Publication: Electron microscopic 3D reconstruction analysis of amyloid deposits in 3xTg-AD mice and aged canines
Issued Date
2011-12-01
Resource Type
ISSN
22105735
22105727
22105727
Other identifier(s)
2-s2.0-84865482765
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Advances in Alzheimer's Disease. Vol.1, (2011), 149-162
Suggested Citation
Paworn Nuntagij, Naiphinich Kotchabhakdi, Reidun Torp Electron microscopic 3D reconstruction analysis of amyloid deposits in 3xTg-AD mice and aged canines. Advances in Alzheimer's Disease. Vol.1, (2011), 149-162. doi:10.3233/978-1-60750-733-8-149 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/12180
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Electron microscopic 3D reconstruction analysis of amyloid deposits in 3xTg-AD mice and aged canines
Other Contributor(s)
Abstract
Little is known about how amyloid-β (Aβ) is deposited in relation to the complex ultrastructure of the brain. Here we combined serial section immunoelectron microscopy with 3D reconstruction to elucidate the spatial relationship between Aβ deposits and ultrastructurally identified cellular compartments. The analysis was performed in a transgenic mouse model with mutant presenilin-1, and mutant amyloid-β protein precursor (AβPP) and tau transgenes (3xTg-AD mice) and in aged dogs that develop Aβ plaques spontaneously. Reconstructions based on serial ultrathin sections of hippocampus (mice) or neocortex (dogs) that had been immunolabeled with Aβ (Aβ1-42) antibodies showed that the organization of extracellular Aβ deposits is more complex than anticipated from light microscopic analyses. In both species, deposits were tightly associated with plasma membranes of pyramidal cell bodies and major dendrites. The deposits typically consisted of thin sheets as well as slender tendrils that climbed along the large caliber dendritic stems of pyramidal neurons. No preferential association was observed between Aβ deposits and thin dendritic branches or spines, nor was there any evidence of preferential accumulation of Aβ around synaptic contacts or glial processes. Our data suggest that plaque formation is a precisely orchestrated process that involves specialized domains of dendrosomatic plasma membranes. © 2011 The authors and IOS Press. All rights reserved.