Linked Life Data

7595652

Source:http://linkedlifedata.com/resource/pubmed/id/7595652

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-12-14
pubmed:abstractText
Gerstmann-Sträussler-Scheinker (GSS) disease is a familial neurological disorder pathologically characterized by accumulation of prion protein (PrP) in the form of fibrillary and non-fibrillary deposits within the cerebrum and cerebellum. We have studied two patients in whom the disease is caused by a leucine for proline amino acid substitution at residue 102 of PrP. In both patients, the neuropathologic findings are similar, consisting of spongiform changes, amyloid deposits, and gliosis. To investigate the antigenic profile of PrP deposits, we used antibodies raised against several peptides that correspond to segments of the N-terminus, repeat region, midregion, and C-terminus of PrP. By immunohistochemistry, PrP amyloid cores are best labeled by antibodies directed to epitopes spanning PrP residues 90-165. In GSS disease caused by a substitution of thymine to cytosine at PRNP codon 198 (Indiana kindred), the major amyloidogenic peptide spans residues 58-150; therefore, in these two genetic forms of GSS disease, amyloid may be composed of different peptides.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-3069
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
790-801
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Gerstmann-Sträussler-Scheinker disease (PRNP P102L): amyloid deposits are best recognized by antibodies directed to epitopes in PrP region 90-165.
pubmed:affiliation
Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.