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Related Experiment Video

Updated: Jul 23, 2026

Preparation of Synaptoneurosomes from Mouse Cortex using a Discontinuous Percoll-Sucrose Density Gradient

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Function of PrP(C) as a copper-binding protein at the synapse.

H A Kretzschmar¹, T Tings, A Madlung

¹Institute of Neuropathology, University of Göttingen, Germany.

Archives of Virology. Supplementum

|February 24, 2001

Summary

The prion protein (PrP(C)) binds copper and is concentrated in synapses. Its absence in mice significantly reduces synaptic copper, suggesting a role in copper regulation.

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Area of Science:

Neuroscience
Biochemistry
Prion Biology

Background:

The prion protein (PrP(C)) possesses an N-terminal octarepeat region with cooperative copper binding capabilities.
PrP(C) is predominantly localized in synaptosomal fractions within brain homogenates.

Purpose of the Study:

To investigate the role of PrP(C) in synaptic copper homeostasis.
To determine the impact of PrP(C) deficiency on copper concentrations in neuronal synapses.

Main Methods:

Comparative analysis of synaptic copper concentrations in wild-type and PrP(C)-deficient (Prnp0/0) mice.
Biochemical fractionation of brain homogenates to isolate synaptosomal components.

Main Results:

Synaptosomal copper concentrations were found to be reduced by approximately 50% in Prnp0/0 mice compared to normal mice.
This indicates a significant role for PrP(C) in maintaining copper levels at the synapse.

Conclusions:

PrP(C) may function as a copper buffer within the synaptic cleft.
PrP(C) might be involved in presynaptic copper re-uptake or play a structural role influencing protein interactions.