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Apolipoprotein E enhances uptake of soluble but not aggregated amyloid‐β protein into synaptic terminals

Gylys, Karen H., Fein, Jeffrey A., Tan, Aiko M., Cole, Gregory M.·2003·Journal of Neurochemistry
DOI 10.1046/j.1471-4159.2003.01643.x
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Abstract

The cellular mechanism by which apolipoprotein E (apoE) affects the pathogenesis of Alzheimer's disease (AD) is not understood. We have examined the effect of apolipoprotein E on the internalization of exogenous amyloid‐β 1–40 (Aβ40) into a rat brain crude synaptosomal preparation. Aβ40 peptide in soluble (within 1 h of dilution in buffer) or aggregated (aged 4 days before dilution in buffer) form was pre‐incubated with lipidated apoE then added to synaptosomes; intraterminal amyloid‐β labeling was quantified using flow cytometry following immunolabeling with the anti‐Aβ (10G4) antibody. The number of Aβ‐positive synaptosomes was increased (∼50%) by treatment with a soluble Aβ/apoE mixture compared with treatment with soluble Aβ40 alone. However, when the Aβ was aggregated, less sodium dodecyl sulfate (SDS)‐stable Aβ/apoE complex was formed and the addition of apoE decreased the number of Aβ‐positive terminals. The addition of the lipoprotein‐receptor related protein (LRP) antagonist receptor‐associated protein (RAP) inhibited the apoE‐induced increase in synaptosomal Aβ, and controls treated with trypsin and heparinase confirm intraterminal localization of the majority of the soluble Aβ. The apoE‐mediated increase in Aβ labeling was confirmed in intact cells by immunocytochemistry of dorsal root ganglion (DRG) neurons. These results suggest that complex formation with apoE enhances internalization of soluble Aβ uptake into terminals.

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Metadata

Authors
Gylys, K. H., Fein, J. A., Tan, A. M., & Cole, G. M.
Venue
Journal of Neurochemistry
Publisher
Wiley
Published
2003-02-28
Volume
84
Issue
6
Pages
1442-1451
ISSN
  • 0022-3042
  • 1471-4159
DOI
10.1046/j.1471-4159.2003.01643.x
Cited by
70
References
7
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)

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