ArticlePloS one2014
The cellular prion protein negatively regulates phagocytosis and cytokine expression in murine bone marrow-derived macrophages.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- A Function of Amyloid-β in Mediating Activity-Dependent Axon/Synapse Competition May Unify Its Roles in Brain Physiology and Pathology.Journal of Alzheimer's disease : JAD · 2023Review
- The multiple functions of PrPJournal of molecular medicine (Berlin, Germany) · 2022Review
- Cellular Prion Protein Expression in the Brain Tissue fromAnimals : an open access journal from MDPI · 2022Article
- Microglia in Prion Diseases: Angels or Demons?International journal of molecular sciences · 2020Review
- Hematological shift in goat kids naturally devoid of prion protein.Frontiers in cell and developmental biology · 2015Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular prion protein (PrP(C)) is a glycosylphosphatidylinositol (GPI)-anchored glycoprotein on the cell surface. Previous studies have demonstrated contradictory roles for PrP(C) in connection with the phagocytic ability of macrophages. In the present work, we investigated the function of PrP(C) in phagocytosis and cytokine expression in bone marrow-derived macrophages infected with Escherichia coli. E. coli infection induced an increase in the PRNP mRNA level. Knockout of PrP(C) promoted bacterial uptake; upregulated Rab5, Rab7, and Eea1 mRNA expression; and increased the recruitment of lysosomal-associated membrane protein-2 to phagosomes, suggesting enhanced microbicidal activity. Remarkably, knockout of PrP(C) suppressed the proliferation of internalized bacteria and increased the expression of cytokines such as interleukin-1β. Collectively, our data reveal an important role of PrP(C) as a negative regulator for phagocytosis, phagosome maturation, cytokine expression, and macrophage microbicidal activity.
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Registered trials
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