Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain.
Prion diseases induce neurodegeneration in specific brain areas for undetermined reasons. A thorough understanding of the localization of the disease-causing molecule, the prion protein (PrP), could inform on this issue but previous studies have generated conflicting conclusions. One of the more int...
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doaj-27d8713a470f4f3e94e5a1e3414124d42020-11-24T22:00:06ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0194e9595810.1371/journal.pone.0095958Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain.Walker S JacksonClemens KrostAndrew W BorkowskiLech KaczmarczykPrion diseases induce neurodegeneration in specific brain areas for undetermined reasons. A thorough understanding of the localization of the disease-causing molecule, the prion protein (PrP), could inform on this issue but previous studies have generated conflicting conclusions. One of the more intriguing disagreements is whether PrP is synthesized by astrocytes. We developed a knock-in reporter mouse line in which the coding sequence of the PrP expressing gene (Prnp), was replaced with that for green fluorescent protein (GFP). Native GFP fluorescence intensity varied between and within brain regions. GFP was present in astrocytes but did not increase during reactive gliosis induced by scrapie prion infection. Therefore, reactive gliosis associated with prion diseases does not cause an acceleration of local PrP production. In addition to aiding in Prnp gene activity studies, this reporter mouse line will likely prove useful for analysis of chimeric animals produced by stem cell and tissue transplantation experiments.http://europepmc.org/articles/PMC3994155?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Walker S Jackson Clemens Krost Andrew W Borkowski Lech Kaczmarczyk |
spellingShingle |
Walker S Jackson Clemens Krost Andrew W Borkowski Lech Kaczmarczyk Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. PLoS ONE |
author_facet |
Walker S Jackson Clemens Krost Andrew W Borkowski Lech Kaczmarczyk |
author_sort |
Walker S Jackson |
title |
Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. |
title_short |
Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. |
title_full |
Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. |
title_fullStr |
Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. |
title_full_unstemmed |
Translation of the prion protein mRNA is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. |
title_sort |
translation of the prion protein mrna is robust in astrocytes but does not amplify during reactive astrocytosis in the mouse brain. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2014-01-01 |
description |
Prion diseases induce neurodegeneration in specific brain areas for undetermined reasons. A thorough understanding of the localization of the disease-causing molecule, the prion protein (PrP), could inform on this issue but previous studies have generated conflicting conclusions. One of the more intriguing disagreements is whether PrP is synthesized by astrocytes. We developed a knock-in reporter mouse line in which the coding sequence of the PrP expressing gene (Prnp), was replaced with that for green fluorescent protein (GFP). Native GFP fluorescence intensity varied between and within brain regions. GFP was present in astrocytes but did not increase during reactive gliosis induced by scrapie prion infection. Therefore, reactive gliosis associated with prion diseases does not cause an acceleration of local PrP production. In addition to aiding in Prnp gene activity studies, this reporter mouse line will likely prove useful for analysis of chimeric animals produced by stem cell and tissue transplantation experiments. |
url |
http://europepmc.org/articles/PMC3994155?pdf=render |
work_keys_str_mv |
AT walkersjackson translationoftheprionproteinmrnaisrobustinastrocytesbutdoesnotamplifyduringreactiveastrocytosisinthemousebrain AT clemenskrost translationoftheprionproteinmrnaisrobustinastrocytesbutdoesnotamplifyduringreactiveastrocytosisinthemousebrain AT andrewwborkowski translationoftheprionproteinmrnaisrobustinastrocytesbutdoesnotamplifyduringreactiveastrocytosisinthemousebrain AT lechkaczmarczyk translationoftheprionproteinmrnaisrobustinastrocytesbutdoesnotamplifyduringreactiveastrocytosisinthemousebrain |
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