Affiliations: [a] A.I. Virtanen Institute, University of Eastern Finland, Kuopio, Finland
| [b] Neuroscience Center, University of Helsinki, Helsinki, Finland
| [c]
Institute of Theoretical & Experimental Biophysics, RAS, Pushchino, Russia | [d] Neurotar Ltd, Helsinki, Finland, http://www.neurotar.com
Correspondence:
[*]
Correspondence to: Irina Gureviciene, PhD, Department of Neurobiology, A.I. Virtanen Institute for Molecular Sciences, University of Eastern Finland (Kuopio Campus), Bioteknia 1 (Neulaniementie 2), P.O. Box 1627, 70211 Kuopio, Finland. Tel.: +358 505265084; Fax: +358 17 163030; E-mail: Irina.Gureviciene@uef.fi.
Abstract: Amyloid plaques, although inducing damage to the immediately surrounding neuropil, have been proposed to provide a relatively innocuous way to deposit toxic soluble amyloid-β (Aβ) species. Here we address this hypothesis by exploring spread and absorption of fluorescent Aβ to pre-existing amyloid plaques after local application in wild-type mice versus APP/PS1 transgenic mice with amyloid plaques. Local intracortical or intracerebroventricular injection of fluorescently-labeled Aβ in APP/PS1 mice with a high plaque density resulted in preferential accumulation of the peptide in amyloid plaques in both conventional postmortem histology and in live imaging using two-photon microscopy. These findings support the contention that amyloid plaques may act as buffers to protect neurons from the toxic effects of momentary high concentrations of soluble Aβ oligomers.
Keywords: Alzheimer’s disease, amyloid-β, in vivo imaging, multiphoton, transgenic
