Identification of Glycoinositol Phospholipid Linked and Truncated Forms of the Scrapie Prion Protein

Biochemistry. 1990 Sep 25;29(38):8879-84. doi: 10.1021/bi00490a001.

Abstract

Analysis of carboxy-terminal peptides derived from endoproteinase Lys-C digests of the scrapie isoform of the hamster prion protein revealed that the majority of the molecules are glycoinositol phospholipid linked through ethanolamine attached at serin-231. However, approximately 15% of PrPSc had a carboxy-terminal peptide that ends at glycine-228. It is intriguing that this glycine is part of the PrP sequence Gly-Arg-Arg, which is an established target sequence for the proteolysis and release of bioactive peptides from larger precursors. The mechanism of formation, as well as the role of the truncated carboxy terminus in the dissemination and neuropathology of scrapie, remains to be determined.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain Chemistry
  • Chromatography, High Pressure Liquid
  • Cricetinae
  • Endopeptidases
  • Ethanolamines / metabolism
  • Glycolipids / chemistry*
  • Glycolipids / metabolism
  • Glycosylphosphatidylinositols
  • Hydrolysis
  • Molecular Sequence Data
  • Phosphatidylinositols / chemistry*
  • Phosphatidylinositols / metabolism
  • PrPSc Proteins
  • Prions / analysis
  • Scrapie / diagnosis
  • Viral Proteins / chemistry*
  • Viral Proteins / metabolism

Substances

  • Ethanolamines
  • Glycolipids
  • Glycosylphosphatidylinositols
  • Phosphatidylinositols
  • PrPSc Proteins
  • Prions
  • Viral Proteins
  • Endopeptidases