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Protein Misfolding Cyclic Amplification of Prions
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Published on: November 7, 2012

Protease-sensitive prions with 144-bp insertion mutations.

Xiangzhu Xiao1, Ignazio Cali, Zhiqian Dong

  • 1Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.

Aging
|March 22, 2013
PubMed
Summary
This summary is machine-generated.

Inherited prion diseases linked to 144-bp insertions may involve abnormal, PK-sensitive prion protein (sPrPSc). This suggests sPrPSc, not just resistant forms, can cause neurotoxicity and prion disease.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Inherited prion diseases are linked to mutations in the prion protein (PrP) gene.
  • A 144-base pair (bp) insertion with six extra octapeptide repeats is associated with these diseases.
  • Previous studies showed detectable proteinase K-resistant PrPSc (rPrPSc) in most cases, but some lacked it.

Purpose of the Study:

  • To investigate the PrP conformer associated with neuropathological changes in inherited prion disease cases lacking detectable rPrPSc.
  • To characterize the abnormal PrP found in a case with a 144-bp insertion but no detectable rPrPSc.

Main Methods:

  • Examination of subjects with 144-bp insertion mutations.
  • Western blotting to detect proteinase K-resistant PrPSc (rPrPSc).
  • Capture of abnormal PrP using gene 5 protein and sodium phosphotungstate, followed by PK-digestion analysis.

Main Results:

  • Most subjects with the 144-bp insertion showed pathognomonic PrP patches.
  • One subject lacked detectable typical rPrPSc.
  • Abnormal PrP captured from this case was predominantly sensitive to PK-digestion (sPrPSc).

Conclusions:

  • The predominant sPrPSc in this case suggests it forms the main component of PrP deposit patches.
  • Absence of rPrPSc indicates that sPrPSc alone may be sufficient to cause neurotoxicity and prion disease.
  • This finding expands understanding of prion protein conformers in inherited prion diseases.