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Cellular prion protein (PRNP) is a glycoprotein involved in the pathogenesis of transmissible spongiform encephalopathies (TSEs). Although the physiological function of PRNP is largely unknown, its key role in prion infection has been extensively documented. This study examines the functionality of PRNP during the course of embryoid body (EB) differentiation in mouse  Prnp -null (KO) and WT embryonic stem cell (ESC) lines. The first feature observed was a new population of EBs that only appeared in the KO line after 5 days of differentiation. These EBs were characterized by their expression of several primordial germ cell (PGC) markers until Day 13. In a comparative mRNA expression analysis of genes playing an important developmental role during ESC differentiation to EBs,  Prnp  was found to participate in the transcription of a key pluripotency marker such as  Nanog . A clear switching off of this gene on Day 5 was observed in the KO line as opposed to the WT line, in which maximum  Prnp  and  Nanog  mRNA levels appeared at this time. Using a specific antibody against PRNP to block PRNP pathways, reduced  Nanog  expression was confirmed in the WT line. In addition, antibody-mediated inhibition of ITGB5 (integrin αvβ5) in the KO line rescued the low expression of  Nanog  on Day 5, suggesting the regulation of  Nanog  transcription by  Prnp  via this  Itgb5 . mRNA expression analysis of the PRNP-related proteins PRND (Doppel) and SPRN (Shadoo), whose PRNP function is known to be redundant, revealed their incapacity to compensate for the absence of PRNP during early ESC differentiation. Our findings provide strong evidence for a relationship between  Prnp  and several key pluripotency genes and attribute  Prnp  a crucial role in regulating self-renewal/differentiation status of ESC, confirming the participation of PRNP during early embryogenesis.

Prion Protein Expression Regulates Embryonic Stem Cell Pluripotency and Differentiation