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Journal Article

Characterization of prion protein function by focal neurite stimulation.

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D'Este,  E.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Amin, L., Nguyen, X. T. A., Rolle, I. G., D'Este, E., Giachin, G., Tran, T. H., et al. (2016). Characterization of prion protein function by focal neurite stimulation. Journal of Cell Science, 129(20), 3878-3891. doi:10.1242/jcs.183137.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-3183-4
Abstract
The cellular prion protein (PrPC), encoded by the PRNP gene, is a ubiquitous glycoprotein, which is highly expressed in the brain. This protein, mainly known for its role in neurodegenerative diseases, is involved in several physiological processes including neurite outgrowth. By using a novel focal stimulation technique, we explored the potential function of PrPC, in its soluble form, as a signaling molecule. Thus, soluble recombinant prion proteins (recPrP) encapsulated in micro-vesicles were released by photolysis near the hippocampal growth cones. Local stimulation of wild-type growth cones with full-length recPrP induced neurite outgrowth and rapid growth cone turning towards the source. This effect was shown to be concentration dependent. Notably, PrPC-knockout growth cones were insensitive to recPrP stimulation, but this property was rescued in PrP-knockout growth cones expressing GFP-PrP. Taken together, our findings indicate that recPrP functions as a signaling molecule, and that its homophilic interaction with membrane-anchored PrPC might promote neurite outgrowth and facilitate growth cone guidance.