| First Author | Wirths O | Year | 2017 |
| Journal | Alzheimers Res Ther | Volume | 9 |
| Issue | 1 | Pages | 80 |
| PubMed ID | 28978359 | Mgi Jnum | J:285070 |
| Mgi Id | MGI:6392945 | Doi | 10.1186/s13195-017-0309-z |
| Citation | Wirths O, et al. (2017) N-truncated Abeta4-x peptides in sporadic Alzheimer's disease cases and transgenic Alzheimer mouse models. Alzheimers Res Ther 9(1):80 |
| abstractText | BACKGROUND: The deposition of neurotoxic amyloid-beta (Abeta) peptides in plaques in the brain parenchyma and in cerebral blood vessels is considered to be a key event in Alzheimer's disease (AD) pathogenesis. Although the presence and impact of full-length Abeta peptides such as Abeta1-40 and Abeta1-42 have been analyzed extensively, the deposition of N-terminally truncated Abeta peptide species has received much less attention, largely because of the lack of specific antibodies. METHODS: This paper describes the generation and characterization of novel antibodies selective for Abeta4-x peptides and provides immunohistochemical evidence of Abeta4-x in the human brain and its distribution in the APP/PS1KI and 5XFAD transgenic mouse models. RESULTS: The Abeta4-x staining pattern was restricted mainly to amyloid plaque cores and cerebral amyloid angiopathy in AD and Down syndrome cases and in both AD mouse models. In contrast, diffuse amyloid deposits were largely negative for Abeta4-x immunoreactivity. No overt intraneuronal staining was observed. CONCLUSIONS: The findings of this study are consistent with previous reports demonstrating a high aggregation propensity of Abeta4-x peptides and suggest an important role of these N-truncated Abeta species in the process of amyloidogenesis and plaque core formation. |
