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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alzheimer Disease / genetics
-
Alzheimer Disease / metabolism*
-
Alzheimer Disease / pathology
-
Amyloid beta-Peptides / metabolism*
-
Amyloid beta-Protein Precursor / metabolism
-
Animals
-
Axons / metabolism*
-
Axons / pathology
-
Axons / ultrastructure
-
Brain / metabolism*
-
Brain / pathology
-
Brain / ultrastructure
-
Disease Models, Animal
-
Membrane Microdomains / metabolism*
-
Membrane Microdomains / pathology
-
Membrane Microdomains / ultrastructure
-
Membrane Proteins / metabolism*
-
Mice
-
Mice, Transgenic
-
Microscopy, Immunoelectron
-
Peptide Fragments / metabolism*
-
Plaque, Amyloid / metabolism
-
Plaque, Amyloid / pathology
-
Plaque, Amyloid / ultrastructure
Substances
-
Amyloid beta-Peptides
-
Amyloid beta-Protein Precursor
-
Membrane Proteins
-
Peptide Fragments
-
amyloid beta-protein (1-42)
-
flotillins