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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
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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“findings that oligomeric A deposits are present preferentially on distal axons and synapses in Tg2576 mouse brain and in central nervous system-derived neuronal cells suggested that these structures are important sites of A entry (14,32).”
From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [14]
In the citing paper
“Deposits of oligomeric A are preferentially found on distal axons and synapses in mouse brains suggesting that these structures might represent the cellular entry points for A (14).”
From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [14]
In the citing paper
“suggested that these structures are important sites of A entry (14,32).”
From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [14]
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Cited by
Sorted by citations
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783
Self-citationInternalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E
Saavedra, L., Mohamed, A., Ma, V., Kar, S., & de Chaves, E. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701823200 · Cited by 118
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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- Kokubo, H., Kayed, R., Glabe, C. G., Saido, T. C., Iwata, N., Helms, J. B., & Yamaguchi, H. (2005). Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain. Brain Research. https://doi.org/10.1016/j.brainres.2005.03.017
