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Hugel, B; Martínez, M C; Kunzelmann, C; Blättler, T; Aguzzi, A; Freyssinet, J M (2004). Modulation of signal transduction through the cellular prion protein is linked to its incorporation in lipid rafts. Cellular and Molecular Life Sciences, 61(23):2998-3007.

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Abstract

Because expressed at a significant level at the membrane of human T cells, we made the hypothesis that the cellular prion protein (PrPc) could behave as a receptor, and be responsible for signal transduction. PrPc engagement by specific antibodies was observed to induce an increase in cytosolic calcium concentration and led to enhanced activity of Src protein tyrosine kinases. Antibodies to CD4 and CD59 did not influence calcium fluxes or signaling. The effect was maximal after the formation of a network involving avidin and biotinylated antibody to PrPc and was inhibited after raft disruption. PrPc localization was not restricted to rafts in resting cells but engagement was a prerequisite for signaling induction, with concomitant PrPc recruitment into rafts. These results suggest a role for PrPc in signaling pathways, and show that lateral redistribution of the protein into rafts is important for subsequent signal transduction.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:01 December 2004
Deposited On:11 Feb 2008 13:26
Last Modified:27 Nov 2013 21:57
Publisher:Springer
ISSN:1420-682X
Publisher DOI:10.1007/s00018-004-4318-2
PubMed ID:15583862
Citations:Web of Science®. Times Cited: 31
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