\(A\beta\) alters the connectivity of olfactory neurons in the absence of amyloid plaques in vivo

DSpace/Manakin Repository

\(A\beta\) alters the connectivity of olfactory neurons in the absence of amyloid plaques in vivo

Citable link to this page

 

 
Title: \(A\beta\) alters the connectivity of olfactory neurons in the absence of amyloid plaques in vivo
Author: Cao, Luxiang; Schrank, Benjamin R.; Rodriguez, Steven; Benz, Eric G.; Moulia, Thomas W.; Rickenbacher, Gregory T.; Gomez, Alexis C.; Levites, Yona; Edwards, Sarah R.; Golde, Todd E.; Hyman, Bradley Theodore; Barnea, Gilad; Albers, Mark W

Note: Order does not necessarily reflect citation order of authors.

Citation: Cao, Luxiang, Benjamin R. Schrank, Steven Rodriguez, Eric G. Benz, Thomas W. Moulia, Gregory T. Rickenbacher, Alexis C. Gomez, et al. 2012. \(A\beta\) alters the connectivity of olfactory neurons in the absence of amyloid plaques in vivo. Nature Communications 3(8): 1009.
Full Text & Related Files:
Abstract: The amyloid beta peptide aggregates into amyloid plaques at presymptomatic stages of Alzheimer's disease, but the temporal relationship between plaque formation and neuronal dysfunction is poorly understood. Here we demonstrate that the connectivity of the peripheral olfactory neural circuit is perturbed in mice overexpressing human APPsw (Swedish mutation) before the onset of plaques. Expression of human APPsw exclusively in olfactory sensory neurons also perturbs connectivity with associated reductions in odour-evoked gene expression and olfactory acuity. By contrast, olfactory sensory neuron axons project correctly in mice overexpressing wild-type human amyloid precursor protein throughout the brain and in mice overexpressing M671V human APP, a missense mutation that reduces amyloid beta production, exclusively in olfactory sensory neurons. Furthermore, expression of Aβ40 or Aβ42 solely in the olfactory epithelium disrupts the olfactory sensory neuron axon targeting. Our data indicate that altering the structural connectivity and function of highly plastic neural circuits is one of the pleiotropic actions of soluble human amyloid beta.
Published Version: doi:10.1038/ncomms2013
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3529477/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:10579035
Downloads of this work:

Show full Dublin Core record

This item appears in the following Collection(s)

 
 

Search DASH


Advanced Search
 
 

Submitters