| First Author | Heilbronner G | Year | 2013 |
| Journal | EMBO Rep | Volume | 14 |
| Issue | 11 | Pages | 1017-22 |
| PubMed ID | 23999102 | Mgi Jnum | J:204530 |
| Mgi Id | MGI:5532773 | Doi | 10.1038/embor.2013.137 |
| Citation | Heilbronner G, et al. (2013) Seeded strain-like transmission of beta-amyloid morphotypes in APP transgenic mice. EMBO Rep 14(11):1017-22 |
| abstractText | The polymorphic beta-amyloid lesions present in individuals with Alzheimer's disease are collectively known as cerebral beta-amyloidosis. Amyloid precursor protein (APP) transgenic mouse models similarly develop beta-amyloid depositions that differ in morphology, binding of amyloid conformation-sensitive dyes, and Abeta40/Abeta42 peptide ratio. To determine the nature of such beta-amyloid morphotypes, beta-amyloid-containing brain extracts from either aged APP23 brains or aged APPPS1 brains were intracerebrally injected into the hippocampus of young APP23 or APPPS1 transgenic mice. APPPS1 brain extract injected into young APP23 mice induced beta-amyloid deposition with the morphological, conformational, and Abeta40/Abeta42 ratio characteristics of beta-amyloid deposits in aged APPPS1 mice, whereas APP23 brain extract injected into young APP23 mice induced beta-amyloid deposits with the characteristics of beta-amyloid deposits in aged APP23 mice. Injecting the two extracts into the APPPS1 host revealed a similar difference between the induced beta-amyloid deposits, although less prominent, and the induced deposits were similar to the beta-amyloid deposits found in aged APPPS1 hosts. These results indicate that the molecular composition and conformation of aggregated Abeta in APP transgenic mice can be maintained by seeded conversion. |
