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Updated: Feb 9, 2026

Detection of Abnormal Prion Protein by Immunohistochemistry
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The cellular and pathologic prion protein.

Andrew C Gill1, Andrew R Castle2

  • 1School of Chemistry, Joseph Banks Laboratories, University of Lincoln, Lincoln, United Kingdom; Division of Neurobiology, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, University of Edinburgh, Edinburgh, United Kingdom.

Handbook of Clinical Neurology
|June 12, 2018
PubMed
Summary
This summary is machine-generated.

The cellular prion protein (PrPC) misfolds into PrPTSE, causing neurodegenerative prion diseases. Understanding this misfolding is key to prion disease research and potential treatments.

Keywords:
PRNPamyloidcofactorsconformational conversionglycosylationmembrane anchormisfoldingprion functionprion proteintoxicity

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Area of Science:

  • Neurobiology
  • Biochemistry
  • Molecular Biology

Background:

  • The cellular prion protein (PrPC) is a cell surface glycoprotein with an undefined function.
  • PrPC is implicated in transmissible spongiform encephalopathies (prion diseases).
  • PrPC misfolding to PrPTSE is central to prion disease pathogenesis.

Purpose of the Study:

  • To review the current knowledge of prion protein biochemistry.
  • To explore the structure, function, and dysfunction of PrPC and PrPTSE.
  • To understand the mechanisms of PrPC to PrPTSE interconversion.

Main Methods:

  • Literature review of prion protein research.
  • Analysis of biochemical and biophysical properties of PrPC and PrPTSE.
  • Examination of prion protein misfolding and dysfunction.

Main Results:

  • PrPTSE formation is the primary molecular event in prion disease pathogenesis.
  • PrPTSE is considered the infectious agent (prion) responsible for disease transmission.
  • Misfolding precedes clinical and pathological manifestations like neuronal loss.

Conclusions:

  • Understanding PrPC and PrPTSE biochemistry is crucial for prion disease biology.
  • Further research into the interconversion mechanisms is critical.
  • Knowledge of prion protein structure and function informs disease understanding.