| First Author | Whitehouse IJ | Year | 2016 |
| Journal | PLoS One | Volume | 11 |
| Issue | 7 | Pages | e0159119 |
| PubMed ID | 27447728 | Mgi Jnum | J:249227 |
| Mgi Id | MGI:6094511 | Doi | 10.1371/journal.pone.0159119 |
| Citation | Whitehouse IJ, et al. (2016) Ablation of Prion Protein in Wild Type Human Amyloid Precursor Protein (APP) Transgenic Mice Does Not Alter The Proteolysis of APP, Levels of Amyloid-beta or Pathologic Phenotype. PLoS One 11(7):e0159119 |
| abstractText | The cellular prion protein (PrPC) has been proposed to play an important role in the pathogenesis of Alzheimer's disease. In cellular models PrPC inhibited the action of the beta-secretase BACE1 on wild type amyloid precursor protein resulting in a reduction in amyloid-beta (Abeta) peptides. Here we have assessed the effect of genetic ablation of PrPC in transgenic mice expressing human wild type amyloid precursor protein (line I5). Deletion of PrPC had no effect on the alpha- and beta-secretase proteolysis of the amyloid precursor protein (APP) nor on the amount of Abeta38, Abeta40 or Abeta42 in the brains of the mice. In addition, ablation of PrPC did not alter Abeta deposition or histopathology phenotype in this transgenic model. Thus using this transgenic model we could not provide evidence to support the hypothesis that PrPC regulates Abeta production. |
