Peer-reviewed veterinary case report
Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain.
- Journal:
- Brain research
- Year:
- 2005
- Authors:
- Kokubo, Hideko et al.
- Affiliation:
- Gunma University School of Health Sciences · Japan
Abstract
We examined the ultrastructural localization of oligomeric proteins, Abeta42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1-immunoreactive rafts than Abeta42, suggesting that rafts are one of the sites of polymeric Abeta deposition, but not of oligomeric proteins including Abeta.
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Search related cases →Original publication: https://pubmed.ncbi.nlm.nih.gov/15910781/