Linked Life Data

18602368

Source:http://linkedlifedata.com/resource/pubmed/id/18602368

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-7-30
pubmed:abstractText
Neurodegenerative disorders such as Alzheimer's, Huntington's, and prion diseases are characterized by abnormal protein deposits in the brain of affected patients. In prion diseases, a key event in the pathogenesis is the conversion of the normal prion protein (PrP(c)) into abnormal protease resistant PrP(Sc) deposits, a phenomenon associated with a higher sensitivity to oxidative stress in vitro. In cellular models of Alzheimer and Huntington diseases, the disaccharide trehalose has been shown to be effective in inhibiting huntingtin and Abeta peptide aggregates and reducing their associated toxicity. We show in this study that trehalose treatment of prion-infected cells decreases the size of de novo produced PrP(Sc) aggregates and modify their subcellular localization. Despite the fact that trehalose does not modify the protease resistance properties of PrP(Sc) molecules, it significantly protects prion-infected cells from induced oxidative damage, suggesting that this compound is of therapeutic interest.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
12
pubmed:volume
374
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
44-8
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage.
pubmed:affiliation
Institut de Génétique Humaine, UPR CNRS1142, 141 Rue de Cardonille, 34396 Montpellier Cedex 5, France. inserm-usa@ambafrance-us.org
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't