The prion protein contributes to epithelial-to-mesenchymal transition in the mouse NMuMG epithelial cell model

ABSTRACT: The physiological function of the prion protein (PrP) has remained elusive despite its widely recognized role in neurodegenerative diseases and sustained efforts to understand its molecular biology. On the basis of its evolutionary relationship to ZIP zinc transporters, protein-protein interactions it engages in, and the characteristics of a gastrulation arrest phenotype in a PrP-deficient model, we considered that PrP may contribute to the morphogenetic reprogramming of cells underlying epithelial-to-mesenchymal (EMT) transitions. We have conducted three global proteomics analyses to (1) identify proteins whose levels are changed during EMT in wild-type NMuMG cells; and determine proteins whose levels are affected by (2) stable knockdown or (3) transient knockdown of the prion protein relative to levels observed in wild-type NMuMG cells. We observed a highly significant correlation between proteins, which are changed during EMT or following PrP knockdown.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Gerold Schmitt-Ulms  

LAB HEAD: Gerold Schmitt-Ulms

PROVIDER: PXD001875 | Pride | 2015-07-10

REPOSITORIES: Pride