planck-Institute for Biochemistry, 82152 Martinsried, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't