Lipofuscin and Abeta42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains.
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.
D'Andrea
Michael R
MR
The R.W. Johnson Pharmaceutical Research Institute, Drug Discovery, Spring House, PA 19477, USA. mdandrea@prius.jnj.com
Nagele
Robert G
RG
Gumula
Norah A
NA
Reiser
Patti A
PA
Polkovitch
Deborah A
DA
Hertzog
Brenda M
BM
Andrade-Gordon
Patricia
P
D000368:Aged; D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology*; D016229:Amyloid beta-Peptides / Q000032:analysis*; D016564:Amyloid beta-Protein Precursor / Q000032:analysis; D006801:Humans; D007150:Immunohistochemistry; D008062:Lipofuscin / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D012016:Reference Values
D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D008062:Lipofuscin; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)