| First Author | Liu P | Year | 2024 |
| Journal | iScience | Volume | 27 |
| Issue | 3 | Pages | 109239 |
| PubMed ID | 38433923 | Mgi Jnum | J:347916 |
| Mgi Id | MGI:7611459 | Doi | 10.1016/j.isci.2024.109239 |
| Citation | Liu P, et al. (2024) Abeta *56 is a stable oligomer that impairs memory function in mice. iScience 27(3):109239 |
| abstractText | Amyloid-beta (Abeta) oligomers consist of fibrillar and non-fibrillar soluble assemblies of the Abeta peptide. Abeta *56 is a non-fibrillar Abeta assembly that is linked to memory deficits. Previous studies did not decipher specific forms of Abeta present in Abeta *56. Here, we confirmed the memory-impairing characteristics of Abeta *56 and extended its biochemical characterization. We used anti-Abeta(1-x), anti-Abeta(x-40), anti-Abeta(x-42), and A11 anti-oligomer antibodies in conjunction with western blotting, immunoaffinity purification, and size-exclusion chromatography to probe aqueous brain extracts from Tg2576, 5xFAD, and APP/TTA mice. In Tg2576, Abeta *56 is a approximately 56-kDa, SDS-stable, A11-reactive, non-plaque-dependent, water-soluble, brain-derived oligomer containing canonical Abeta(1-40). In 5xFAD, Abeta *56 is composed of Abeta(1-42), whereas in APP/TTA, it contains both Abeta(1-40) and Abeta(1-42). When injected into the hippocampus of wild-type mice, Abeta *56 derived from Tg2576 mice impairs memory. The unusual stability of this oligomer renders it an attractive candidate for studying relationships between molecular structure and effects on brain function. |
