| First Author | Xu G | Year | 2015 |
| Journal | Acta Neuropathol Commun | Volume | 3 |
| Pages | 72 | PubMed ID | 26566997 |
| Mgi Jnum | J:340366 | Mgi Id | MGI:6838794 |
| Doi | 10.1186/s40478-015-0252-9 | Citation | Xu G, et al. (2015) Murine Abeta over-production produces diffuse and compact Alzheimer-type amyloid deposits. Acta Neuropathol Commun 3:72 |
| abstractText | INTRODUCTION: Transgenic overexpression of amyloid precursor protein (APP) genes that are either entirely human in sequence or have humanized Abeta sequences can produce Alzheimer-type amyloidosis in mice, provided the transgenes also encode mutations linked to familial Alzheimer's Disease (FAD). Although transgenic mice have been produced that overexpress wild-type mouse APP, no mice have been generated that express mouse APP with FAD mutations. Here we describe two different versions of such mice that produce amyloid deposits consisting of entirely of mouse Abeta peptides. One line of mice co-expresses mouse APP-Swedish (moAPPswe) with a human presenilin exon-9 deleted variant (PS1dE9) and another line expresses mouse APP-Swedish/Indiana (APPsi) using tetracycline-regulated vectors (tet.moAPPsi). RESULTS: Both lines of mice that produce mouse Abeta develop amyloid deposits, with the moAPPswe/PS1dE9 mice developing extracellular compact, cored, neuritic deposits that primarily localize to white matter tracts and meningial layers, whereas the tet.moAPPsi mice developed extracellular diffuse cortical/hippocampal deposits distributed throughout the parenchyma. CONCLUSIONS: These findings demonstrate that murine Abeta peptides have the capacity to produce amyloid deposits that are morphologically similar to deposits found in human AD provided the murine APP gene harbors mutations linked to human FAD. |
