Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain.
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.
Kokubo
Hideko
H
Gunma University School of Health Sciences, 3-39-15 Showa-machi, Maebashi 371-8514, Japan.
Kayed
Rakez
R
Glabe
Charles G
CG
Saido
Takaomi C
TC
Iwata
Nobuhisa
N
Helms
J Bernd
JB
Yamaguchi
Haruyasu
H
D000544:Alzheimer Disease / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D016564:Amyloid beta-Protein Precursor / Q000378:metabolism; D000818:Animals; D001369:Axons / Q000378:metabolism* / Q000473:pathology / Q000648:ultrastructure; D001921:Brain / Q000378:metabolism* / Q000473:pathology / Q000648:ultrastructure; D004195:Disease Models, Animal; D021962:Membrane Microdomains / Q000378:metabolism* / Q000473:pathology / Q000648:ultrastructure; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D008822:Mice, Transgenic; D016253:Microscopy, Immunoelectron; D010446:Peptide Fragments / Q000378:metabolism*; D058225:Plaque, Amyloid / Q000378:metabolism / Q000473:pathology / Q000648:ultrastructure
D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D008565:Membrane Proteins; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42); C106354:flotillins