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Related Experiment Video

Updated: May 30, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Prion protein in ESC regulation.

Alberto Miranda¹, Eva Pericuesta, Miguel Ángel Ramírez

¹Departamento de Reproducción Animal y Conservación de Recursos Zoogenéticos, INIA, Madrid, Spain. miranda.alberto@inia.es

|August 5, 2011

Summary

The prion protein (PrP(C)) regulates embryonic stem cell pluripotency and differentiation. Its absence leads to abnormal development, suggesting a role in prion diseases and brain repair.

Area of Science:

Neuroscience
Stem Cell Biology
Prion Biology

Background:

The function of the prion protein (PrP(C)) in mammals remains incompletely understood.
While sequence conservation suggests importance, its precise role, particularly in prion diseases, is not fully established.
Previous research has not identified a definitive, non-redundant function for PrP(C).

Purpose of the Study:

To investigate the non-redundant functions of the prion protein (PrP(C)) in mammalian embryonic stem cells (ESCs).
To explore the role of PrP(C) in regulating pluripotency and early differentiation.
To examine the potential in vivo implications of PrP(C) absence and its link to prion diseases.

Main Methods:

Analysis of PrP(C) function in embryonic stem cells (ESCs).

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Protein Misfolding Cyclic Amplification of Prions

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

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Protein Misfolding Cyclic Amplification of Prions

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Investigation of Nanog mRNA expression regulation by PrP(C).

Comparative study of PrP(C) family members (Doppel, Shadoo) in the absence of PrP(C).

In vitro culture of embryoid bodies (EBs) to assess developmental abnormalities.

Main Results:

PrP(C) was identified as a regulator of Nanog mRNA expression in ESCs, controlling pluripotency and early differentiation.
The absence of PrP(C) resulted in the emergence of a distinct embryoid body (EB) population, indicating developmental defects.
Prion protein family members Doppel and Shadoo could not compensate for the loss of PrP(C) function.
These findings suggest a potential link between PrP(C) loss-of-function and neuronal degeneration observed in prion diseases.

Conclusions:

PrP(C) plays a critical, non-redundant role in maintaining embryonic stem cell pluripotency and regulating early differentiation.
The inability of Doppel and Shadoo to substitute for PrP(C) highlights its unique function.
The observed in vitro developmental abnormalities may mirror in vivo processes, suggesting PrP(C) is crucial for early embryonic development.
A reduction in PrP(C) function, particularly when misfolded into PrP(Sc), could impair brain stem cell pluripotency, hindering recovery from neuronal damage in prion diseases.