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Journal Article

Characterization of prion protein function by focal neurite stimulation.


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

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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
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.