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dc.creatorVARELA-NALLAR,LORENA
dc.creatorTOLEDO,ENRIQUE M
dc.creatorCHACÓN,MARCELO A
dc.creatorINESTROSA,NIBALDO C
dc.date2006-01-01
dc.date.accessioned2019-05-02T21:21:28Z
dc.date.available2019-05-02T21:21:28Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000100005
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/81617
dc.descriptionPrion diseases are fatal neurodegenerative disorders associated with the conversion of the cellular prion protein (PrPC) into a pathologic isoform. Although the physiological function of PrPC remains unknown, evidence relates PrPC to copper metabolism and oxidative stress as suggested by its copper-binding properties in the N-terminal octapeptide repeat region. This region also reduces copper ions in vitro, and this reduction ability is associated with the neuroprotection exerted by the octarepeat region against copper in vivo. In addition, the promoter region of the PrPC gene contains putative metal response elements suggesting it may be regulated by heavy metals. Here we address some of the evidence that support a physiological link between PrPC and copper. Also, in vivo experiments suggesting the physiological relevance of PrPC interaction with heparan sulfate proteoglycans are discussed.
dc.formattext/html
dc.languageen
dc.publisherSociedad de Biología de Chile
dc.relation10.4067/S0716-97602006000100005
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceBiological Research v.39 n.1 2006
dc.subjectPrion protein
dc.subjectcopper
dc.subjectheparin
dc.subjectHSPG
dc.subjectPrnp
dc.subjectMRE
dc.titleThe functional links between prion protein and copper


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