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Alzheimer's disease (AD) is characterized by cerebral proteinaceous deposits comprised of amyloid beta (Aβ). Evidence suggests that enhanced blood-to-brain delivery of Aβ occurs when plasma concentration is increased, exacerbating amyloidosis. In blood, significant Aβ is associated with apolipoprotein (apo) B lipoproteins. In this study, immunofluorescent microscopy was utilised to explore if there is an association between apo B lipoproteins and proteoglycan expression within Aβ-rich plaques in transgenic-amyloid mice. Focal accumulation of apo B was found with Aβ-plaque in APP/PS1 mice. There was enrichment in the proteoglycans, agrin, perlecan, biglycan and decorin within the core of dense Aβ-plaque. Perlecan, biglycan and decorin were positively associated with apo B lipoprotein abundance within amyloid plaque consistent with a cause-for-retention effect. These findings show that proteoglycans are an integral component of Aβ deposits in APP/PS1 mice. This study suggests that some proteoglycans contribute to Aβ retention, whilst other proteoglycans have different functions in the aetiology of AD.

Original publication

DOI

10.1016/j.neulet.2011.02.001

Type

Journal article

Journal

Neurosci Lett

Publication Date

04/04/2011

Volume

492

Pages

160 - 164

Keywords

Agrin, Alzheimer Disease, Amyloid beta-Peptides, Animals, Apolipoproteins B, Biglycan, Cerebral Cortex, Decorin, Disease Models, Animal, Heparan Sulfate Proteoglycans, Male, Mice, Mice, Inbred C57BL, Mice, Transgenic, Plaque, Amyloid, Proteoglycans