| Literature DB >> 29676205 |
Giuseppe Legname1,2, Tommaso Virgilio3,4, Edoardo Bistaffa1,3, Chiara Maria Giulia De Luca3, Marcella Catania3, Paola Zago1, Elisa Isopi1, Ilaria Campagnani3, Fabrizio Tagliavini3, Giorgio Giaccone3, Fabio Moda3.
Abstract
Pin1 is a peptidyl-prolyl isomerase that induces the cis-trans conversion of specific Ser/Thr-Pro peptide bonds in phosphorylated proteins, leading to conformational changes through which Pin1 regulates protein stability and activity. Since down-regulation of Pin1 has been described in several neurodegenerative disorders, including Alzheimer's Disease (AD), Parkinson's Disease (PD) and Huntington's Disease (HD), we investigated its potential role in prion diseases. Animals generated on wild-type (Pin1+/+), hemizygous (Pin1+/-) or knock-out (Pin1-/-) background for Pin1 were experimentally infected with RML prions. The study indicates that, neither the total depletion nor reduced levels of Pin1 significantly altered the clinical and neuropathological features of the disease.Entities:
Keywords: PMCA; Pin1; neurodegeneration; prion
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Year: 2018 PMID: 29676205 PMCID: PMC6016513 DOI: 10.1080/19336896.2018.1464367
Source DB: PubMed Journal: Prion ISSN: 1933-6896 Impact factor: 3.931