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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1999-10-18
pubmed:abstractText
Creutzfeldt-Jakob disease (CJD) and other transmissible spongiform encephalopathies (TSEs) are characterised by the accumulation of a pathological conformer of PrP, named PrPsc. Molecular weight and glycosylation of the protease-resistant core of PrPsc (PrP27-30) are heterogeneous in different forms of TSEs. We analysed PrP27-30 glycotypes in a large number of TSE-affected patients: 50 sporadic CJD (sCJD), 1 iatrogenic CJD, 1 Gerstmann-Sträussler-Scheinker syndrome (GSS) with the Pro102Leu mutation of PrP, 3 familial CJD (fCJD) with the Glu200Lys mutation and, for the first time, 7 fCJD with the Val210ll3e mutation. All patients were screened for the polymorphic codon 129 of the PrP gene. PrP27-30 deglycosylation and PrPsc immunohistochemistry were performed in selected cases. We found that two PrP27-30 glycotypes (type 1A and type 2A) are produced in sCJD. Type 1A is more frequently associated with methionine than valine in position 129. Type 1A is also formed in Val210lle fCJD. In Glu200Lys fCJD and GSS patients, we found that PrP27-30 has the same mobility of type 1 but different glycosylation ratios (type 1B). Our findings indicate that the polymorphic residue 129 of PrP has a leading role in determining the proteinase degradation site of PrPsc while mutant residues 102 or 200 influence only the glycosylation pattern.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0361-9230
pubmed:author
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
429-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Prion protein glycotype analysis in familial and sporadic Creutzfeldt-Jakob disease patients.
pubmed:affiliation
Laboratory of Virology, Istituto Superiore di Sanità, Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't