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Presenilin-1 C410Y Alzheimer Disease Plaques Contain Synaptic Proteins
Journal article   Open access   Peer reviewed

Presenilin-1 C410Y Alzheimer Disease Plaques Contain Synaptic Proteins

Kamran Haleem, Carol F. Lippa, Thomas W. Smith, Hisatomo Kowa, Jianlin Wu and Takeshi Iwatsubo
American journal of Alzheimer's disease and other dementias, v 22(2), pp 137-144
Apr 2007
DOI: https://doi.org/10.1177/1533317506298051
PMID: 17545141
url
https://doi.org/10.1177/1533317506298051View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze),  Open

Abstract

Presenilin-1 (PS-1) mutations are associated with familial Alzheimer's disease (AD). Although beta-amyloid (Aβ) plaques in brain tissue are characteristic of AD patients, space occupying “cotton-wool” plaques (CWPs) lacking dense Aβ cores have also been described in patients with mutations in exon 9 of the PS-1 gene. The composition of CWPs has not been fully described. To better elucidate the composition of these space-occupying plaques, we used immunohistochemistry with antibodies to the synaptic proteins synapsin-1 and synaptophysin, as well as antibodies to tau, Aβ -42 , Aβ -40 , ubiquitin, neurofilament, and glial fibrillary acidic protein. Confocal laser scanning microscopy (CLSM) was utilized to further characterize these plaques. CWPs showed increased synapsin-1 and synaptophysin immunoreactivity relative to the background gray matter. Synaptic protein-containing CWPs occurred in all affected MTL regions, including the granule cell layer of the dentate gyrus, where synaptic terminals are usually sparse. These data suggest that in C410Y PS-1 AD patients, CWPs may constitute a major component of synaptic terminal-specific proteins, and that the C410Y PS-1 mutation may influence either synaptic structure or synaptic protein expression.

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