Lipofuscin and Aβ42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains

Michael R. D'Andrea, Robert G. Nagele, Norah A. Gumula, Patti A. Reiser, Deborah A. Polkovitch, Brenda M. Hertzog, Patricia Andrade-Gordon

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

Our recent study has provided evidence that Aβ42, 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 Aβ42 co-localizes with lipofuscin in neurons and those increased levels of lipofuscin and Aβ42 are associated with AD. Other studies have questioned this relationship and suggested that β-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 Aβ42 and lipofuscin in AD brains tissue using a novel combined immunohistochemical:histochemical staining protocol. Our results show separate and distinct localization patterns of Aβ42 and lipofuscin in neurons and amyloid plaques.

Original languageEnglish (US)
Pages (from-to)45-49
Number of pages5
JournalNeuroscience Letters
Volume323
Issue number1
DOIs
StatePublished - Apr 19 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

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