Ricerc@Sapienza

Cellular prion protein (PrPC) is expressed in a wide variety of stem cells in which regulates their self-renewal as well as differentiation potential. In this study we investigated the presence of PrPCin human dental pulp-derived stem cells (hDPSCs) and its role in neuronal differentiation process. We show that hDPSCs expresses early PrPCat low concentration and its expression increases after two weeks of treatment with EGF/bFGF. Then, we analyzed the association of PrPCwith gangliosides and EGF receptor (EGF-R) during neuronal differentiation process.

Bioethical issues related to the manipulation of embryonic stem cells have hindered advances in the field of medical research. For this reason, it is very important to obtain adult stem cells from different tissues such as adipose, umbilical cord, bone marrow and blood. Among the possible sources, dental pulp is particularly interesting because it is easy to obtain in respect of bioethical considerations.

Aims. Prion protein (PrPC), like many GPI-anchored protein, is found in sphingolipid-rich membrane microdomains known as lipid raft. This membrane-bound isoform dimerizes and can act as cell surface receptor, co-receptor or form multimolecular complexes and recruit downstream signal transduction pathways. As known, dimerization of membrane-bound PrPC leads to clustering in multimolecular complexes and serves to regulate different aspect of neuronal homeostasis, while intracellular dimerization appears to be the most relevant event in neuroprotection, via N1 and C1 prion metabolites.

Prion protein (PrPC) localizes stably in lipid rafts microdomains and is able to recruit downstream signal transduction pathways by the interaction with promiscuous partners. Other proteins have the ability to occasionally be recruited to these specialized membrane areas, within multimolecular complexes.