Linked Life Data

12500977

Source:http://linkedlifedata.com/resource/pubmed/id/12500977

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2003-3-10
pubmed:abstractText
The N-terminal region of the prion protein PrP(C) contains a series of octapeptide repeats. This region has been implicated in the binding of divalent metal ions, particularly copper. PrP(C) has been suggested to be involved in copper transport and metabolism and in cell defense mechanisms against oxidative insult, possibly through the regulation of the intracellular CuZn superoxide dismutase activity (CuZn-SOD) or a SOD-like activity of PrP(C) itself. However, up to now the link between PrP(C) expression and copper metabolism or SOD activity has still to be formally established; particularly because conflicting results have been obtained in vivo. In this study, we report a link between PrP(C), copper binding, and resistance to oxidative stress. Radioactive copper ((64)Cu) was used at a physiological concentration to demonstrate that binding of copper to the outer plasma cell membrane is related to the level of PrP(C) expression in a cell line expressing a doxycycline-inducible murine PrP(C) gene. Cellular PIPLC pretreatment indicated that PrP(C) was not involved in copper delivery at physiological concentrations. We also demonstrated that murine PrP(C) expression increases several antioxidant enzyme activities and glutathione levels. Prion protein may be a stress sensor sensitive to copper and able to initiate, following copper binding, a signal transduction process acting on the antioxidant systems to improve cell defenses.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9064-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12500977-Animals, pubmed-meshheading:12500977-Antioxidants, pubmed-meshheading:12500977-Blotting, Western, pubmed-meshheading:12500977-Cell Membrane, pubmed-meshheading:12500977-Cell Survival, pubmed-meshheading:12500977-Copper, pubmed-meshheading:12500977-Dose-Response Relationship, Drug, pubmed-meshheading:12500977-Doxycycline, pubmed-meshheading:12500977-Glutathione, pubmed-meshheading:12500977-Glutathione Peroxidase, pubmed-meshheading:12500977-Lipid Peroxidation, pubmed-meshheading:12500977-Manganese, pubmed-meshheading:12500977-Mice, pubmed-meshheading:12500977-Microscopy, Fluorescence, pubmed-meshheading:12500977-Molsidomine, pubmed-meshheading:12500977-Oxidative Stress, pubmed-meshheading:12500977-Prions, pubmed-meshheading:12500977-Protein Binding, pubmed-meshheading:12500977-Signal Transduction, pubmed-meshheading:12500977-Superoxide Dismutase, pubmed-meshheading:12500977-Time Factors
pubmed:year
2003
pubmed:articleTitle
Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery.
pubmed:affiliation
Laboratoire de Biologie du Stress Oxydant (LBSO), Faculté de Pharmacie, Domaine de La Merci, 38706 La Tronche-Grenoble cedex 9, France. walid.rachidi@ujf-grenoble.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't