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Related Experiment Video

Updated: Dec 2, 2025

Differential Labeling of Cell-surface and Internalized Proteins after Antibody Feeding of Live Cultured Neurons

Differential Labeling of Cell-surface and Internalized Proteins after Antibody Feeding of Live Cultured Neurons

Published on: February 12, 2014

Evidence for aggregation-independent, PrP^C-mediated Aβ cellular internalization.

Alejandro R Foley¹, Graham P Roseman¹, Ka Chan¹

¹Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064.

Proceedings of the National Academy of Sciences of the United States of America

|November 3, 2020

Summary

Amyloid beta (Aβ) uptake by neurons is receptor-mediated and sequence-specific, involving the prion protein (PrP^C). Targeting these receptors may offer new Alzheimer's disease therapies.

Keywords:

Alzheimer’s disease amyloid β mirror-image peptides prion protein (PrP)receptor-mediated internalization

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Published on: February 12, 2014

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Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Amyloid beta (Aβ) cellular uptake is linked to toxicity, but mechanisms remain unclear.
Key questions involve Aβ aggregation dependence and sequence specificity in uptake.
Cellular prion protein (PrP^C) is implicated in Aβ toxicity and neuronal internalization.

Purpose of the Study:

To investigate if Aβ uptake is aggregation-dependent and sequence-specific.
To determine the role of PrP^C in stereoselective Aβ internalization.
To identify the molecular interactions between Aβ and PrP^C.

Main Methods:

Utilized a soluble, nonfibrillizing Aβ (1-30) peptide to decouple aggregation from internalization.
Assessed Aβ (1-30) uptake dependence on PrP^C expression.
Employed NMR spectroscopy for molecular-level characterization of Aβ-PrP^C interactions.

Main Results:

Aβ (1-30) peptide demonstrated stereoselective cellular uptake, independent of aggregation.
Aβ (1-30) uptake was dependent on PrP^C expression.
NMR identified the PrP^C docking site for stereoselective Aβ (1-30) binding, revealing a specific recognition sequence.

Conclusions:

Aβ cellular uptake is stereoselective and mediated by specific sequences and receptors like PrP^C.
PrP^C recognizes a specific Aβ sequence, facilitating PrP^C-dependent cellular uptake.
Additional receptor interactions contribute to Aβ internalization; targeting surface receptors is a potential therapeutic strategy for Alzheimer's disease.