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Plasminogen: A cellular protein cofactor for PrPSc propagation.

Charles E Mays1, Chongsuk Ryou

  • 1Department of Microbiology, Immunology and Molecular Genetics, College of Medicine, University of Kentucky, Lexington, KY, USA.

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Plasminogen significantly enhances prion protein (PrP) misfolding and replication, acting as the first identified cellular factor to accelerate PrPSc propagation. This discovery sheds light on prion disease mechanisms.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Prion diseases involve the misfolding and replication of prion protein (PrP) into the pathogenic PrPSc isoform.
  • The mechanism of PrPSc propagation is not fully understood, with evidence suggesting a role for auxiliary factors.
  • Plasminogen has been observed to interact with PrP, but its functional significance in PrPSc propagation was unknown.

Purpose of the Study:

  • To investigate the role of plasminogen in the propagation of prion protein misfolded isoforms (PrPSc).
  • To determine if plasminogen acts as a cellular auxiliary factor in PrPSc generation.

Main Methods:

  • In vitro prion conversion assays were performed to measure PrPSc generation.
  • Plasminogen concentration was varied, and its depletion or structural destabilization was tested.
  • PrP-plasminogen interactions were manipulated.
  • Cell culture models were used to confirm findings.

Main Results:

  • Plasminogen substantially stimulated PrPSc propagation in a concentration-dependent manner.
  • Accelerated PrPSc generation was observed in the presence of plasminogen.
  • Depleting plasminogen, destabilizing its structure, or interfering with its interaction with PrP hindered PrPSc propagation.
  • Increased PrPSc formation was confirmed in cell culture models.

Conclusions:

  • Plasminogen is the first identified cellular protein auxiliary factor proven to stimulate PrPSc propagation.
  • Plasminogen significantly accelerates the rate of PrPSc generation.
  • Further research is needed to elucidate the molecular mechanisms underlying plasminogen's activity in prion propagation.