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129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal.

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TLDR
The use of a different targeting strategy is reported, to produce inbred mice with a complete absence of both PrP protein and mRNA sequences, which are being used in experiments designed to address the role of PrP in the pathogenesis of scrapie and the replication of infectivity.
Abstract
The neural membrane glycoprotein PrP is implicated in the pathogenesis of the transmissible spongiform encephalopathies; however, the normal function of PrP and its precise role in disease are not understood. Recently, gene targeting has been used to produce mice withneo/PrP fusion transcripts, but no detectable PrP protein in the brain (1). Here we report the use of a different targeting strategy, to produce inbred mice with a complete absence of both PrP protein and mRNA sequences. At 7 mo of age, these mice show no overt phenotypic abnormalities despite the normal high levels of expression of PrP during mouse development. The mice are being used in experiments designed to address the role of PrP in the pathogenesis of scrapie and the replication of infectivity.

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Contributions of neuronal prion protein on sleep recovery and stress response following sleep deprivation

TL;DR: Findings demonstrate that neuronal, but not non-neuronal, PrP(C) is involved in sleep homeostasis and sleep continuity and suggest that neuronalPrP(c)-dependent hormonal regulation of HPA axis may contribute to the sleep homestasis.
Journal ArticleDOI

Neuroimmunoendocrine regulation of the prion protein in neutrophils

TL;DR: The data demonstrate a novel interplay of the nervous, endocrine, and immune systems upon both the expression and function of PrPC in neutrophils, which may have a broad impact upon the physiology and pathology of various organs and systems.
Journal ArticleDOI

A role of cellular prion protein in programming T-cell cytokine responses in disease

TL;DR: It is shown here that Prnp mRNA is highly inducible within 8‐24 h of T‐cell activation, with surface protein levels rising from 24 h, consistent with its up‐regulation being a late activation event, and PrP deletion did not alter T‐ cell‐antigen presenting cell conjugate formation.
Journal ArticleDOI

Is, indeed, the prion protein a Harlequin servant of "many" masters?

TL;DR: The validity of past and more recent literature supporting that, as part of protein platforms at the cell surface, PrPC may bridge extracellular matrix molecules and membrane proteins to intracellular signaling pathways is discussed.
Journal ArticleDOI

Prion protein is required for tumor necrosis factor α (TNFα)-triggered nuclear factor κB (NF-κB) signaling and cytokine production

TL;DR: PrP enhances the responses to TNFα, promoting proinflammatory cytokine production, which may contribute to inflammation and tumorigenesis, and concludes that PrP traps CYLD, preventing it from binding and deubiquitinating RIP1 and TRAF2.
References
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Journal ArticleDOI

Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction

TL;DR: A new method of total RNA isolation by a single extraction with an acid guanidinium thiocyanate-phenol-chloroform mixture is described, providing a pure preparation of undegraded RNA in high yield and can be completed within 4 h.
Journal ArticleDOI

Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours

TL;DR: Observations indicate that a normal p53 gene is dispensable for embryonic development, that its absence predisposes the animal to neoplastic disease, and that an oncogenic mutant form of p53 is not obligatory for the genesis of many types of tumours.
Journal ArticleDOI

Site-directed mutagenesis by gene targeting in mouse embryo-derived stem cells.

TL;DR: This work mutated, by gene targeting, the endogenous hypoxanthine phosphoribosyl transferase (HPRT) gene in mouse embryo-derived stem (ES) cells and compared the gene-targeting efficiencies of two classes of neor-Hprt recombinant vectors.
Journal ArticleDOI

Multiple intestinal neoplasia caused by a mutation in the murine homolog of the APC gene.

TL;DR: In this paper, a mouse lineage that exhibits an autosomal dominantly inherited predisposition to multiple intestinal neoplasia (Min) was described and linkage analysis showed that the murine homolog of the APC gene (mApc) was tightly linked to the Min locus.
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