Modulation of L-type voltage-gated calcium channels by recombinant prion protein

2003 | journal article. A publication with affiliation to the University of Göttingen.

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​Modulation of L-type voltage-gated calcium channels by recombinant prion protein​
Korte, S.; Vassallo, N.; Kramer, M. L.; Kretzschmar, H. A. & Herms, J.​ (2003) 
Journal of Neurochemistry87(4) pp. 1037​-1042​.​ DOI: https://doi.org/10.1046/j.1471-4159.2003.02080.x 

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Authors
Korte, S.; Vassallo, N.; Kramer, Michael L.; Kretzschmar, Hans A.; Herms, J.
Abstract
The prion protein (PrPC) has a primary role in the pathogenesis of transmissible spongiform encephalopathies. Here we analysed in detail the effect of recombinant PrPC and N- and C-terminal fragments of PrPC on the whole-cell current amplitude through voltage-gated calcium channels (VGCCs) of cultured wild-type cerebellar granule cells. With the application of full-length recombinant PrPC (50-500 nm), a highly significant reduction of the whole-cell current amplitude was observed in a dose-dependent manner. Amplitude reduction was abolished when cells were pre-incubated with nifedipine, a specific blocker of voltage-gated L-type calcium channels. N-terminal PrP fragments also led to a dose-dependent reduction of the maximal current amplitude, whereas a C-terminal fragment did not affect the current amplitude. These data demonstrate that nanomolar concentrations of PrPC modulate L-type VGCCs in mouse cerebellar granule cells, an effect that is dependent upon the copper-binding amino-terminal domain of PrPC.
Issue Date
2003
Status
published
Publisher
Blackwell Publishing Ltd
Journal
Journal of Neurochemistry 
ISSN
0022-3042

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