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Prion protein induced signaling cascades in monocytes

Bjarne Krebs1, Cornelia Dorner-Ciossek, Rüdiger Schmalzbauer

  • 1Center for Neuropathology and Prion Research, Ludwig-Maximilians-University Munich, München, Germany.

Biochemical and Biophysical Research Communications
|December 14, 2005
PubMed

Insights

Cellular prion protein (PrP(C)) fusion proteins attach to and activate signaling pathways in monocyte/macrophages. This study reveals PrP(C) interactions with immune cells, potentially clarifying its physiological role.

Area of Science:

  • Immunology
  • Cell Biology
  • Neuroscience

Background:

  • Prion proteins are central to transmissible spongiform encephalopathies.
  • The physiological function of cellular prion protein (PrP(C)) is not fully understood.
  • PrP(C) is found on cell surfaces, including immune cells like macrophages.

Purpose of the Study:

  • To investigate the interaction between PrP(C) fusion proteins and a mouse monocyte/macrophage cell line.
  • To explore the cellular signaling responses triggered by PrP(C) exposure in these immune cells.

Main Methods:

  • Synthesized PrP(C) fusion proteins with a human Fc-tag.
  • Exposed a mouse monocyte/macrophage cell line to PrP(C) fusion proteins.
  • Analyzed cellular attachment, tyrosine phosphorylation, and downstream signaling pathway activation (ERK1,2 and Akt).

Main Results:

  • PrP(C) fusion proteins attached to monocyte/macrophages at nanomolar concentrations.
  • Attachment led to increased cellular tyrosine phosphorylation, indicating activated signaling.
  • Stimulation with PrP fusion proteins activated downstream pathways, including phosphorylation of ERK(1,2) and Akt kinase.

Conclusions:

  • PrP(C) interacts with and activates signaling pathways in monocytes and macrophages.
  • These findings suggest a role for PrP(C) in immune cell function.
  • Understanding PrP(C) molecular function in monocytes/macrophages is crucial for prion disease research.

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