Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/28285
Title: Amyloid deposits show complexity and intimate spatial relationship with dendrosomatic plasma membranes: An electron microscopic 3D reconstruction analysis in 3xTg-AD mice and aged canines
Authors: Paworn Nuntagij
Salvatore Oddo
Frank M. LaFerla
Naiphinich Kotchabhakdi
Ole P. Ottersen
Reidun Torp
Universitetet i Oslo
The Institute of Science and Technology for Research and Development, Mahidol University
University of Texas Health Science Center at San Antonio
University of California, Irvine
Keywords: Medicine;Psychology
Issue Date: 1-Jan-2009
Citation: Journal of Alzheimer's Disease. Vol.16, No.2 (2009), 315-323
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. © 2009 - IOS Press and the authors. All rights reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=60349123706&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/28285
ISSN: 13872877
Appears in Collections:Scopus 2006-2010

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.