| Literature DB >> 23747948 |
Jeffrey L Frost1, Kevin X Le, Holger Cynis, Elizabeth Ekpo, Martin Kleinschmidt, Roberta M Palmour, Frank R Ervin, Shikha Snigdha, Carl W Cotman, Takaomi C Saido, Robert J Vassar, Peter St George-Hyslop, Tsuneya Ikezu, Stephan Schilling, Hans-Ulrich Demuth, Cynthia A Lemere.
Abstract
Amyloid-β (Aβ) peptides, starting with pyroglutamate at the third residue (pyroGlu-3 Aβ), are a major species deposited in the brain of Alzheimer disease (AD) patients. Recent studies suggest that this isoform shows higher toxicity and amyloidogenecity when compared to full-length Aβ peptides. Here, we report the first comprehensive and comparative IHC evaluation of pyroGlu-3 Aβ deposition in humans and animal models. PyroGlu-3 Aβ immunoreactivity (IR) is abundant in plaques and cerebral amyloid angiopathy of AD and Down syndrome patients, colocalizing with general Aβ IR. PyroGlu-3 Aβ is further present in two nontransgenic mammalian models of cerebral amyloidosis, Caribbean vervets, and beagle canines. In addition, pyroGlu-3 Aβ deposition was analyzed in 12 different AD-like transgenic mouse models. In contrast to humans, all transgenic models showed general Aβ deposition preceding pyroGlu-3 Aβ deposition. The findings varied greatly among the mouse models concerning age of onset and cortical brain region. In summary, pyroGlu-3 Aβ is a major species of β-amyloid deposited early in diffuse and focal plaques and cerebral amyloid angiopathy in humans and nonhuman primates, whereas it is deposited later in a subset of focal and vascular amyloid in AD-like transgenic mouse models. Given the proposed decisive role of pyroGlu-3 Aβ peptides for the development of human AD pathology, this study provides insights into the usage of animal models in AD studies.Entities:
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Year: 2013 PMID: 23747948 PMCID: PMC3730768 DOI: 10.1016/j.ajpath.2013.05.005
Source DB: PubMed Journal: Am J Pathol ISSN: 0002-9440 Impact factor: 4.307