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

Kokubo, Hideko, Kayed, Rakez, Glabe, Charles G., Saido, Takaomi C., Iwata, Nobuhisa, Helms, J. Bernd, Yamaguchi, Haruyasu·2005·Brain Research

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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Crossref · 10.1016/j.brainres.2005.03.017

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Research works printed but not linked: 15

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Metadata

Authors
Kokubo, H., Kayed, R., Glabe, C. G., Saido, T. C., Iwata, N., Helms, J. B., & Yamaguchi, H.
Venue
Brain Research
Publisher
Elsevier BV
Published
2005-05
Volume
1045
Issue
1-2
Pages
224-228
ISSN
0006-8993
Cited by
16
References
1
Language
en
Funders
Ministry of Education, Culture, Sports, Science and Technology

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