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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2005-3-14
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pubmed:abstractText |
Several lines of evidence indicate that some glycoconjugates are efficient effectors of the cellular prion protein (PrP(C)) conversion into its pathogenic (PrP(Sc)) isoform. To assess how glycoconjugate glycan moieties participate in the biogenesis of PrP(Sc), an exhaustive comparative analysis of the expression of about 200 glycosylation-related genes was performed on prion-infected or not, hypothalamus-derived GT1 cells by hybridization of DNA microarrays, semiquantitative RT-PCR, and biochemical assays. A significant up- (30-fold) and down- (17-fold) regulation of the expression of the ChGn1 and Chst8 genes, respectively, was observed in prion-infected cells. ChGn1 and Chst8 are involved in the initiation of the synthesis of chondroitin sulfate and in the 4-O-sulfation of non-reducing N-acetylgalactosamine residues, respectively. A possible role for a hyposulfated chondroitin in PrP(Sc) accumulation was evidenced at the protein level and by determination of chondroitin and heparan sulfate amounts. Treatment of Sc-GT1 cells with a heparan mimetic (HM2602) induced an important reduction of the amount of PrP(Sc), associated with a total reversion of the transcription pattern of the N-acetylgalactosamine-4-O-sulfotransferase 8. It suggests a link between the genetic control of 4-O-sulfation and PrP(Sc) accumulation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylgalactosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylgalactosamine-4-sulfotransfe...,
http://linkedlifedata.com/resource/pubmed/chemical/PrPSc Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prions,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10516-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15632154-Acetylgalactosamine,
pubmed-meshheading:15632154-Animals,
pubmed-meshheading:15632154-Blotting, Western,
pubmed-meshheading:15632154-Brain,
pubmed-meshheading:15632154-Cell Line,
pubmed-meshheading:15632154-Cell Proliferation,
pubmed-meshheading:15632154-Chondroitin,
pubmed-meshheading:15632154-Chondroitin Sulfates,
pubmed-meshheading:15632154-DNA, Complementary,
pubmed-meshheading:15632154-Down-Regulation,
pubmed-meshheading:15632154-Gene Expression Regulation,
pubmed-meshheading:15632154-Glycosaminoglycans,
pubmed-meshheading:15632154-Glycosylation,
pubmed-meshheading:15632154-Heparitin Sulfate,
pubmed-meshheading:15632154-Immunohistochemistry,
pubmed-meshheading:15632154-Kinetics,
pubmed-meshheading:15632154-Mice,
pubmed-meshheading:15632154-Mice, Inbred C57BL,
pubmed-meshheading:15632154-Models, Biological,
pubmed-meshheading:15632154-Nucleic Acid Hybridization,
pubmed-meshheading:15632154-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:15632154-PrPSc Proteins,
pubmed-meshheading:15632154-Prions,
pubmed-meshheading:15632154-RNA,
pubmed-meshheading:15632154-RNA, Messenger,
pubmed-meshheading:15632154-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15632154-Sulfotransferases,
pubmed-meshheading:15632154-Time Factors,
pubmed-meshheading:15632154-Up-Regulation
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pubmed:year |
2005
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pubmed:articleTitle |
Glycosylation-related gene expression in prion diseases: PrPSc accumulation in scrapie infected GT1 cells depends on beta-1,4-linked GalNAc-4-SO4 hyposulfation.
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pubmed:affiliation |
Groupe d'Innovation Diagnostique et Thérapeutique des Infections à Prions, Commissariat à l'Energie Atomique, 18 route du Panorama, 92265, Fontenay-aux-Roses, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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