PMID: 11911987Mar 26, 2002Paper

Lipofuscin and Abeta42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains

Neuroscience Letters
Michael R D'AndreaPatricia Andrade-Gordon

Abstract

Our recent study has provided evidence that Abeta42, a 42 amino acid fragment of the amyloid precursor protein, accumulates intracellularly in vulnerable neurons. This study appears to show that neurons lyse and form dense-core amyloid plaques in Alzheimer's disease (AD) entorhinal cortex. Previous studies have suggested that intracellular Abeta42 co-localizes with lipofuscin in neurons and those increased levels of lipofuscin and Abeta42 are associated with AD. Other studies have questioned this relationship and suggested that beta-amyloid and lipofuscin are not co-localized and that their levels are independent of one another in AD and age-matched control tissues. In an effort to resolve this controversy, we investigated the relative spatial relationship of intracellular Abeta42 and lipofuscin in AD brains tissue using a novel combined immunohistochemical:histochemical staining protocol. Our results show separate and distinct localization patterns of Abeta42 and lipofuscin in neurons and amyloid plaques.

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Citations

Nov 27, 2007·Acta Neuropathologica·Charles DuyckaertsBenoît Delatour
Apr 22, 2009·Acta Neuropathologica·Charles DuyckaertsMarie-Claude Potier
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Sep 25, 2007·Progress in Neurobiology·Meng LiYan Zhang
Nov 29, 2008·Free Radical Biology & Medicine·Lin ZhengAlexei Terman

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