Abeta*56 is a stable oligomer that correlates with age-related memory loss in Tg2576 mice
Ashe, K.; Liu, P.; Lapcinski, I.; Shapiro, S.; Kemper, L.
Show abstract
Amyloid-{beta} (A{beta}) oligomers consist of fibrillar and non-fibrillar soluble assemblies of the A{beta} peptide. Tg2576 human amyloid precursor protein (APP)-expressing transgenic mice modeling Alzheimers disease produce A{beta}*56, a non-fibrillar A{beta} assembly that has been shown by several groups to relate more closely to memory deficits than plaques. Previous studies did not decipher specific forms of A{beta} present in A{beta}*56. Here, we confirm and extend the biochemical characterization of A{beta}*56. We used anti-A{beta}(1-x), anti-A{beta}(x-40), and A11 anti-oligomer antibodies in conjunction with western blotting, immunoaffinity purification, and size-exclusion chromatography to probe aqueous brain extracts from Tg2576 mice of different ages. We found that A{beta}*56 is a [~]56-kDa, SDS-stable, A11-reactive, non-plaque-related, water-soluble, brain-derived oligomer containing canonical A{beta}(1-40) that correlates with age-related memory loss. The unusual stability of this high molecular-weight oligomer renders it an attractive candidate for studying relationships between molecular structure and effects on brain function.
Matching journals
The top 10 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Wild-type sTREM2 blocks Aβ aggregation and neurotoxicity, while the Alzheimer's R47H mutant does the opposite 94%
- The inhibition of cellular toxicity of amyloid-beta by dissociated transthyretin 93%
- Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau 93%
Similar papers in this journal
- Tauopathy in the APPswe/PS1ΔE9 mouse model of familial Alzheimer’s disease 94%
- Improvement of glymphatic-lymphatic drainage of beta-amyloid by focused ultrasound in Alzheimer's disease model 94%
- Genetic dissection of Down syndrome-associated alterations in APP/amyloid-β biology using mouse models 93%
Similar papers in this journal
- Divergent age-dependent conformational rearrangement within Aβ-amyloid deposits in APP23, APPPS1, and AppNL-F mice 95%
- Fast purification of recombinant monomeric amyloid-β from E. coli and amyloid-β-mCherry aggregates from mammalian cells 94%
- The double-layered structure of amyloid-β assemblage on GM1-containing membranes catalytically promotes fibrillization 92%
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.