Author: Giese Armin Buchholz Malte Herms Jochen Kretzschmar Hans
Publisher: Humana Press, Inc
ISSN: 0895-8696
Source: Journal of Molecular Neuroscience, Vol.27, Iss.3, 2005-10, pp. : 347-354
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Abstract
The prion protein (PrPC) is a copper-binding, cell-surface protein that plays an essential role in the etiology of transmissible spongiform encephalopathies. Atomic absorption spectroscopy studies have established that synaptosomal copper content is reduced in PrPC-deficient mice as compared with wild-type (WT) or PrP-overexpressing mice. To address the question of whether this is the result of a loss of function of PrPC in copper transport across the plasma membrane at the synapse, we have used synaptosomes incubated with 67Cu as a model system to characterize the mechanism of copper accumulation in nerve terminals. Our results demonstrate that mouse brain synaptosomes accumulate copper efficiently by at least two distinct mechanisms. In the presence of 1 m
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