Abstract
The biological function of the Prion protein remains largely unknown but recent data revealed its implication in early zebrafish and mammalian embryogenesis. To gain further insight into its biological function, comparative transcriptomic analysis between FVB/N and FVB/N Prnp knockout mice was performed at early embryonic stages. RNAseq analysis revealed the differential expression of 73 and 263 genes at E6.5 and E7.5, respectively. The related metabolic pathways identified in this analysis partially overlap with those described in PrP1 and PrP2 knockdown zebrafish embryos and prion-infected mammalian brains and emphasize a potentially important role for the PrP family genes in early developmental processes.
Highlights
The Prion protein, PrP, has been the focus of intensive research for decades due to its pivotal role in transmissible spongiform encephalopathies, a group of infectious neurodegenerative diseases of animal and human characterized by the accumulation of a pathological form of the protein (PrPSc) [1,2,3]
Even the sub-cellular localization of this glycosyl-phosphatidyl-inositolanchored cell surface glycoprotein remains a subject of debate leading to yet other purported physiological processes involving PrP ([8] for exemple)
It has been hypothesized that another host-encoded protein is able to compensate for the lack of PrP [15] or, if not redundant, that PrP has no physiological function [16]
Summary
The Prion protein, PrP, has been the focus of intensive research for decades due to its pivotal role in transmissible spongiform encephalopathies, a group of infectious neurodegenerative diseases of animal and human characterized by the accumulation of a pathological form of the protein (PrPSc) [1,2,3]. Cellular homeostasis, response to oxidative stress, cell proliferation and differentiation, synaptic function and signal transduction have been proposed [4,5,6,7]. The difficulty to define a role for this protein partially comes from the observation that Prnp-knockout mice [9,10], cattle [11] and goat [12] suffer from no drastic developmental phenotype. Invalidation of this gene in adult mouse neurons does not affect the overall health of the mice [13,14]. It has been hypothesized that another host-encoded protein is able to compensate for the lack of PrP [15] or, if not redundant, that PrP has no physiological function [16]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
