Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain

Hideko Kokubo, Rakez Kayed, Charles G. Glabe, Takaomi C. Saido, Nobuhisa Iwata, J. Bernd Helms, Haruyasu Yamaguchi

Research output: Contribution to journalArticle

17 Scopus citations


We examined the ultrastructural localization of oligomeric proteins, Aβ42, 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 Aβ42, suggesting that rafts are one of the sites of polymeric Aβ deposition, but not of oligomeric proteins including Aβ.

Original languageEnglish (US)
Pages (from-to)224-228
Number of pages5
JournalBrain Research
Issue number1-2
StatePublished - May 31 2005
Externally publishedYes



  • Alzheimer's disease
  • Amyloid-β
  • Flotillin-1
  • Oligomer
  • Raft
  • Tg2576 mouse

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this